INCORPORATION BY REFERENCE OF MATERIAL ON COMPACT DISK
This application incorporates by reference the Sequence Listing contained on the two compact disks (Copy 1 and Copy 2), filed concurrently herewith, containing the following file:
- File name: 3687.1000-023SequenceList.txt; created Dec. 27, 2004, 8,134 KB in size.
This application also incorporates by reference Table 2 contained on the two compact disks (Copy 1 and Copy 2), filed concurrently herewith, containing the following file:
File name: 521614—1.txt; created Dec. 23, 2004, 351 KB in size.
TABLES FILED ON CD
The patent application contains tables filed on compact disc. These tables have been included at the end of the specification
FIELD OF THE INVENTION
The invention relates to isolated nucleic acids and polypeptides derived from Streptococcus pneumoniae that are useful as molecular targets for diagnostics, prophylaxis and treatment of pathological conditions, as well as materials and methods for the diagnosis, prevention, and amelioration of pathological conditions resulting from bacterial infection.
BACKGROUND OF THE INVENTION
Streptococcus pneumoniae (S. pneumoniae) is a common, spherical, gram-positive bacterium. Worldwide it is a leading cause of illness among children, the elderly, and individuals with debilitating medical conditions (Breiman, R. F. et al., 1994, JAMA 271: 1831). S. pneumoniae is estimated to be the causal agent in 3,000 cases of meningitis, 50,000 cases of bacteremia, 500,000 cases of pneumonia, and 7,000,000 cases of otitis media annually in the United States alone (Reichler, M. R. et al., 1992, J. Infect. Dis. 166: 1346; Stool, S. E. and Field, M. J., 1989 Pediatr. Infect. Dis J. 8: S11). In the United States alone, 40,000 deaths result annually from S. pneumoniae infections (Williams, W. W. et al., 1988 Ann. Intern. Med. 108: 616) with a death rate approaching 30% from bacteremia (Butler, J. C. et al., 1993, JAMA 270: 1826). Pneumococcal pneumonia is a serious problem among the elderly of industrialized nations (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis. 2: 289) and is a leading cause of death among children in developing nations (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis. 2: 289; Stansfield, S. K., 1987 Pediatr. Infect. Dis. 6: 622).
Vaccines against S. pneumoniae have been available for a number of years. There are a large number of serotypes based on the polysaccharide capsule (van Dam, J. E., Fleer, A., and Snippe, H., 1990 Antonie van Leeuwenhoek 58: 1) although only a fraction of the serotypes seem to be associated with infections (Martin, D. R. and Brett, M. S., 1996 N. Z. Med. J. 109: 288). A multivalent vaccine against capsular polysaccharides of 23 serotypes (Smart, L. E., Dougall, A. J. and Gridwood, R. W., 1987 J. Infect. 14: 209) has provided protection for some groups but not for several groups at risk for pneumococcal infections, such as infants and the elderly (Makel, P. H. et al., 1980 Lancet 2: 547; Sankilampi, U., 1996 J. Infect. Dis. 173: 387). Conjugated pneumococcal capsular polysaccharide vaccines have somewhat improved efficacy, but are costly and, therefore, are not likely to be in widespread use (Käyhty, H. and Eskola, J., 1996 Emerg. Infect. Dis. 2: 289).
At one time, S. pneumoniae strains were uniformly susceptible to penicillin. The report of a penicillin-resistant strain of (Hansman, D. and Bullen, M. M., 1967 Lancet 1: 264) was followed rapidly by many reports indicating the worldwide emergence of penicillin-resistant and penicillin non-susceptible strains (Klugman, K. P., 1990 Clin. Microbiol. Rev. 3: 171). S. pneumoniae strains which are resistant to multiple antibiotics (including penicillin) have also been observed recently within the United States (Welby, P. L., 1994 Pediatr. Infect. Dis. J. 13: 281; Ducin, J. S. et al., 1995 Pediatr. Infect. Dis. J. 14: 745; Butler, J. C., 1996 J. Infect. Dis. 174: 986) as well as internationally (Boswell, T. C. et al., 1996; J. Infect. 33: 17; Catchpole, C., Fraise, A., and Wise, R., 1996 Microb. Drug Resist. 2: 431; Tarasi, A. et al., 1997 Microb. Drug Resist. 3: 105).
A high incidence of morbidity is associated with invasive S. pneumoniae infections (Williams, W. W. et al., 1988 Ann. Intern. Med. 108: 616). Because of the incomplete effectiveness of currently available vaccines and antibiotics, the identification of new targets for antimicrobial therapies, including, but not limited to, the design of vaccines and antibiotics, which may help prevent infection or that may be useful in fighting existing infections, is highly desirable.
SUMMARY OF THE INVENTION
The present invention fulfills the need for diagnostic tools and therapeutics by providing bacterial-specific compositions and methods for detecting, treating, and preventing bacterial infection, in particular S. pneumoniae infection.
The present invention encompasses isolated polypeptides and nucleic acids derived from S. pneumoniae that are useful as reagents for diagnosis of bacterial infection, components of effective antibacterial vaccines, and/or as targets for antibacterial drugs, including anti-S. pneumoniae drugs. The nucleic acids and peptides of the present invention also have utility for diagnostics and therapeutics for S. pneumoniae and other Streptococcus species. They can also be used to detect the presence of S. pneumoniae and other Streptococcus species in a sample; and in screening compounds for the ability to interfere with the S. pneumoniae life cycle or to inhibit S. pneumoniae infection. More specifically, this invention features compositions of nucleic acids corresponding to entire coding sequences of S. pneumoniae proteins, including surface or secreted proteins or parts thereof, nucleic acids capable of binding mRNA from S. pneumoniae proteins to block protein translation, and methods for producing S. pneumoniae proteins or parts thereof using peptide synthesis and recombinant DNA techniques. This invention also features antibodies and nucleic acids useful as probes to detect S. pneumoniae infection. In addition, vaccine compositions and methods for the protection or treatment of infection by S. pneumoniae are within the scope of this invention.
The nucleotide sequences provided in SEQ ID NO: 1-SEQ ID NO: 2661, a fragment thereof, or a nucleotide sequence at least 99.5% identical to a sequence contained within SEQ ID NO: 1-SEQ ID NO: 2661 may be “provided” in a variety of medias to facilitate use thereof. As used herein, “provided” refers to a manufacture, other than an isolated nucleic acid molecule, which contains a nucleotide sequence of the present invention, i.e., the nucleotide sequence provided in SEQ ID NO: 1-SEQ ID NO: 2661, a fragment thereof, or a nucleotide sequence at least 99.5% identical to a sequence contained within SEQ ID NO: 1-SEQ ID NO: 2661. Uses for and methods for providing nucleotide sequences in a variety of media is well known in the art (see e.g., EPO Publication No. EP 0 756 006).
In one application of this embodiment, a nucleotide sequence of the present invention can be recorded on computer readable media. As used herein, “computer readable media” refers to any media which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media, such as floppy discs, hard disc storage media, and magnetic tape; optical storage media such as CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media. A person skilled in the art can readily appreciate how any of the presently known computer readable media can be used to create a manufacture comprising computer readable media having recorded thereon a nucleotide sequence of the present invention.
As used herein, “recorded” refers to a process for storing information on computer readable media. A person skilled in the art can readily adopt any of the presently known methods for recording information on computer readable media to generate manufactures comprising the nucleotide sequence information of the present invention.
A variety of data storage structures are available to a person skilled in the art for creating a computer readable media having recorded thereon a nucleotide sequence of the present invention. The choice of the data storage structure will generally be based on the means chosen to access the stored information. In addition, a variety of data processor programs and formats can be used to store the nucleotide sequence information of the present invention on computer readable media. The sequence information can be represented in a word processing text file, formatted in commercially-available software such as WordPerfect and Microsoft Word, or represented in the form of an ASCII file, stored in a database application, such as DB2, Sybase, Oracle, or the like. A person skilled in the art can readily adapt any number of data processor structuring formats (e.g. text file or database) in order to obtain computer readable media having recorded thereon the nucleotide sequence information of the present invention.
By providing the nucleotide sequence of SEQ ID NO: 1-SEQ ID NO: 2661, a fragment thereof, or a nucleotide sequence at least 99.5% identical to a sequence contained within SEQ ID NO: 1-SEQ ID NO: 2661 in computer readable form, a person skilled in the art can routinely access the sequence information for a variety of purposes. Computer software is publicly available which allows a person skilled in the art to access sequence information provided in a computer readable media. Examples of such computer software include programs of the “Staden Package”, “DNA Star”, “MacVector”, GCG “Wisconsin Package” (Genetics Computer Group, Madison, Wis.) and “NCBI toolbox” (National Center for Biotechnology Information).
Computer algorithms enable the identification of S. pneumoniae open reading frames (ORFs) within SEQ ID NO: 1-SEQ ID NO: 2661 which contain homology to ORFs or proteins from other organisms. Examples of such similarity-search algorithms include the BLAST [Altschul et al., J. Mol. Biol. 215: 403-410 (1990)] and Smith-Waterman [Smith and Waterman (1981) Advances in Applied Mathematics, 2: 482-489] search algorithms. These algorithms are utilized on computer systems as exemplified below. The ORFs so identified represent protein encoding fragments within the S. pneumoniae genome and are useful in producing commercially important proteins such as enzymes used in fermentation reactions and in the production of commercially useful metabolites.
The present invention further provides systems, particularly computer-based systems, which contain the sequence information described herein. Such systems are designed to identify commercially important fragments of the S. pneumoniae genome. As used herein, “a computer-based system” refers to the hardware means, software means, and data storage means used to analyze the nucleotide sequence information of the present invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means, and data storage means. A person skilled in the art can readily appreciate that any one of the currently available computer-based systems is suitable for use in the present invention. The computer-based systems of the present invention comprise a data storage means having stored therein a nucleotide sequence of the present invention and the necessary hardware means and software means for supporting and implementing a search means. As used herein, “data storage means” refers to memory which can store nucleotide sequence information of the present invention, or a memory access means which can access manufactures having recorded thereon the nucleotide sequence information of the present invention.
As used herein, “search means” refers to one or more programs which are implemented on the computer-based system to compare a target sequence or target structural motif with the sequence information stored within the data storage means. Search means are used to identify fragments or regions of the S. pneumoniae genome which are similar to, or “match”, a particular target sequence or target motif. A variety of known algorithms are known in the art and have been disclosed publicly, and a variety of commercially available software for conducting homology-based similarity searches are available and can be used in the computer-based systems of the present invention. Examples of such software include, but is not limited to, FASTA (GCG Wisconsin Package), Bic_SW (Compugen Bioccelerator, BLASTN2, BLASTP2 and BLASTX2 (NCBI) and Motifs (GCG). BLASTN2, A person skilled in the art can readily recognize that any one of the available algorithms or implementing software packages for conducting homology searches can be adapted for use in the present computer-based systems.
As used herein, a “target sequence” can be any DNA or amino acid sequence of six or more nucleotides or two or more amino acids. A person skilled in the art can readily recognize that the longer a target sequence is, the less likely a target sequence will be present as a random occurrence in the database. The most preferred sequence length of a target sequence is from about 10 to 100 amino acids or from about 30 to 300 nucleotide residues. However, it is well recognized that many genes are longer than 500 amino acids, or 1.5 kb in length, and that commercially important fragments of the S. pneumoniae genome, such as sequence fragments involved in gene expression and protein processing, will often be shorter than 30 nucleotides.
As used herein, “a target structural motif,” or “target motif,” refers to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a specific functional domain or three-dimensional configuration which is formed upon the folding of the target polypeptide. There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzymatic active sites, membrane spanning regions, and signal sequences. Nucleic acid target motifs include, but are not limited to, promoter sequences, hairpin structures and inducible expression elements (protein binding sequences).
A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the present invention. A preferred format for an output means ranks fragments of the S. pneumoniae genome possessing varying degrees of homology to the target sequence or target motif. Such presentation provides a person skilled in the art with a ranking of sequences which contain various amounts of the target sequence or target motif and identifies the degree of homology contained in the identified fragment.
A variety of comparing means can be used to compare a target sequence or target motif with the data storage means to identify sequence fragments of the S. pneumoniae genome. In the present examples, implementing software which implement the BLASTP2 and bic_SW algorithms (Altschul et al., J. Mol. Biol. 215: 403-410 (1990); Compugen Biocellerator) was used to identify open reading frames within the S. pneumoniae genome. A person skilled in the art can readily recognize that any one of the publicly available homology search programs can be used as the search means for the computer-based systems of the present invention.
The invention features S. pneumoniae polypeptides, preferably a substantially pure preparation of an S. pneumoniae polypeptide, or a recombinant S. pneumoniae polypeptide. In preferred embodiments: the polypeptide has biological activity; the polypeptide has an amino acid sequence at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% identical to an amino acid sequence of the invention contained in the Sequence Listing, preferably it has about 65% sequence identity with an amino acid sequence of the invention contained in the Sequence Listing, and most preferably it has about 92% to about 99% sequence identity with an amino acid sequence of the invention contained in the Sequence Listing; the polypeptide has an amino acid sequence essentially the same as an amino acid sequence of the invention contained in the Sequence Listing; the polypeptide is at least 5, 10, 20, 50, 100, or 150 amino acid residues in length; the polypeptide includes at least 5, preferably at least 10, more preferably at least 20, more preferably at least 50, 100, or 150 contiguous amino acid residues of the invention contained in the Sequence Listing. In yet another preferred embodiment, the amino acid sequence which differs in sequence identity by about 7% to about 8% from the S. pneumoniae amino acid sequences of the invention contained in the Sequence Listing is also encompassed by the invention.
In preferred embodiments: the S. pneumoniae polypeptide is encoded by a nucleic acid of the invention contained in the Sequence Listing, or by a nucleic acid having at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% homology with a nucleic acid of the invention contained in the Sequence Listing.
In a preferred embodiment, the subject S. pneumoniae polypeptide differs in amino acid sequence at 1, 2, 3, 5, 10 or more residues from a sequence of the invention contained in the Sequence Listing. The differences, however, are such that the S. pneumoniae polypeptide exhibits an S. pneumoniae biological activity, e.g., the S. pneumoniae polypeptide retains a biological activity of a naturally occurring S. pneumoniae enzyme.
In preferred embodiments, the polypeptide includes all or a fragment of an amino acid sequence of the invention contained in the Sequence Listing; fused, in reading frame, to additional amino acid residues, preferably to residues encoded by genomic DNA 5′ or 3′ to the genomic DNA which encodes a sequence of the invention contained in the Sequence Listing.
In yet other preferred embodiments, the S. pneumoniae polypeptide is a recombinant fusion protein having a first S. pneumoniae polypeptide portion and a second polypeptide portion, e.g., a second polypeptide portion having an amino acid sequence unrelated to S. pneumoniae. The second polypeptide portion can be, e.g., any of glutathione-S-transferase, a DNA binding domain, or a polymerase activating domain. In preferred embodiment the fusion protein can be used in a two-hybrid assay.
Polypeptides of the invention include those which arise as a result of alternative transcription events, alternative RNA splicing events, and alternative translational and postranslational events.
In a preferred embodiment, the encoded S. pneumoniae polypeptide differs (e.g., by amino acid substitution, addition or deletion of at least one amino acid residue) in amino acid sequence at 1, 2, 3, 5, 10 or more residues, from a sequence of the invention contained in the Sequence Listing. The differences, however, are such that: the S. pneumoniae encoded polypeptide exhibits a S. pneumoniae biological activity, e.g., the encoded S. pneumoniae enzyme retains a biological activity of a naturally occurring S. pneumoniae.
In preferred embodiments, the encoded polypeptide includes all or a fragment of an amino acid sequence of the invention contained in the Sequence Listing; fused, in reading frame, to additional amino acid residues, preferably to residues encoded by genomic DNA 5′ or 3′ to the genomic DNA which encodes a sequence of the invention contained in the Sequence Listing.
The S. pneumoniae strain, 14453, from which genomic sequences have been sequenced, has been deposited on Jun. 26, 1997 in the American Type Culture Collection and assigned the ATCC designation # 55987.
Included in the invention are: allelic variations; natural mutants; induced mutants; proteins encoded by DNA that hybridize under high or low stringency conditions to a nucleic acid which encodes a polypeptide of the invention contained in the Sequence Listing (for definitions of high and low stringency see Current Protocols in Molecular Biology, John Wiley & Sons, New York, 1989, 6.3.1-6.3.6, hereby incorporated by reference); and, polypeptides specifically bound by antisera to S. pneumoniae polypeptides, especially by antisera to an active site or binding domain of S. pneumoniae polypeptide. The invention also includes fragments, preferably biologically active fragments. These and other polypeptides are also referred to herein as S. pneumoniae polypeptide analogs or variants.
The invention further provides nucleic acids, e.g., RNA or DNA, encoding a polypeptide of the invention. This includes double stranded nucleic acids as well as coding and antisense single strands.
In preferred embodiments, the subject S. pneumoniae nucleic acid will include a transcriptional regulatory sequence, e.g. at least one of a transcriptional promoter or transcriptional enhancer sequence, operably linked to the S. pneumoniae gene sequence, e.g., to render the S. pneumoniae gene sequence suitable for expression in a recombinant host cell.
In yet a further preferred embodiment, the nucleic acid which encodes an S. pneumoniae polypeptide of the invention, hybridizes under stringent conditions to a nucleic acid probe corresponding to at least 8 consecutive nucleotides of the invention contained in the Sequence Listing; more preferably to at least 12 consecutive nucleotides of the invention contained in the Sequence Listing; more preferably to at least 20 consecutive nucleotides of the invention contained in the Sequence Listing; more preferably to at least 40 consecutive nucleotides of the invention contained in the Sequence Listing.
In another aspect, the invention provides a substantially pure nucleic acid having a nucleotide sequence which encodes an S. pneumoniae polypeptide. In preferred embodiments: the encoded polypeptide has biological activity; the encoded polypeptide has an amino acid sequence at least 60%, 70%, 80%, 90%, 95%, 98%, or 99% homologous to an amino acid sequence of the invention contained in the Sequence Listing; the encoded polypeptide has an amino acid sequence essentially the same as an amino acid sequence of the invention contained in the Sequence Listing; the encoded polypeptide is at least 5, 10, 20, 50, 100, or 150 amino acids in length; the encoded polypeptide comprises at least 5, preferably at least 10, more preferably at least 20, more preferably at least 50, 100, or 150 contiguous amino acids of the invention contained in the Sequence Listing.
In another aspect, the invention encompasses: a vector including a nucleic acid which encodes an S. pneumoniae polypeptide or an S. pneumoniae polypeptide variant as described herein; a host cell transfected with the vector; and a method of producing a recombinant S. pneumoniae polypeptide or S. pneumoniae polypeptide variant; including culturing the cell, e.g., in a cell culture medium, and isolating an S. pneumoniae polypeptide or an S. pneumoniae polypeptide variant, e.g., from the cell or from the cell culture medium.
In another series of embodiments, the invention provides isolated nucleic acids comprising sequences at least about 8 nucleotides in length, more preferably at least about 12 nucleotides in length, and most preferably at least about 15-20 nucleotides in length, that correspond to a subsequence of any one of SEQ ID NO: 1-SEQ ID NO: 2661 or complements thereof. Alternatively, the nucleic acids comprise sequences contained within any ORF (open reading frame), including a complete protein-coding sequence, of which any of SEQ ID NO: 1-SEQ ID NO: 2661 forms a part. The invention encompasses sequence-conservative variants and function-conservative variants of these sequences. The nucleic acids may be DNA, RNA, DNA/RNA duplexes, protein-nucleic acid (PNA), or derivatives thereof.
In another aspect, the invention features, a purified recombinant nucleic acid having at least 50%, 60%, 70%, 80%, 90%, 95%, 98%, or 99% homology with a sequence of the invention contained in the Sequence Listing.
In another aspect, the invention features nucleic acids capable of binding mRNA of S. pneumoniae. Such nucleic acid is capable of acting as antisense nucleic acid to control the translation of mRNA of S. pneumoniae. A further aspect features a nucleic acid which is capable of binding specifically to an S. pneumoniae nucleic acid. These nucleic acids are also referred to herein as complements and have utility as probes and as capture reagents.
In another aspect, the invention features an expression system comprising an open reading frame corresponding to S. pneumoniae nucleic acid. The nucleic acid further comprises a control sequence compatible with an intended host. The expression system is useful for making polypeptides corresponding to S. pneumoniae nucleic acid.
In another aspect, the invention features a cell transformed with the expression system to produce S. pneumoniae polypeptides.
In yet another embodiment, the invention encompasses reagents for detecting bacterial infection, including S. pneumoniae infection, which comprise at least one S. pneumoniae-derived nucleic acid defined by any one of SEQ ID NO: 1-SEQ ID NO: 2661, or sequence-conservative or function-conservative variants thereof. Alternatively, the diagnostic reagents comprise polypeptide sequences that are contained within any open reading frames (ORFs), including complete protein-coding sequences, contained within any of SEQ ID NO: 1-SEQ ID NO: 2661, or polypeptide sequences contained within any of SEQ ID NO: 2662-SEQ ID NO: 5322, or polypeptides of which any of the above sequences forms a part, or antibodies directed against any of the above peptide sequences or function-conservative variants and/or fragments thereof.
The invention further provides antibodies, preferably monoclonal antibodies, which specifically bind to the polypeptides of the invention. Methods are also provided for producing antibodies in a host animal. The methods of the invention comprise immunizing an animal with at least one S. pneumoniae-derived immunogenic component, wherein the immunogenic component comprises one or more of the polypeptides encoded by any one of SEQ ID NO: 1-SEQ ID NO: 2661 or sequence-conservative or function-conservative variants thereof; or polypeptides that are contained within any ORFs, including complete protein-coding sequences, of which any of SEQ ID NO: 1-SEQ ID NO: 2661 forms a part; or polypeptide sequences contained within any of SEQ ID NO: 2662-SEQ ID NO: 5322; or polypeptides of which any of SEQ ID NO: 2662-SEQ ID NO: 5322 forms a part. Host animals include any warm blooded animal, including without limitation mammals and birds. Such antibodies have utility as reagents for immunoassays to evaluate the abundance and distribution of S. pneumoniae-specific antigens.
In yet another aspect, the invention provides a method for detecting bacterial antigenic components in a sample, which comprises the steps of: (i) contacting a sample suspected to contain a bacterial antigenic component with a bacterial-specific antibody, under conditions in which a stable antigen-antibody complex can form between the antibody and bacterial antigenic components in the sample; and (ii) detecting any antigen-antibody complex formed in step (i), wherein detection of an antigen-antibody complex indicates the presence of at least one bacterial antigenic component in the sample. In different embodiments of this method, the antibodies used are directed against a sequence encoded by any of SEQ ID NO: 1-SEQ ID NO: 2661 or sequence-conservative or function-conservative variants thereof, or against a polypeptide sequence contained in any of SEQ ID NO: 2662-SEQ ID NO: 5322 or function-conservative variants thereof.
In yet another aspect, the invention provides a method for detecting antibacterial-specific antibodies in a sample, which comprises: (i) contacting a sample suspected to contain antibacterial-specific antibodies with a S. pneumoniae antigenic component, under conditions in which a stable antigen-antibody complex can form between the S. pneumoniae antigenic component and antibacterial antibodies in the sample; and (ii) detecting any antigen-antibody complex formed in step (i), wherein detection of an antigen-antibody complex indicates the presence of antibacterial antibodies in the sample. In different embodiments of this method, the antigenic component is encoded by a sequence contained in any of SEQ ID NO: 1-SEQ ID NO: 2661 or sequence-conservative and function-conservative variants thereof, or is a polypeptide sequence contained in any of SEQ ID NO: 2662-SEQ ID NO: 5322 or function-conservative variants thereof.
In another aspect, the invention features a method of generating vaccines for immunizing an individual against S. pneumoniae. The method includes: immunizing a subject with an S. pneumoniae polypeptide, e.g., a surface or secreted polypeptide, or active portion thereof, and a pharmaceutically acceptable carrier. Such vaccines have therapeutic and prophylactic utilities.
In another aspect, the invention features a method of evaluating a compound, e.g. a polypeptide, e.g., a fragment of a host cell polypeptide, for the ability to bind an S. pneumoniae polypeptide. The method includes: contacting the candidate compound with an S. pneumoniae polypeptide and determining if the compound binds or otherwise interacts with an S. pneumoniae polypeptide. Compounds which bind S. pneumoniae are candidates as activators or inhibitors of the bacterial life cycle These assays can be performed in vitro or in vivo.
In another aspect, the invention features a method of evaluating a compound, e.g. a polypeptide, e.g., a fragment of a host cell polypeptide, for the ability to bind an S. pneumoniae nucleic acid, e.g., DNA or RNA. The method includes: contacting the candidate compound with an S. pneumoniae nucleic acid and determining if the compound binds or otherwise interacts with an S. pneumoniae polypeptide. Compounds which bind S. pneumoniae are candidates as activators or inhibitors of the bacterial life cycle. These assays can be performed in vitro or in vivo.
DETAILED DESCRIPTION OF THE INVENTION
The sequences of the present invention include the specific nucleic acid and amino acid sequences set forth in the Sequence Listing that forms a part of the present specification, and which are designated SEQ ID NO: 1-SEQ ID NO: 5322. Use of the terms “SEQ ID NO: 1-SEQ ID NO: 2661”, “SEQ ID NO: 2662-SEQ ID NO: 5322”, “the sequences depicted in Table 2”, etc., is intended, for convenience, to refer to each individual SEQ ID NO individually, and is not intended to refer to the genus of these sequences. In other words, it is a shorthand for listing all of these sequences individually. The invention encompasses each sequence individually, as well as any combination thereof.
Definitions
“Nucleic acid” or “polynucleotide” as used herein refers to purine- and pyrimidine-containing polymers of any length, either polyribonucleotides or polydeoxyribonucleotides or mixed polyribo-polydeoxyribo nucleotides. This includes single- and double-stranded molecules, i.e., DNA-DNA, DNA-RNA and RNA-RNA hybrids, as well as “protein nucleic acids” (PNA) formed by conjugating bases to an amino acid backbone. This also includes nucleic acids containing modified bases.
A nucleic acid or polypeptide sequence that is “derived from” a designated sequence refers to a sequence that corresponds to a region of the designated sequence. For nucleic acid sequences, this encompasses sequences that are homologous or complementary to the sequence, as well as “sequence-conservative variants” and “function-conservative variants.” For polypeptide sequences, this encompasses “function-conservative variants.” Sequence-conservative variants are those in which a change of one or more nucleotides in a given codon position results in no alteration in the amino acid encoded at that position. Function-conservative variants are those in which a given amino acid residue in a polypeptide has been changed without altering the overall conformation and function of the native polypeptide, including, but not limited to, replacement of an amino acid with one having similar physico-chemical properties (such as, for example, acidic, basic, hydrophobic, and the like). “Function-conservative” variants also include any polypeptides that have the ability to elicit antibodies specific to a designated polypeptide.
An “S. pneumoniae-derived” nucleic acid or polypeptide sequence may or may not be present in other bacterial species, and may or may not be present in all S. pneumoniae strains. This term is intended to refer to the source from which the sequence was originally isolated. Thus, a S. pneumoniae-derived polypeptide, as used herein, may be used, e.g., as a target to screen for a broad spectrum antibacterial agent, to search for homologous proteins in other species of bacteria or in eukaryotic organisms such as fungi and humans, etc.
A purified or isolated polypeptide or a substantially pure preparation of a polypeptide are used interchangeably herein and, as used herein, mean a polypeptide that has been separated from other proteins, lipids, and nucleic acids with which it naturally occurs. Preferably, the polypeptide is also separated from substances, e.g., antibodies or gel matrix, e.g., polyacrylamide, which are used to purify it. Preferably, the polypeptide constitutes at least 10, 20, 50 70, 80 or 95% dry weight of the purified preparation. Preferably, the preparation contains: sufficient polypeptide to allow protein sequencing; at least 1, 10, or 100 mg of the polypeptide.
A purified preparation of cells refers to, in the case of plant or animal cells, an in vitro preparation of cells and not an entire intact plant or animal. In the case of cultured cells or microbial cells, it consists of a preparation of at least 10% and more preferably 50% of the subject cells.
A purified or isolated or a substantially pure nucleic acid, e.g., a substantially pure DNA, (are terms used interchangeably herein) is a nucleic acid which is one or both of the following: not immediately contiguous with both of the coding sequences with which it is immediately contiguous (i.e., one at the 5′ end and one at the 3′ end) in the naturally-occurring genome of the organism from which the nucleic acid is derived; or which is substantially free of a nucleic acid with which it occurs in the organism from which the nucleic acid is derived. The term includes, for example, a recombinant DNA which is incorporated into a vector, e.g., into an autonomously replicating plasmid or virus, or into the genomic DNA of a prokaryote or eukaryote, or which exists as a separate molecule (e.g., a cDNA or a genomic DNA fragment produced by PCR or restriction endonuclease treatment) independent of other DNA sequences. Substantially pure DNA also includes a recombinant DNA which is part of a hybrid gene encoding additional S. pneumoniae DNA sequence.
A “contig” as used herein is a nucleic acid representing a continuous stretch of genomic sequence of an organism.
An “open reading frame”, also referred to herein as ORF, is a region of nucleic acid which encodes a polypeptide. This region usually represents the total coding region for the polypeptide and can be determined from a stop to stop codon or from a start to stop codon.
As used herein, a “coding sequence” is a nucleic acid which is transcribed into messenger RNA and/or translated into a polypeptide when placed under the control of appropriate regulatory sequences. The boundaries of the coding sequence are determined by a translation start codon at the five prime terminus and a translation stop codon at the three prime terminus. A coding sequence can include but is not limited to messenger RNA, synthetic DNA, and recombinant nucleic acid sequences.
A “complement” of a nucleic acid as used herein refers to an anti-parallel or antisense sequence that participates in Watson-Crick base-pairing with the original sequence.
A “gene product” is a protein or structural RNA which is specifically encoded by a gene.
As used herein, the term “probe” refers to a nucleic acid, peptide or other chemical entity which specifically binds to a molecule of interest. Probes are often associated with or capable of associating with a label. A label is a chemical moiety capable of detection. Typical labels comprise dyes, radioisotopes, luminescent and chemiluminescent moieties, fluorophores, enzymes, precipitating agents, amplification sequences, and the like. Similarly, a nucleic acid, peptide or other chemical entity which specifically binds to a molecule of interest and immobilizes such molecule is referred herein as a “capture ligand”. Capture ligands are typically associated with or capable of associating with a support such as nitro-cellulose, glass, nylon membranes, beads, particles and the like. The specificity of hybridization is dependent on conditions such as the base pair composition of the nucleotides, and the temperature and salt concentration of the reaction. These conditions are readily discernable to one of ordinary skill in the art using routine experimentation.
“Homologous” refers to the sequence similarity or sequence identity between two polypeptides or between two nucleic acid molecules. When a position in both of the two compared sequences is occupied by the same base or amino acid monomer subunit, e.g., if a position in each of two DNA molecules is occupied by adenine, then the molecules are homologous at that position. The percent of homology between two sequences is a function of the number of matching or homologous positions shared by the two sequences divided by the number of positions compared×100. For example, if 6 of 10 of the positions in two sequences are matched or homologous then the two sequences are 60% homologous. By way of example, the DNA sequences ATTGCC and TATGGC share 50% homology. Generally, a comparison is made when two sequences are aligned to give maximum homology.
Nucleic acids are hybridizable to each other when at least one strand of a nucleic acid can anneal to the other nucleic acid under defined stringency conditions. Stringency of hybridization is determined by: (a) the temperature at which hybridization and/or washing is performed; and (b) the ionic strength and polarity of the hybridization and washing solutions. Hybridization requires that the two nucleic acids contain complementary sequences; depending on the stringency of hybridization, however, mismatches may be tolerated. Typically, hybridization of two sequences at high stingency (such as, for example, in a solution of 0.5×SSC, at 65° C.) requires that the sequences be essentially completely homologous. Conditions of intermediate stringency (such as, for example, 2×SSC at 65° C.) and low stringency (such as, for example 2×SSC at 55° C.), require correspondingly less overall complementarity between the hybridizing sequences. (1×SSC is 0.15 M NaCl, 0.015 M Na citrate).
The terms peptides, proteins, and polypeptides are used interchangeably herein.
As used herein, the term “surface protein” refers to all surface accessible proteins, e.g. inner and outer membrane proteins, proteins adhering to the cell wall, and secreted proteins.
A polypeptide has S. pneumoniae biological activity if it has one, two and preferably more of the following properties: (1) if when expressed in the course of an S. pneumoniae infection, it can promote, or mediate the attachment of S. pneumoniae to a cell; (2) it has an enzymatic activity, structural or regulatory function characteristic of an S. pneumoniae protein; (3) or the gene which encodes it can rescue a lethal mutation in an S. pneumoniae gene. A polypeptide has biological activity if it is an antagonist, agonist, or super-agonist of a polypeptide having one of the above-listed properties.
A biologically active fragment or analog is one having an in vivo or in vitro activity which is characteristic of the S. pneumoniae polypeptides of the invention contained in the Sequence Listing, or of other naturally occurring S. pneumoniae polypeptides, e.g., one or more of the biological activities described herein. Especially preferred are fragments which exist in vivo, e.g., fragments which arise from post transcriptional processing or which arise from translation of alternatively spliced RNA's. Fragments include those expressed in native or endogenous cells as well as those made in expression systems, e.g., in CHO cells. Because peptides such as S. pneumoniae polypeptides often exhibit a range of physiological properties and because such properties may be attributable to different portions of the molecule, a useful S. pneumoniae fragment or S. pneumoniae analog is one which exhibits a biological activity in any biological assay for S. pneumoniae activity. Most preferably the fragment or analog possesses 10%, preferably 40%, more preferably 60%, 70%, 80% or 90% or greater of the activity of S. pneumoniae, in any in vivo or in vitro assay.
Analogs can differ from naturally occurring S. pneumoniae polypeptides in amino acid sequence or in ways that do not involve sequence, or both. Non-sequence modifications include changes in acetylation, methylation, phosphorylation, carboxylation, or glycosylation. Preferred analogs include S. pneumoniae polypeptides (or biologically active fragments thereof) whose sequences differ from the wild-type sequence by one or more conservative amino acid substitutions or by one or more non-conservative amino acid substitutions, deletions, or insertions which do not substantially diminish the biological activity of the S. pneumoniae polypeptide. Conservative substitutions typically include the substitution of one amino acid for another with similar characteristics, e.g., substitutions within the following groups: valine, glycine; glycine, alanine; valine, isoleucine, leucine; aspartic acid, glutamic acid; asparagine, glutamine; serine, threonine; lysine, arginine; and phenylalanine, tyrosine. Other conservative substitutions can be made in view of the table below.
TABLE 1
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CONSERVATIVE AMINO ACID REPLACEMENTS
For Amino AcidCodeReplace with any of
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AlanineAD-Ala, Gly, beta-Ala, L-Cys, D-Cys
ArginineRD-Arg, Lys, D-Lys, homo-Arg,
D-homo-Arg, Met, Ile,
D-Met, D-Ile, Orn, D-Orn
AsparagineND-Asn, Asp, D-Asp, Glu, D-Glu, Gln, D-Gln
Aspartic AcidDD-Asp, D-Asn, Asn, Glu, D-Glu, Gln, D-Gln
CysteineCD-Cys, S-Me-Cys, Met, D-Met, Thr, D-Thr
GlutamineQD-Gln, Asn, D-Asn, Glu, D-Glu, Asp, D-Asp
Glutamic AcidED-Glu, D-Asp, Asp, Asn, D-Asn, Gln, D-Gln
GlycineGAla, D-Ala, Pro, D-Pro, β-Ala, Acp
IsoleucineID-Ile, Val, D-Val, Leu, D-Leu, Met, D-Met
LeucineLD-Leu, Val, D-Val, Leu, D-Leu, Met, D-Met
LysineKD-Lys, Arg, D-Arg, homo-Arg,
D-homo-Arg, Met, D-
Met, Ile, D-Ile, Orn, D-Orn
MethionineMD-Met, S-Me-Cys, Ile, D-Ile,
Leu, D-Leu, Val, D-Val
PhenylalanineFD-Phe, Tyr, D-Thr, L-Dopa,
His, D-His, Trp, D-Trp,
Trans-3,4, or 5-phenylproline,
cis-3,4, or 5-phenylproline
ProlinePD-Pro, L-I-thioazolidine-4-carboxylic
acid, D-or L-1-
oxazolidine-4-carboxylic acid
SerineSD-Ser, Thr, D-Thr, allo-Thr,
Met, D-Met, Met(O),
D-Met(O), L-Cys, D-Cys
ThreonineTD-Thr, Ser, D-Ser,
allo-Thr, Met, D-Met, Met(O),
D-Met(O), Val, D-Val
TyrosineYD-Tyr, Phe, D-Phe, L-Dopa, His, D-His
ValineVD-Val, Leu, D-Leu, Ile, D-Ile, Met, D-Met
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Other analogs within the invention are those with modifications which increase peptide stability; such analogs may contain, for example, one or more non-peptide bonds (which replace the peptide bonds) in the peptide sequence. Also included are: analogs that include residues other than naturally occurring L-amino acids, e.g., D-amino acids or non-naturally occurring or synthetic amino acids, e.g., β or γ amino acids; and cyclic analogs.
As used herein, the term “fragment”, as applied to an S. pneumoniae analog, will ordinarily be at least about 20 residues, more typically at least about 40 residues, preferably at least about 60 residues in length. Fragments of S. pneumoniae polypeptides can be generated by methods known to those skilled in the art. The ability of a candidate fragment to exhibit a biological activity of S. pneumoniae polypeptide can be assessed by methods known to those skilled in the art as described herein. Also included are S. pneumoniae polypeptides containing residues that are not required for biological activity of the peptide or that result from alternative mRNA splicing or alternative protein processing events.
An “immunogenic component” as used herein is a moiety, such as an S. pneumoniae polypeptide, analog or fragment thereof, that is capable of eliciting a humoral and/or cellular immune response in a host animal.
An “antigenic component” as used herein is a moiety, such as an S. pneumoniae polypeptide, analog or fragment thereof, that is capable of binding to a specific antibody with sufficiently high affinity to form a detectable antigen-antibody complex.
The term “antibody” as used herein is intended to include fragments thereof which are specifically reactive with S. pneumoniae polypeptides.
As used herein, the term “cell-specific promoter” means a DNA sequence that serves as a promoter, i.e., regulates expression of a selected DNA sequence operably linked to the promoter, and which effects expression of the selected DNA sequence in specific cells of a tissue. The term also covers so-called “leaky” promoters, which regulate expression of a selected DNA primarily in one tissue, but cause expression in other tissues as well.
Misexpression, as used herein, refers to a non-wild type pattern of gene expression. It includes: expression at non-wild type levels, i.e., over or under expression; a pattern of expression that differs from wild type in terms of the time or stage at which the gene is expressed, e.g., increased or decreased expression (as compared with wild type) at a predetermined developmental period or stage; a pattern of expression that differs from wild type in terms of decreased expression (as compared with wild type) in a predetermined cell type or tissue type; a pattern of expression that differs from wild type in terms of the splicing size, amino acid sequence, post-translational modification, or biological activity of the expressed polypeptide; a pattern of expression that differs from wild type in terms of the effect of an environmental stimulus or extracellular stimulus on expression of the gene, e.g., a pattern of increased or decreased expression (as compared with wild type) in the presence of an increase or decrease in the strength of the stimulus.
As used herein, “host cells” and other such terms denoting microorganisms or higher eukaryotic cell lines cultured as unicellular entities refers to cells which can become or have been used as recipients for a recombinant vector or other transfer DNA, and include the progeny of the original cell which has been transfected. It is understood by individuals skilled in the art that the progeny of a single parental cell may not necessarily be completely identical in genomic or total DNA compliment to the original parent, due to accident or deliberate mutation.
As used herein, the term “control sequence” refers to a nucleic acid having a base sequence which is recognized by the host organism to effect the expression of encoded sequences to which they are ligated. The nature of such control sequences differs depending upon the host organism; in prokaryotes, such control sequences generally include a promoter, ribosomal binding site, terminators, and in some cases operators; in eukaryotes, generally such control sequences include promoters, terminators and in some instances, enhancers. The term control sequence is intended to include at a minimum, all components whose presence is necessary for expression, and may also include additional components whose presence is advantageous, for example, leader sequences.
As used herein, the term “operably linked” refers to sequences joined or ligated to function in their intended manner. For example, a control sequence is operably linked to coding sequence by ligation in such a way that expression of the coding sequence is achieved under conditions compatible with the control sequence and host cell.
The “metabolism” of a substance, as used herein, means any aspect of the expression, function, action, or regulation of the substance. The metabolism of a substance includes modifications, e.g., covalent or non-covalent modifications of the substance. The metabolism of a substance includes modifications, e.g., covalent or non-covalent modification, the substance induces in other substances. The metabolism of a substance also includes changes in the distribution of the substance. The metabolism of a substance includes changes the substance induces in the distribution of other substances.
A “sample” as used herein refers to a biological sample, such as, for example, tissue or fluid isolated from an individual (including without limitation plasma, serum, cerebrospinal fluid, lymph, tears, saliva and tissue sections) or from in vitro cell culture constituents, as well as samples from the environment.
Technical and scientific terms used herein have the meanings commonly understood by one of ordinary skill in the art to which the present invention pertains, unless otherwise defined. Reference is made herein to various methodologies known to those of skill in the art. Publications and other materials setting forth such known methodologies to which reference is made are incorporated herein by reference in their entireties as though set forth in full. The practice of the invention will employ, unless otherwise indicated, conventional techniques of chemistry, molecular biology, microbiology, recombinant DNA, and immunology, which are within the skill of the art. Such techniques are explained fully in the literature. See e.g., Sambrook, Fritsch, and Maniatis, Molecular Cloning; Laboratory Manual 2nd ed. (1989); DNA Cloning, Volumes I and II (D. N Glover ed. 1985); Oligonucleotide Synthesis (M. J. Gait ed, 1984); Nucleic Acid Hybridization (B. D. Hames & S. J. Higgins eds. 1984); the series, Methods in Enzymology (Academic Press, Inc.), particularly Vol. 154 and Vol. 155 (Wu and Grossman, eds.); PCR-A Practical Approach (McPherson, Quirke, and Taylor, eds., 1991); Immunology, 2d Edition, 1989, Roitt et al., C. V. Mosby Company, and New York; Advanced Immunology, 2d Edition, 1991, Male et al., Grower Medical Publishing, New York.; DNA Cloning: A Practical Approach, Volumes I and II, 1985 (D. N. Glover ed.); Oligonucleotide Synthesis, 1984, (M. L. Gait ed); Transcription and Translation, 1984 (Hames and Higgins eds.); Animal Cell Culture, 1986 (R. I. Freshney ed.); Immobilized Cells and Enzymes, 1986 (IRL Press); Perbal, 1984, A Practical Guide to Molecular Cloning; and Gene Transfer Vectors for Mammalian Cells, 1987 (J. H. Miller and M. P. Calos eds., Cold Spring Harbor Laboratory).
Any suitable materials and/or methods known to those of skill can be utilized in carrying out the present invention: however preferred materials and/or methods are described. Materials, reagents and the like to which reference is made in the following description and examples are obtainable from commercial sources, unless otherwise noted.
S. pneumoniae Genomic Sequence
This invention provides nucleotide sequences of the genome of S. pneumoniae which thus comprises a DNA sequence library of S. pneumoniae genomic DNA. The detailed description that follows provides nucleotide sequences of S. pneumoniae, and also describes how the sequences were obtained and how ORFs and protein-coding sequences were identified. Also described are methods of using the disclosed S. pneumoniae sequences in methods including diagnostic and therapeutic applications. Furthermore, the library can be used as a database for identification and comparison of medically important sequences in this and other strains of S. pneumoniae.
To determine the genomic sequence of S. pneumoniae, DNA was isolated from strain 14453 of S. pneumoniae and mechanically sheared by nebulization to a median size of 2 kb. Following size fractionation by gel electrophoresis, the fragments were blunt-ended, ligated to adapter oligonucleotides, and cloned into each of 20 different pMPX vectors (Rice et al., abstracts of Meeting of Genome Mapping and Sequencing, Cold Spring Harbor, N.Y., May 11-May 15, 1994, p. 225) and the PUC19 vector to construct a series of “shotgun” subclone libraries.
DNA sequencing was achieved using two sequencing methods. The first method used multiplex sequencing procedures essentially as disclosed in Church et al., 1988, Science 240: 185; U.S. Pat. Nos. 4,942,124 and 5,149,625). DNA was extracted from pooled cultures and subjected to chemical or enzymatic sequencing. Sequencing reactions were resolved by electrophoresis, and the products were transferred and covalently bound to nylon membranes. Finally, the membranes were sequentially hybridized with a series of labelled oligonucleotides complimentary to “tag” sequences present in the different shotgun cloning vectors. In this manner, a large number of sequences could be obtained from a single set of sequencing reactions. The remainder of the sequencing was performed on ABI377 automated DNA sequencers. The cloning and sequencing procedures are described in more detail in the Exemplification.
Individual sequence reads were assembled using PHRAP (P. Green, Abstracts of DOE Human Genome Program Contractor-Grantee Workshop V, January 1996, p. 157). The average contig length was about 3-4 kb.
A variety of approaches are used to order the contigs so as to obtain a continuous sequence representing the entire S. pneumoniae genome. Synthetic oligonucleotides are designed that are complementary to sequences at the end of each contig. These oligonucleotides may be hybridized to libaries of S. pneumoniae genomic DNA in, for example, lambda phage vectors or plasmid vectors to identify clones that contain sequences corresponding to the junctional regions between individual contigs. Such clones are then used to isolate template DNA and the same oligonucleotides are used as primers in polymerase chain reaction (PCR) to amplify junctional fragments, the nucleotide sequence of which is then determined.
The S. pneumoniae sequences were analyzed for the presence of open reading frames (ORFs) comprising at least 180 nucleotides. As a result of the initial analysis of ORFs based on stop-to-stop codon reads, it should be understood that these ORFs may not correspond to the ORF of a naturally-occurring S. pneumoniae polypeptide. These ORFs may contain start codons which indicate the initiation of protein synthesis of a naturally-occurring S. pneumoniae polypeptide. Such start codons within the ORFs provided herein can be identified by those of ordinary skill in the relevant art, and the resulting ORF and the encoded S. pneumoniae polypeptide is within the scope of this invention. For example, within the ORFs a codon such as AUG or GUG (encoding methionine or valine) which is part of the initiation signal for protein synthesis can be identified and the portion of an ORF to corresponding to a naturally-occurring S. pneumoniae polypeptide can be recognized.
The second analysis of the ORFs included identifying the start codons and the predicted coding regions. These ORFs provided in this invention were defined by one or more of the following methods: evaluating the coding potential of such sequences with the program GENEMARK™ (Borodovsky and McIninch, 1993, Comp. 17: 123), distinguishing the coding from noncoding regions using the program Glimmer (Fraser et al, Nature, 1997), determining codon usage (Staden et al., Nucleic Acid Research 10: 141), and each predicted ORF amino acid sequence was compared with all protein sequences found in current GENBANK, SWISS-PROT, and PIR databases using the BLAST algorithm. BLAST identifies local alignments occurring by chance between the ORF sequence and the sequence in the databank (Altschal et al., 1990, L Mol. Biol. 215: 403-410). Homologous ORFs (probabilities less than 10−5 by chance) and ORF's that are probably non-homologous (probabilities greater than 10−5 by chance) but have good codon usage were identified. Both homologous, sequences and non-homologous sequences with good codon usage are likely to encode proteins and are encompassed by the invention.
S. pneumoniae Nucleic Acids
The nucleic acids of this invention may be obtained directly from the DNA of the above referenced S. pneumoniae strain by using the polymerase chain reaction (PCR). See “PCR, A Practical Approach” (McPherson, Quirke, and Taylor, eds., IRL Press, Oxford, UK, 1991) for details about the PCR. High fidelity PCR can be used to ensure a faithful DNA copy prior to expression. In addition, the authenticity of amplified products can be verified by conventional sequencing methods. Clones carrying the desired sequences described in this invention may also be obtained by screening the libraries by means of the PCR or by hybridization of synthetic oligonucleotide probes to filter lifts of the library colonies or plaques as known in the art (see, e.g., Sambrook et al., Molecular Cloning, A Laboratory Manual 2nd edition, 1989, Cold Spring Harbor Press, NY).
It is also possible to obtain nucleic acids encoding S. pneumoniae polypeptides from a cDNA library in accordance with protocols herein described. A cDNA encoding an S. pneumoniae polypeptide can be obtained by isolating total mRNA from an appropriate strain. Double stranded cDNAs can then be prepared from the total mRNA. Subsequently, the cDNAs can be inserted into a suitable plasmid or viral (e.g., bacteriophage) vector using any one of a number of known techniques. Genes encoding S. pneumoniae polypeptides can also be cloned using established polymerase chain reaction techniques in accordance with the nucleotide sequence information provided by the invention. The nucleic acids of the invention can be DNA or RNA. Preferred nucleic acids of the invention are contained in the Sequence Listing.
The nucleic acids of the invention can also be chemically synthesized using standard techniques. Various methods of chemically synthesizing polydeoxynucleotides are known, including solid-phase synthesis which, like peptide synthesis, has been fully automated in commercially available DNA synthesizers (See e.g., Itakura et al. U.S. Pat. No. 4,598,049; Caruthers et al. U.S. Pat. No. 4,458,066; and Itakura U.S. Pat. Nos. 4,401,796 and 4,373,071, incorporated by reference herein).
Nucleic acids isolated or synthesized in accordance with features of the present invention are useful, by way of example, without limitation, as probes, primers, capture ligands, antisense genes and for developing expression systems for the synthesis of proteins and peptides corresponding to such sequences. As probes, primers, capture ligands and antisense agents, the nucleic acid normally consists of all or part (approximately twenty or more nucleotides for specificity as well as the ability to form stable hybridization products) of the nucleic acids of the invention contained in the Sequence Listing. These uses are described in further detail below.
Probes
A nucleic acid isolated or synthesized in accordance with the sequence of the invention contained in the Sequence Listing can be used as a probe to specifically detect S. pneumoniae. With the sequence information set forth in the present application, sequences of twenty or more nucleotides are identified which provide the desired inclusivity and exclusivity with respect to S. pneumoniae, and extraneous nucleic acids likely to be encountered during hybridization conditions. More preferably, the sequence will comprise at least twenty to thirty nucleotides to convey stability to the hybridization product formed between the probe and the intended target molecules.
Sequences larger than 1000 nucleotides in length are difficult to synthesize but can be generated by recombinant DNA techniques. Individuals skilled in the art will readily recognize that the nucleic acids, for use as probes, can be provided with a label to facilitate detection of a hybridization product.
Nucleic acid isolated and synthesized in accordance with the sequence of the invention contained in the Sequence Listing can also be useful as probes to detect homologous regions (especially homologous genes) of other Streptococcus species using appropriate stringency hybridization conditions as described herein.
Capture Ligand
For use as a capture ligand, the nucleic acid selected in the manner described above with respect to probes, can be readily associated with a support. The manner in which nucleic acid is associated with supports is well known. Nucleic acid having twenty or more nucleotides in a sequence of the invention contained in the Sequence Listing have utility to separate S. pneumoniae nucleic acid from the nucleic acid of each other and other organisms. Nucleic acid having twenty or more nucleotides in a sequence of the invention contained in the Sequence Listing can also have utility to separate other Streptococcus species from each other and from other organisms. Preferably, the sequence will comprise at least twenty nucleotides to convey stability to the hybridization product formed between the probe and the intended target molecules. Sequences larger than 1000 nucleotides in length are difficult to synthesize but can be generated by recombinant DNA techniques.
Primers
Nucleic acid isolated or synthesized in accordance with the sequences described herein have utility as primers for the amplification of S. pneumoniae nucleic acid. These nucleic acids may also have utility as primers for the amplification of nucleic acids in other Streptococcus species. With respect to polymerase chain reaction (PCR) techniques, nucleic acid sequences of ≧10-15 nucleotides of the invention contained in the Sequence Listing have utility in conjunction with suitable enzymes and reagents to create copies of S. pneumoniae nucleic acid. More preferably, the sequence will comprise twenty or more nucleotides to convey stability to the hybridization product formed between the primer and the intended target molecules. Binding conditions of primers greater than 100 nucleotides are more difficult to control to obtain specificity. High fidelity PCR can be used to ensure a faithful DNA copy prior to expression. In addition, amplified products can be checked by conventional sequencing methods.
The copies can be used in diagnostic assays to detect specific sequences, including genes from S. pneumoniae and/or other Streptococcus species. The copies can also be incorporated into cloning and expression vectors to generate polypeptides corresponding to the nucleic acid synthesized by PCR, as is described in greater detail herein.
Antisense
Nucleic acid or nucleic acid-hybridizing derivatives isolated or synthesized in accordance with the sequences described herein have utility as antisense agents to prevent the expression of S. pneumoniae genes. These sequences also have utility as antisense agents to prevent expression of genes of other Streptococcus species.
In one embodiment, nucleic acid or derivatives corresponding to S. pneumoniae nucleic acids is loaded into a suitable carrier such as a liposome or bacteriophage for introduction into bacterial cells. For example, a nucleic acid having twenty or more nucleotides is capable of binding to bacteria nucleic acid or bacteria messenger RNA. Preferably, the antisense nucleic acid is comprised of 20 or more nucleotides to provide necessary stability of a hybridization product of non-naturally occurring nucleic acid and bacterial nucleic acid and/or bacterial messenger RNA. Nucleic acid having a sequence greater than 1000 nucleotides in length is difficult to synthesize but can be generated by recombinant DNA techniques. Methods for loading antisense nucleic acid in liposomes is known in the art as exemplified by U.S. Pat. No. 4,241,046 issued Dec. 23, 1980 to Papahadjopoulos et al.
The present invention encompasses isolated polypeptides and nucleic acids derived from S. pneumoniae that are useful as reagents for diagnosis of bacterial infection, components of effective antibacterial vaccines, and/or as targets for antibacterial drugs, including anti-S. pneumoniae drugs.
Expression of S. pneumoniae Nucleic Acids
Table 2 provides a list of open reading frames (ORFs) in both strands. An ORF is a region of nucleic acid which encodes a polypeptide. This region normally represents a complete coding sequence or a total sequence and was determined from an initial analysis of stop to stop codons followed by the prediction of start codons. The first column lists the ORF designation. The second and third columns list the SEQ ID numbers for the nucleic acid and amino acid sequences corresponding to each ORF, respectively. The fourth and fifth columns list the length of the nucleic acid ORF and the length of the amino acid ORF, respectively. Most of the nucleotide sequences corresponding to each ORF begin at the first nucleotide of the start codon and end at the nucleotide immediately preceding the next downstream stop codon in the same reading frame. It will be recognized by one skilled in the art that the natural translation initiation sites will correspond to ATG, GTG, or TTG codons located within the ORFs. The natural initiation sites depend not only on the sequence of a start codon but also on the context of the DNA sequence adjacent to the start codon. Usually, a recognizable ribosome binding site is found within 20 nucleotides upstream from the initiation codon. In some cases where genes are translationally coupled and coordinately expressed together in “operons”, ribosome binding sites are not present, but the initiation codon of a downstream gene may occur very close to, or overlap, the stop codon of the an upstream gene in the same operon. The correct start codons can be generally identified rapidly and efficiently because only a few codons need be tested. It is recognized that the translational machinery in bacteria initiates most polypeptide chains with the amino acid methionine. In some cases, polypeptides are post-translationally modified, resulting in an N-terminal amino acid other than methionine in vivo. The sixth and seventh columns provide metrics for assessing the likelihood of the homology match (determined by the BLASTP2 algorithm), as is known in the art, to the genes indicated in the description field. Specifically, the sixth column represents the “Score” for the match (a higher score is a better match), and the seventh column represents the “P-value” for the match (the probability that such a match could have occurred by chance; the lower the value, the more likely the match is valid). If a BLASTP2 score of less than 46 was obtained, no value is reported in the table the “P-value”. The description field provides, where available, the accession number (AC) or the Swissprot accession number (SP), the locus name (LN), Superfamily Classification (CL), the Organism (OR), Source of variant (SR), E.C. number (EC), the gene name (GN), the product name (PN), the Function Description (FN), the Map Position (MP), Left End (LE), Right End (RE), Coding Direction (DI), the Database from which the sequence originates (DB), and the description (DE) or notes (NT) for each ORF. This information allows one of ordinary skill in the art to determine a potential use and function for each identified coding sequence and, as a result, allows the use of the polypeptides of the present invention for commercial and industrial purposes.
Using the information provided in SEQ ID NO: 1-SEQ ID NO: 2661 and in Table 2 together with routine cloning and sequencing methods, one of ordinary skill in the art will be able to clone and sequence all the nucleic acid fragments of interest including open reading frames (ORFs) encoding a large variety proteins of S. pneumoniae.
Nucleic acid isolated or synthesized in accordance with the sequences described herein have utility to generate polypeptides. The nucleic acid of the invention exemplified in SEQ ID NO: 1-SEQ ID NO: 2661 and in Table 2 or fragments of said nucleic acid encoding active portions of S. pneumoniae polypeptides can be cloned into suitable vectors or used to isolate nucleic acid. The isolated nucleic acid is combined with suitable DNA linkers and cloned into a suitable vector.
The function of a specific gene or operon can be ascertained by expression in a bacterial strain under conditions where the activity of the gene product(s) specified by the gene or operon in question can be specifically measured. Alternatively, a gene product may be produced in large quantities in an expressing strain for use as an antigen, an industrial reagent, for structural studies, etc. This expression can be accomplished in a mutant strain which lacks the activity of the gene to be tested, or in a strain that does not produce the same gene product(s). This includes, but is not limited to, Eucaryotic species such as the yeast Saccharomyces cerevisiae, Methanobacterium strains or other Archaea, and Eubacteria such as E. coli, B. subtilis, S. aureus, S. pneumonia or Pseudomonas putida. In some cases the expression host will utilize the natural S. pneumoniae promoter whereas in others, it will be necessary to drive the gene with a promoter sequence derived from the expressing organism (e.g., an E. coli beta-galactosidase promoter for expression in E. coli).
To express a gene product using the natural S. pneumoniae promoter, a procedure such as the following can be used. A restriction fragment containing the gene of interest, together with its associated natural promoter element and regulatory sequences (identified using the DNA sequence data) is cloned into an appropriate recombinant plasmid containing an origin of replication that functions in the host organism and an appropriate selectable marker. This can be accomplished by a number of procedures known to those skilled in the art. It is most preferably done by cutting the plasmid and the fragment to be cloned with the same restriction enzyme to produce compatible ends that can be ligated to join the two pieces together. The recombinant plasmid is introduced into the host organism by, for example, electroporation and cells containing the recombinant plasmid are identified by selection for the marker on the plasmid. Expression of the desired gene product is detected using an assay specific for that gene product.
In the case of a gene that requires a different promoter, the body of the gene (coding sequence) is specifically excised and cloned into an appropriate expression plasmid. This subcloning can be done by several methods, but is most easily accomplished by PCR amplification of a specific fragment and ligation into an expression plasmid after treating the PCR product with a restriction enzyme or exonuclease to create suitable ends for cloning.
A suitable host cell for expression of a gene can be any procaryotic or eucaryotic cell. For example, an S. pneumoniae polypeptide can be expressed in bacterial cells such as E. coli or B. subtilis, insect cells (baculovirus), yeast, or mammalian cells such as Chinese hamster ovary cell (CHO). Other suitable host cells are known to those skilled in the art.
Expression in eucaryotic cells such as mammalian, yeast, or insect cells can lead to partial or complete glycosylation and/or formation of relevant inter- or intra-chain disulfide bonds of a recombinant peptide product. Examples of vectors for expression in yeast S. cerivisae include pYepSec1 (Baldari. et al., (1987) Embo J. 6: 229-234), pMFa (Kurjan and Herskowitz, (1982) Cell 30: 933-943), pJRY88 (Schultz et al., (1987) Gene 54: 113-123), and pYES2 (Invitrogen Corporation, San Diego, Calif.). Baculovirus vectors available for expression of proteins in cultured insect cells (SF 9 cells) include the pAc series (Smith et al., (1983) Mol. Cell Biol. 3: 2156-2165) and the pVL series (Lucklow, V. A., and Summers, M. D., (1989) Virology 170: 31-39). Generally, COS cells (Gluzman, Y., (1981) Cell 23: 175-182) are used in conjunction with such vectors as pCDM 8 (Aruffo, A. and Seed, B., (1987) Proc. Natl. Acad. Sci. USA 84: 8573-8577) for transient amplification/expression in mammalian cells, while CHO (dhfr− Chinese Hamster Ovary) cells are used with vectors such as pMT2PC (Kaufman et al. (1987), EMBO J. 6: 187-195) for stable amplification/expression in mammalian cells. Vector DNA can be introduced into mammalian cells via conventional techniques such as calcium phosphate or calcium chloride co-precipitation, DEAE-dextran-mediated transfection, or electroporation. Suitable methods for transforming host cells can be found in Sambrook et al. (Molecular Cloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratory press (1989)), and other laboratory textbooks.
Expression in procaryotes is most often carried out in E. coli with either fusion or non-fusion inducible expression vectors. Fusion vectors usually add a number of NH2 terminal amino acids to the expressed target gene. These NH2 terminal amino acids often are referred to as a reporter group or an affinity purification group. Such reporter groups usually serve two purposes: 1) to increase the solubility of the target recombinant protein; and 2) to aid in the purification of the target recombinant protein by acting as a ligand in affinity purification. Often, in fusion expression vectors, a proteolytic cleavage site is introduced at the junction of the reporter group and the target recombinant protein to enable separation of the target recombinant protein from the reporter group subsequent to purification of the fusion protein. Such enzymes, and their cognate recognition sequences, include Factor Xa, thrombin and enterokinase. Typical fusion expression vectors include pGEX (Amrad Corp., Melbourne, Australia), pMAL (New England Biolabs, Beverly, Mass.) and pRIT5 (Pharmacia, Piscataway, N.J.) which fuse glutathione S-transferase, maltose E binding protein, or protein A, respectively, to the target recombinant protein. A preferred reporter group is poly(His), which may be fused to the amino or carboxy terminus of the protein and which renders the recombinant fusion protein easily purifiable by metal chelate chromatography.
Inducible non-fusion expression vectors include pTrc (Amann et al., (1988) Gene 69: 301-315) and pET11d (Studier et al., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 60-89). While target gene expression relies on host RNA polymerase transcription from the hybrid trp-lac fusion promoter in pTrc, expression of target genes inserted into pET11d relies on transcription from the T7 gn10-lac 0 fusion promoter mediated by coexpressed viral RNA polymerase (T7 gn1). This viral polymerase is supplied by host strains BL21(DE3) or HMS174(DE3) from a resident λ prophage harboring a T7 gn1 under the transcriptional control of the lacUV 5 promoter.
For example, a host cell transfected with a nucleic acid vector directing expression of a nucleotide sequence encoding an S. pneumoniae polypeptide can be cultured under appropriate conditions to allow expression of the polypeptide to occur. The polypeptide may be secreted and isolated from a mixture of cells and medium containing the peptide. Alternatively, the polypeptide may be retained cytoplasmically and the cells harvested, lysed and the protein isolated. A cell culture includes host cells, media and other byproducts. Suitable media for cell culture are well known in the art. Polypeptides of the invention can be isolated from cell culture medium, host cells, or both using techniques known in the art for purifying proteins including ion-exchange chromatography, gel filtration chromatography, ultrafiltration, electrophoresis, and immunoaffinity purification with antibodies specific for such polypeptides. Additionally, in many situations, polypeptides can be produced by chemical cleavage of a native protein (e.g., tryptic digestion) and the cleavage products can then be purified by standard techniques.
In the case of membrane bound proteins, these can be isolated from a host cell by contacting a membrane-associated protein fraction with a detergent forming a solubilized complex, where the membrane-associated protein is no longer entirely embedded in the membrane fraction and is solubilized at least to an extent which allows it to be chromatographically isolated from the membrane fraction. Several different criteria are used for choosing a detergent suitable for solubilizing these complexes. For example, one property considered is the ability of the detergent to solubilize the S. pneumoniae protein within the membrane fraction at minimal denaturation of the membrane-associated protein allowing for the activity or functionality of the membrane-associated protein to return upon reconstitution of the protein. Another property considered when selecting the detergent is the critical micelle concentration (CMC) of the detergent in that the detergent of choice preferably has a high CMC value allowing for ease of removal after reconstitution. A third property considered when selecting a detergent is the hydrophobicity of the detergent. Typically, membrane-associated proteins are very hydrophobic and therefore detergents which are also hydrophobic, e.g., the triton series, would be useful for solubilizing the hydrophobic proteins. Another property important to a detergent can be the capability of the detergent to remove the S. pneumoniae protein with minimal protein-protein interaction facilitating further purification. A fifth property of the detergent which should be considered is the charge of the detergent. For example, if it is desired to use ion exchange resins in the purification process then preferably detergent should be an uncharged detergent. Chromatographic techniques which can be used in the final purification step are known in the art and include hydrophobic interaction, lectin affinity, ion exchange, dye affinity and immunoaffinity.
One strategy to maximize recombinant S. pneumoniae peptide expression in E. coli is to express the protein in a host bacteria with an impaired capacity to proteolytically cleave the recombinant protein (Gottesman, S., Gene Expression Technology: Methods in Enzymology 185, Academic Press, San Diego, Calif. (1990) 119-128). Another strategy would be to alter the nucleic acid encoding an S. pneumoniae peptide to be inserted into an expression vector so that the individual codons for each amino acid would be those preferentially utilized in highly expressed E. coli proteins (Wada et al., (1992) Nuc. Acids Res. 20: 2111-2118). Such alteration of nucleic acids of the invention can be carried out by standard DNA synthesis techniques.
The nucleic acids of the invention can also be chemically synthesized using standard techniques. Various methods of chemically synthesizing polydeoxynucleotides are known, including solid-phase synthesis which, like peptide synthesis, has been fully automated in commercially available DNA synthesizers (See, e.g., Itakura et al. U.S. Pat. No. 4,598,049; Caruthers et al. U.S. Pat. No. 4,458,066; and Itakura U.S. Pat. Nos. 4,401,796 and 4,373,071, incorporated by reference herein).
The present invention provides a library of S. pneumoniae-derived nucleic acid sequences. The libraries provide probes, primers, and markers which can be used as markers in epidemiological studies. The present invention also provides a library of S. pneumoniae-derived nucleic acid sequences which comprise or encode targets for therapeutic drugs.
Nucleic acids comprising any of the sequences disclosed herein or sub-sequences thereof can be prepared by standard methods using the nucleic acid sequence information provided in SEQ ID NO: 1-SEQ ID NO: 2661. For example, DNA can be chemically synthesized using, e.g., the phosphoramidite solid support method of Matteucci et al., 1981, J. Am. Chem. Soc. 103: 3185, the method of Yoo et al., 1989, J. Biol. Chem. 764: 17078, or other well known methods. This can be done by sequentially linking a series of oligonucleotide cassettes comprising pairs of synthetic oligonucleotides, as described below.
Of course, due to the degeneracy of the genetic code, many different nucleotide sequences can encode polypeptides having the amino acid sequences defined by SEQ ID NO: 2662-SEQ ID NO: 5322 or sub-sequences thereof. The codons can be selected for optimal expression in prokaryotic or eukaryotic systems. Such degenerate variants are also encompassed by this invention.
Insertion of nucleic acids (typically DNAs) encoding the polypeptides of the invention into a vector is easily accomplished when the termini of both the DNAs and the vector comprise compatible restriction sites. If this cannot be done, it may be necessary to modify the termini of the DNAs and/or vector by digesting back single-stranded DNA overhangs generated by restriction endonuclease cleavage to produce blunt ends, or to achieve the same result by filling in the single-stranded termini with an appropriate DNA polymerase.
Alternatively, any site desired may be produced, e.g., by ligating nucleotide sequences (linkers) onto the termini. Such linkers may comprise specific oligonucleotide sequences that define desired restriction sites. Restriction sites can also be generated by the use of the polymerase chain reaction (PCR). See, e.g., Saiki et al., 1988, Science 239: 48. The cleaved vector and the DNA fragments may also be modified if required by homopolymeric tailing.
In certain embodiments, the invention encompasses isolated nucleic acid fragments comprising all or part of the individual nucleic acid sequences disclosed herein. The fragments are at least about 8 nucleotides in length, preferably at least about 12 nucleotides in length, and most preferably at least about 15-20 nucleotides in length.
The nucleic acids may be isolated directly from cells. Alternatively, the polymerase chain reaction (PCR) method can be used to produce the nucleic acids of the invention, using either chemically synthesized strands or genomic material as templates. Primers used for PCR can be synthesized using the sequence information provided herein and can further be designed to introduce appropriate new restriction sites, if desirable, to facilitate incorporation into a given vector for recombinant expression.
The nucleic acids of the present invention may be flanked by natural S. pneumoniae regulatory sequences, or may be associated with heterologous sequences, including promoters, enhancers, response elements, signal sequences, polyadenylation sequences, introns, 5′- and 3′-noncoding regions, and the like. The nucleic acids may also be modified by many means known in the art. Non-limiting examples of such modifications include methylation, “caps”, substitution of one or more of the naturally occurring nucleotides with an analog, internucleotide modifications such as, for example, those with uncharged linkages (e.g., methyl phosphonates, phosphotriesters, phosphoroamidates, carbamates, etc.) and with charged linkages (e.g., phosphorothioates, phosphorodithioates, etc.). Nucleic acids may contain one or more additional covalently linked moieties, such as, for example, proteins (e.g., nucleases, toxins, antibodies, signal peptides, poly-L-lysine, etc.), intercalators (e.g., acridine, psoralen, etc.), chelators (e.g., metals, radioactive metals, iron, oxidative metals, etc.), and alkylators. PNAs are also included. The nucleic acid may be derivatized by formation of a methyl or ethyl phosphotriester or an alkyl phosphoramidate linkage. Furthermore, the nucleic acid sequences of the present invention may also be modified with a label capable of providing a detectable signal, either directly or indirectly. Exemplary labels include radioisotopes, fluorescent molecules, biotin, and the like.
The invention also provides nucleic acid vectors comprising the disclosed S. pneumoniae-derived sequences or derivatives or fragments thereof. A large number of vectors, including plasmid and fungal vectors, have been described for replication and/or expression in a variety of eukaryotic and prokaryotic hosts, and may be used for gene therapy as well as for simple cloning or protein expression.
The encoded S. pneumoniae polypeptides may be expressed by using many known vectors, such as pUC plasmids, pET plasmids (Novagen, Inc., Madison, Wis.), or pRSET or pREP (Invitrogen, San Diego, Calif.), and many appropriate host cells, using methods disclosed or cited herein or otherwise known to those skilled in the relevant art. The particular choice of vector/host is not critical to the practice of the invention.
Recombinant cloning vectors will often include one or more replication systems for cloning or expression, one or more markers for selection in the host, e.g. antibiotic resistance, and one or more expression cassettes. The inserted S. pneumoniae coding sequences may be synthesized by standard methods, isolated from natural sources, or prepared as hybrids, etc. Ligation of the S. pneumoniae coding sequences to transcriptional regulatory elements and/or to other amino acid coding sequences may be achieved by known methods. Suitable host cells may be transformed/transfected/infected as appropriate by any suitable method including electroporation, CaCl2 mediated DNA uptake, fungal infection, microinjection, microprojectile, or other established methods.
Appropriate host cells include bacteria, archebacteria, fungi, especially yeast, and plant and animal cells, especially mammalian cells. Of particular interest are S. pneumoniae, E. coli, B. Subtilis, Saccharomyces cerevisiae, Saccharomyces carlsbergensis, Schizosaccharomyces pombi, SF9 cells, C129 cells, 293 cells, Neurospora, and CHO cells, COS cells, HeLa cells, and immortalized mammalian myeloid and lymphoid cell lines. Preferred replication systems include M13, ColE1, SV40, baculovirus, lambda, adenovirus, and the like. A large number of transcription initiation and termination regulatory regions have been isolated and shown to be effective in the transcription and translation of heterologous proteins in the various hosts. Examples of these regions, methods of isolation, manner of manipulation, etc. are known in the art. Under appropriate expression conditions, host cells can be used as a source of recombinantly produced S. pneumoniae-derived peptides and polypeptides.
Advantageously, vectors may also include a transcription regulatory element (i.e., a promoter) operably linked to the S. pneumoniae portion. The promoter may optionally contain operator portions and/or ribosome binding sites. Non-limiting examples of bacterial promoters compatible with E. coli include: b-lactamase (penicillinase) promoter; lactose promoter; tryptophan (trp) promoter; araBAD (arabinose) operon promoter; lambda-derived P1 promoter and N gene ribosome binding site; and the hybrid tac promoter derived from sequences of the trp and lac Uv5 promoters. Non-limiting examples of yeast promoters include 3-phosphoglycerate kinase promoter, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) promoter, galactokinase (GAL1) promoter, galactoepimerase promoter, and alcohol dehydrogenase (ADH) promoter. Suitable promoters for mammalian cells include without limitation viral promoters such as that from Simian Virus 40 (SV40), Rous sarcoma virus (RSV), adenovirus (ADV), and bovine papilloma virus (BPV). Mammalian cells may also require terminator sequences, polyA addition sequences and enhancer sequences to increase expression. Sequences which cause amplification of the gene may also be desirable. Furthermore, sequences that facilitate secretion of the recombinant product from cells, including, but not limited to, bacteria, yeast, and animal cells, such as secretory signal sequences and/or prohormone pro region sequences, may also be included. These sequences are well described in the art.
Nucleic acids encoding wild-type or variant S. pneumoniae-derived polypeptides may also be introduced into cells by recombination events. For example, such a sequence can be introduced into a cell, and thereby effect homologous recombination at the site of an endogenous gene or a sequence with substantial identity to the gene. Other recombination-based methods such as nonhomologous recombinations or deletion of endogenous genes by homologous recombination may also be used.
The nucleic acids of the present invention find use as templates for the recombinant production of S. pneumoniae-derived peptides or polypeptides.
Identification and Use of S. pneumoniae Nucleic Acid Sequences
The disclosed S. pneumoniae polypeptide and nucleic acid sequences, or other sequences that are contained within ORFs, including complete protein-coding sequences, of which any of the disclosed S. pneumoniae-specific sequences forms a part, are useful as target components for diagnosis and/or treatment of S. pneumoniae-caused infection.
It will be understood that the sequence of an entire protein-coding sequence of which each disclosed nucleic acid sequence forms a part can be isolated and identified based on each disclosed sequence. This can be achieved, for example, by using an isolated nucleic acid encoding the disclosed sequence, or fragments thereof, to prime a sequencing reaction with genomic S. pneumoniae DNA as template; this is followed by sequencing the amplified product. The isolated nucleic acid encoding the disclosed sequence, or fragments thereof, can also be hybridized to S. pneumoniae genomic libraries to identify clones containing additional complete segments of the protein-coding sequence of which the shorter sequence forms a part. Then, the entire protein-coding sequence, or fragments thereof, or nucleic acids encoding all or part of the sequence, or sequence-conservative or function-conservative variants thereof, may be employed in practicing the present invention.
Preferred sequences are those that are useful in diagnostic and/or therapeutic applications. Diagnostic applications include without limitation nucleic-acid-based and antibody-based methods for detecting bacterial infection. Therapeutic applications include without limitation vaccines, passive immunotherapy, and drug treatments directed against gene products that are both unique to bacteria and essential for growth and/or replication of bacteria.
Identification of Nucleic Acids Encoding Vaccine Components and Targets for Agents Effective Against S. pneumoniae
The disclosed S. pneumoniae genome sequence includes segments that direct the synthesis of ribonucleic acids and polypeptides, as well as origins of replication, promoters, other types of regulatory sequences, and intergenic nucleic acids. The invention encompasses nucleic acids encoding immunogenic components of vaccines and targets for agents effective against S. pneumoniae. Identification of said immunogenic components involved in the determination of the function of the disclosed sequences, which can be achieved using a variety of approaches. Non-limiting examples of these approaches are described briefly below.
Homology to Known Sequences:
Computer-assisted comparison of the disclosed S. pneumoniae sequences with previously reported sequences present in publicly available databases is useful for identifying functional S. pneumoniae nucleic acid and polypeptide sequences. It will be understood that protein-coding sequences, for example, may be compared as a whole, and that a high degree of sequence homology between two proteins (such as, for example, >80-90%) at the amino acid level indicates that the two proteins also possess some degree of functional homology, such as, for example, among enzymes involved in metabolism, DNA synthesis, or cell wall synthesis, and proteins involved in transport, cell division, etc. In addition, many structural features of particular protein classes have been identified and correlate with specific consensus sequences, such as, for example, binding domains for nucleotides, DNA, metal ions, and other small molecules; sites for covalent modifications such as phosphorylation, acylation, and the like; sites of protein:protein interactions, etc. These consensus sequences may be quite short and thus may represent only a fraction of the entire protein-coding sequence. Identification of such a feature in an S. pneumoniae sequence is therefore useful in determining the function of the encoded protein and identifying useful targets of antibacterial drugs.
Of particular relevance to the present invention are structural features that are common to secretory, transmembrane, and surface proteins, including secretion signal peptides and hydrophobic transmembrane domains. S. pneumoniae proteins identified as containing putative signal sequences and/or transmembrane domains are useful as immunogenic components of vaccines.
Targets for therapeutic drugs according to the invention include, but are not limited to, polypeptides of the invention, whether unique to S. pneumoniae or not, that are essential for growth and/or viability of S. pneumoniae under at least one growth condition. Polypeptides essential for growth and/or viability can be determined by examining the effect of deleting and/or disrupting the genes, i.e., by so-called gene “knockout”. Alternatively, genetic footprinting can be used (Smith et al., 1995, Proc. Natl. Acad. Sci. USA 92: 5479-6433; Published International Application WO 94/26933; U.S. Pat. No. 5,612,180). Still other methods for assessing essentiality includes the ability to isolate conditional lethal mutations in the specific gene (e.g., temperature sensitive mutations). Other useful targets for therapeutic drugs, which include polypeptides that are not essential for growth or viability per se but lead to loss of viability of the cell, can be used to target therapeutic agents to cells.
Strain-Specific Sequences:
Because of the evolutionary relationship between different S. pneumoniae strains, it is believed that the presently disclosed S. pneumoniae sequences are useful for identifying, and/or discriminating between, previously known and new S. pneumoniae strains. It is believed that other S. pneumoniae strains will exhibit at least 70% sequence homology with the presently disclosed sequence. Systematic and routine analyses of DNA sequences derived from samples containing S. pneumoniae strains, and comparison with the present sequence allows for the identification of sequences that can be used to discriminate between strains, as well as those that are common to all S. pneumoniae strains. In one embodiment, the invention provides nucleic acids, including probes, and peptide and polypeptide sequences that discriminate between different strains of S. pneumoniae. Strain-specific components can also be identified functionally by their ability to elicit or react with antibodies that selectively recognize one or more S. pneumoniae strains.
In another embodiment, the invention provides nucleic acids, including probes, and peptide and polypeptide sequences that are common to all S. pneumoniae strains but are not found in other bacterial species.
S. pneumoniae Polypeptides
This invention encompasses isolated S. pneumoniae polypeptides encoded by the disclosed S. pneumoniae genomic sequences, including the polypeptides of the invention contained in the Sequence Listing. Polypeptides of the invention are preferably at least 5 amino acid residues in length. Using the DNA sequence information provided herein, the amino acid sequences of the polypeptides encompassed by the invention can be deduced using methods well-known in the art. It will be understood that the sequence of an entire nucleic acid encoding an S. pneumoniae polypeptide can be isolated and identified based on an ORF that encodes only a fragment of the cognate protein-coding region. This can be achieved, for example, by using the isolated nucleic acid encoding the ORF, or fragments thereof, to prime a polymerase chain reaction with genomic S. pneumoniae DNA as template; this is followed by sequencing the amplified product.
The polypeptides of the present invention, including function-conservative variants of the disclosed ORFs, may be isolated from wild-type or mutant S. pneumoniae cells, or from heterologous organisms or cells (including, but not limited to, bacteria, fungi, insect, plant, and mammalian cells) including S. pneumoniae into which a S. pneumoniae-derived protein-coding sequence has been introduced and expressed. Furthermore, the polypeptides may be part of recombinant fusion proteins.
S. pneumoniae polypeptides of the invention can be chemically synthesized using commercially automated procedures such as those referenced herein, including, without limitation, exclusive solid phase synthesis, partial solid phase methods, fragment condensation or classical solution synthesis. The polypeptides are preferably prepared by solid phase peptide synthesis as described by Merrifield, 1963, J. Am. Chem. Soc. 85: 2149. The synthesis is carried out with amino acids that are protected at the alpha-amino terminus. Trifunctional amino acids with labile side-chains are also protected with suitable groups to prevent undesired chemical reactions from occurring during the assembly of the polypeptides. The alpha-amino protecting group is selectively removed to allow subsequent reaction to take place at the amino-terminus. The conditions for the removal of the alpha-amino protecting group do not remove the side-chain protecting groups.
The alpha-amino protecting groups are those known to be useful in the art of stepwise polypeptide synthesis. Included are acyl type protecting groups, e.g., formyl, trifluoroacetyl, acetyl, aromatic urethane type protecting groups, e.g., benzyloxycarbonyl (Cbz), substituted benzyloxycarbonyl and 9-fluorenylmethyloxycarbonyl (Fmoc), aliphatic urethane protecting groups, e.g., t-butyloxycarbonyl (Boc), isopropyloxycarbonyl, cyclohexyloxycarbonyl, and alkyl type protecting groups, e.g., benzyl, triphenylmethyl. The preferred protecting group is Boc. The side-chain protecting groups for Tyr include tetrahydropyranyl, tert-butyl, trityl, benzyl, Cbz, 4-Br-Cbz and 2,6-dichlorobenzyl. The preferred side-chain protecting group for Tyr is 2,6-dichlorobenzyl. The side-chain protecting groups for Asp include benzyl, 2,6-dichlorobenzyl, methyl, ethyl and cyclohexyl. The preferred side-chain protecting group for Asp is cyclohexyl. The side-chain protecting groups for Thr and Ser include acetyl, benzoyl, trityl, tetrahydropyranyl, benzyl, 2,6-dichlorobenzyl and Cbz. The preferred protecting group for Thr and Ser is benzyl. The side-chain protecting groups for Arg include nitro, Tos, Cbz, adamantyloxycarbonyl and Boc. The preferred protecting group for Arg is Tos. The side-chain amino group of Lys may be protected with Cbz, 2-Cl-Cbz, Tos or Boc. The 2-Cl-Cbz group is the preferred protecting group for Lys.
The side-chain protecting groups selected must remain intact during coupling and not be removed during the deprotection of the amino-terminus protecting group or during coupling conditions. The side-chain protecting groups must also be removable upon the completion of synthesis, using reaction conditions that will not alter the finished polypeptide.
Solid phase synthesis is usually carried out from the carboxy-terminus by coupling the alpha-amino protected (side-chain protected) amino acid to a suitable solid support. An ester linkage is formed when the attachment is made to a chloromethyl or hydroxymethyl resin, and the resulting polypeptide will have a free carboxyl group at the C-terminus. Alternatively, when a benzhydrylamine or p-methylbenzhydrylamine resin is used, an amide bond is formed and the resulting polypeptide will have a carboxamide group at the C-terminus. These resins are commercially available, and their preparation was described by Stewart et al., 1984, Solid Phase Peptide Synthesis (2nd Edition), Pierce Chemical Co., Rockford, Ill.
The C-terminal amino acid, protected at the side chain if necessary and at the alpha-amino group, is coupled to the benzhydrylamine resin using various activating agents including dicyclohexylcarbodiimide (DCC), N,N′-diisopropyl-carbodiimide and carbonyldiimidazole. Following the attachment to the resin support, the alpha-amino protecting group is removed using trifluoroacetic acid (TFA) or HCl in dioxane at a temperature between 0 and 25° C. Dimethylsulfide is added to the TFA after the introduction of methionine (Met) to suppress possible S-alkylation. After removal of the alpha-amino protecting group, the remaining protected amino acids are coupled stepwise in the required order to obtain the desired sequence.
Various activating agents can be used for the coupling reactions including DCC, N,N′-diisopropyl-carbodiimide, benzotriazol-1-yl-oxy-tris-(dimethylamino)-phosphonium hexa-fluorophosphate (BOP) and DCC-hydroxybenzotriazole (HOBt). Each protected amino acid is used in excess (>2.0 equivalents), and the couplings are usually carried out in N-methylpyrrolidone (NMP) or in DMF, CH2Cl2 or mixtures thereof. The extent of completion of the coupling reaction is monitored at each stage, e.g., by the ninhydrin reaction as described by Kaiser et al., 1970, Anal. Biochem. 34: 595. In cases where incomplete coupling is found, the coupling reaction is repeated. The coupling reactions can be performed automatically with commercially available instruments.
After the entire assembly of the desired polypeptide, the polypeptide-resin is cleaved with a reagent such as liquid HF for 1-2 hours at 0° C., which cleaves the polypeptide from the resin and removes all side-chain protecting groups. A scavenger such as anisole is usually used with the liquid HF to prevent cations formed during the cleavage from alkylating the amino acid residues present in the polypeptide. The polypeptide-resin may be deprotected with TFA/dithioethane prior to cleavage if desired.
Side-chain to side-chain cyclization on the solid support requires the use of an orthogonal protection scheme which enables selective cleavage of the side-chain functions of acidic amino acids (e.g., Asp) and the basic amino acids (e.g., Lys). The 9-fluorenylmethyl (Fm) protecting group for the side-chain of Asp and the 9-fluorenylmethyloxycarbonyl (Fmoc) protecting group for the side-chain of Lys can be used for this purpose. In these cases, the side-chain protecting groups of the Boc-protected polypeptide-resin are selectively removed with piperidine in DMF. Cyclization is achieved on the solid support using various activating agents including DCC, DCC/HOBt or BOP. The HF reaction is carried out on the cyclized polypeptide-resin as described above.
Methods for polypeptide purification are well-known in the art, including, without limitation, preparative disc-gel electrophoresis, isoelectric focusing, HPLC, reversed-phase HPLC, gel filtration, ion exchange and partition chromatography, and countercurrent distribution. For some purposes, it is preferable to produce the polypeptide in a recombinant system in which the S. pneumoniae protein contains an additional sequence tag that facilitates purification, such as, but not limited to, a polyhistidine sequence. The polypeptide can then be purified from a crude lysate of the host cell by chromatography on an appropriate solid-phase matrix. Alternatively, antibodies produced against a S. pneumoniae protein or against peptides derived therefrom can be used as purification reagents. Other purification methods are possible.
The present invention also encompasses derivatives and homologues of S. pneumoniae-encoded polypeptides. For some purposes, nucleic acid sequences encoding the peptides may be altered by substitutions, additions, or deletions that provide for functionally equivalent molecules, i.e., function-conservative variants. For example, one or more amino acid residues within the sequence can be substituted by another amino acid of similar properties, such as, for example, positively charged amino acids (arginine, lysine, and histidine); negatively charged amino acids (aspartate and glutamate); polar neutral amino acids; and non-polar amino acids. The isolated polypeptides may be modified by, for example, phosphorylation, sulfation, acylation, or other protein modifications. They may also be modified with a label capable of providing a detectable signal, either directly or indirectly, including, but not limited to, radioisotopes and fluorescent compounds.
Agents.
To identify S. pneumoniae-derived polypeptides for use in the present invention, essentially the complete genomic sequence of a virulent, methicillin-resistant isolate of Streptococcus pneumoniae isolate was analyzed. While, in very rare instances, a nucleic acid sequencing error may be revealed, resolving a rare sequencing error is well within the art, and such an occurrence will not prevent one skilled in the art from practicing the invention.
Also encompassed are any S. pneumoniae polypeptide sequences that are contained within the open reading frames (ORFs), including complete protein-coding sequences, of which any of SEQ ID NO: 2662-SEQ ID NO: 5322 forms a part. Table 2, which is appended herewith and which forms part of the present specification, provides a putative identification of the particular function of a polypeptide which is encoded by each ORF. As a result, one skilled in the art can use the polypeptides of the present invention for commercial and industrial purposes consistent with the type of putative identification of the polypeptide.
The present invention provides a library of S. Pneumoniae-derived polypeptide sequences, and a corresponding library of nucleic acid sequences encoding the polypeptides, wherein the polypeptides themselves, or polypeptides contained within ORFs of which they form a part, comprise sequences that are contemplated for use as components of vaccines. Non-limiting examples of such sequences are listed by SEQ ID NO in Table 2, which is appended herewith and which forms part of the present specification.
The present invention also provides a library of S. pneumoniae-derived polypeptide sequences, and a corresponding library of nucleic acid sequences encoding the polypeptides, wherein the polypeptides themselves, or polypeptides contained within ORFs of which they form a part, comprise sequences lacking homology to any known prokaryotic or eukaryotic sequences. Such libraries provide probes, primers, and markers which can be used to diagnose S. pneumoniae infection, including use as markers in epidemiological studies. Non-limiting examples of such sequences are listed by SEQ ID NO in Table 2, which is appended.
The present invention also provides a library of S. pneumoniae-derived polypeptide sequences, and a corresponding library of nucleic acid sequences encoding the polypeptides, wherein the polypeptides themselves, or polypeptides contained within ORFs of which they form a part, comprise targets for therapeutic drugs.
Specific Example: Determination of Candidate Protein Antigens for Antibody and Vaccine Development
The selection of candidate protein antigens for vaccine development can be derived from the nucleic acids encoding S. pneumoniae polypeptides. First, the ORF's can be analyzed for homology to other known exported or membrane proteins and analyzed using the discriminant analysis described by Klein, et al. (Klein, P., Kanehsia, M., and DeLisi, C. (1985) Biochimica et Biophysica Acta 815, 468-476) for predicting exported and membrane proteins.
Homology searches can be performed using the BLAST algorithm contained in the Wisconsin Sequence Analysis Package (Genetics Computer Group, University Research Park, 575 Science Drive, Madison, Wis. 53711) to compare each predicted ORF amino acid sequence with all sequences found in the current GenBank, SWISS-PROT and PIR databases. BLAST searches for local alignments between the ORF and the databank sequences and reports a probability score which indicates the probability of finding this sequence by chance in the database. ORF's with significant homology (e.g. probabilities lower than 1×10−6 that the homology is only due to random chance) to membrane or exported proteins represent protein antigens for vaccine development. Possible functions can be provided to S. pneumoniae genes based on sequence homology to genes cloned in other organisms.
Discriminant analysis (Klein, et al. supra) can be used to examine the ORF amino acid sequences. This algorithm uses the intrinsic information contained in the ORF amino acid sequence and compares it to information derived from the properties of known membrane and exported proteins. This comparison predicts which proteins will be exported, membrane associated or cytoplasmic. ORF amino acid sequences identified as exported or membrane associated by this algorithm are likely protein antigens for vaccine development.
Production of Fragments and Analogs of S. pneumoniae Nucleic Acids and Polypeptides
Based on the discovery of the S. pneumoniae gene products of the invention provided in the Sequence Listing, one skilled in the art can alter the disclosed structure (of S. pneumoniae genes), e.g., by producing fragments or analogs, and test the newly produced structures for activity. Examples of techniques known to those skilled in the relevant art which allow the production and testing of fragments and analogs are discussed below. These, or analogous methods can be used to make and screen libraries of polypeptides, e.g., libraries of random peptides or libraries of fragments or analogs of cellular proteins for the ability to bind S. pneumoniae polypeptides. Such screens are useful for the identification of inhibitors of S. pneumoniae.
Generation of Fragments
Fragments of a protein can be produced in several ways, e.g., recombinantly, by proteolytic digestion, or by chemical synthesis. Internal or terminal fragments of a polypeptide can be generated by removing one or more nucleotides from one end (for a terminal fragment) or both ends (for an internal fragment) of a nucleic acid which encodes the polypeptide. Expression of the mutagenized DNA produces polypeptide fragments. Digestion with “end-nibbling” endonucleases can thus generate DNA's which encode an array of fragments. DNA's which encode fragments of a protein can also be generated by random shearing, restriction digestion or a combination of the above-discussed methods.
Fragments can also be chemically synthesized using techniques known in the art such as conventional Merrifield solid phase f-Moc or t-Boc chemistry. For example, peptides of the present invention may be arbitrarily divided into fragments of desired length with no overlap of the fragments, or divided into overlapping fragments of a desired length.
Alteration of Nucleic Acids and Polypeptides: Random Methods
Amino acid sequence variants of a protein can be prepared by random mutagenesis of DNA which encodes a protein or a particular domain or region of a protein. Useful methods include PCR mutagenesis and saturation mutagenesis. A library of random amino acid sequence variants can also be generated by the synthesis of a set of degenerate oligonucleotide sequences. (Methods for screening proteins in a library of variants are elsewhere herein).
PCR Mutagenesis
In PCR mutagenesis, reduced Taq polymerase fidelity is used to introduce random mutations into a cloned fragment of DNA (Leung et al., 1989, Technique 1: 11-15). The DNA region to be mutagenized is amplified using the polymerase chain reaction (PCR) under conditions that reduce the fidelity of DNA synthesis by Taq DNA polymerase, e.g., by using a dGTP/dATP ratio of five and adding Mn2+ to the PCR reaction. The pool of amplified DNA fragments are inserted into appropriate cloning vectors to provide random mutant libraries.
Saturation Mutagenesis
Saturation mutagenesis allows for the rapid introduction of a large number of single base substitutions into cloned DNA fragments (Mayers et al., 1985, Science 229: 242). This technique includes generation of mutations, e.g., by chemical treatment or irradiation of single-stranded DNA in vitro, and synthesis of a complimentary DNA strand. The mutation frequency can be modulated by modulating the severity of the treatment, and essentially all possible base substitutions can be obtained. Because this procedure does not involve a genetic selection for mutant fragments both neutral substitutions, as well as those that alter function, are obtained. The distribution of point mutations is not biased toward conserved sequence elements.
Degenerate Oligonucleotides
A library of homologs can also be generated from a set of degenerate oligonucleotide sequences. Chemical synthesis of a degenerate sequences can be carried out in an automatic DNA synthesizer, and the synthetic genes then ligated into an appropriate expression vector. The synthesis of degenerate oligonucleotides is known in the art (see for example, Narang, S A (1983) Tetrahedron 39: 3; Itakura et al. (1981) Recombinant DNA, Proc 3rd Cleveland Sympos. Macromolecules, ed. A G Walton, Amsterdam: Elsevier pp 273-289; Itakura et al. (1984) Annu. Rev. Biochem. 53: 323; Itakura et al. (1984) Science 198: 1056; Ike et al. (1983) Nucleic Acid Res. 11: 477. Such techniques have been employed in the directed evolution of other proteins (see, for example, Scott et al. (1990) Science 249: 386-390; Roberts et al. (1992) PNAS 89: 2429-2433; Devlin et al. (1990) Science 249: 404-406; Cwirla et al. (1990) PNAS 87: 6378-6382; as well as U.S. Pat. Nos. 5,223,409, 5,198,346, and 5,096,815).
Alteration of Nucleic Acids and Polypeptides: Methods for Directed Mutagenesis
Non-random or directed, mutagenesis techniques can be used to provide specific sequences or mutations in specific regions. These techniques can be used to create variants which include, e.g., deletions, insertions, or substitutions, of residues of the known amino acid sequence of a protein. The sites for mutation can be modified individually or in series, e.g., by (1) substituting first with conserved amino acids and then with more radical choices depending upon results achieved, (2) deleting the target residue, or (3) inserting residues of the same or a different class adjacent to the located site, or combinations of options 1-3.
Alanine Scanning Mutagenesis
Alanine scanning mutagenesis is a useful method for identification of certain residues or regions of the desired protein that are preferred locations or domains for mutagenesis, Cunningham and Wells (Science 244: 1081-1085, 1989). In alanine scanning, a residue or group of target residues are identified (e.g., charged residues such as Arg, Asp, His, Lys, and Glu) and replaced by a neutral or negatively charged amino acid (most preferably alanine or polyalanine). Replacement of an amino acid can affect the interaction of the amino acids with the surrounding aqueous environment in or outside the cell. Those domains demonstrating functional sensitivity to the substitutions are then refined by introducing further or other variants at or for the sites of substitution. Thus, while the site for introducing an amino acid sequence variation is predetermined, the nature of the mutation per se need not be predetermined. For example, to optimize the performance of a mutation at a given site, alanine scanning or random mutagenesis may be conducted at the target codon or region and the expressed desired protein subunit variants are screened for the optimal combination of desired activity.
Oligonucleotide-Mediated Mutagenesis
Oligonucleotide-mediated mutagenesis is a useful method for preparing substitution, deletion, and insertion variants of DNA, see, e.g., Adelman et al., (DNA 2: 183, 1983). Briefly, the desired DNA is altered by hybridizing an oligonucleotide encoding a mutation to a DNA template, where the template is the single-stranded form of a plasmid or bacteriophage containing the unaltered or native DNA sequence of the desired protein. After hybridization, a DNA polymerase is used to synthesize an entire second complementary strand of the template that will thus incorporate the oligonucleotide primer, and will code for the selected alteration in the desired protein DNA. Generally, oligonucleotides of at least 25 nucleotides in length are used. An optimal oligonucleotide will have 12 to 15 nucleotides that are completely complementary to the template on either side of the nucleotide(s) coding for the mutation. This ensures that the oligonucleotide will hybridize properly to the single-stranded DNA template molecule. The oligonucleotides are readily synthesized using techniques known in the art such as that described by Crea et al. (Proc. Natl. Acad. Sci. USA, 75: 5765 [1978]).
Cassette Mutagenesis
Another method for preparing variants, cassette mutagenesis, is based on the technique described by Wells et al. (Gene, 34: 315 [1985]). The starting material is a plasmid (or other vector) which includes the protein subunit DNA to be mutated. The codon(s) in the protein subunit DNA to be mutated are identified. There must be a unique restriction endonuclease site on each side of the identified mutation site(s). If no such restriction sites exist, they may be generated using the above-described oligonucleotide-mediated mutagenesis method to introduce them at appropriate locations in the desired protein subunit DNA. After the restriction sites have been introduced into the plasmid, the plasmid is cut at these sites to linearize it. A double-stranded oligonucleotide encoding the sequence of the DNA between the restriction sites but containing the desired mutation(s) is synthesized using standard procedures. The two strands are synthesized separately and then hybridized together using standard techniques. This double-stranded oligonucleotide is referred to as the cassette. This cassette is designed to have 3′ and 5′ ends that are comparable with the ends of the linearized plasmid, such that it can be directly ligated to the plasmid. This plasmid now contains the mutated desired protein subunit DNA sequence.
Combinatorial Mutagenesis
Combinatorial mutagenesis can also be used to generate mutants (Ladner et al., WO 88/06630). In this method, the amino acid sequences for a group of homologs or other related proteins are aligned, preferably to promote the highest homology possible. All of the amino acids which appear at a given position of the aligned sequences can be selected to create a degenerate set of combinatorial sequences. The variegated library of variants is generated by combinatorial mutagenesis at the nucleic acid level, and is encoded by a variegated gene library. For example, a mixture of synthetic oligonucleotides can be enzymatically ligated into gene sequences such that the degenerate set of potential sequences are expressible as individual peptides, or alternatively, as a set of larger fusion proteins containing the set of degenerate sequences.
Other Modifications of S. pneumoniae Nucleic Acids and Polypeptides
It is possible to modify the structure of an S. pneumoniae polypeptide for such purposes as increasing solubility, enhancing stability (e.g., shelf life ex vivo and resistance to proteolytic degradation in vivo). A modified S. pneumoniae protein or peptide can be produced in which the amino acid sequence has been altered, such as by amino acid substitution, deletion, or addition as described herein.
An S. pneumoniae peptide can also be modified by substitution of cysteine residues preferably with alanine, serine, threonine, leucine or glutamic acid residues to minimize dimerization via disulfide linkages. In addition, amino acid side chains of fragments of the protein of the invention can be chemically modified. Another modification is cyclization of the peptide.
In order to enhance stability and/or reactivity, an S. pneumoniae polypeptide can be modified to incorporate one or more polymorphisms in the amino acid sequence of the protein resulting from any natural allelic variation. Additionally, D-amino acids, non-natural amino acids, or non-amino acid analogs can be substituted or added to produce a modified protein within the scope of this invention. Furthermore, an S. pneumoniae polypeptide can be modified using polyethylene glycol (PEG) according to the method of A. Sehon and co-workers (Wie et al., supra) to produce a protein conjugated with PEG. In addition, PEG can be added during chemical synthesis of the protein. Other modifications of S. pneumoniae proteins include reduction/alkylation (Tarr, Methods of Protein Microcharacterization, J. E. Silver ed., Humana Press, Clifton N.J. 155-194 (1986)); acylation (Tarr, supra); chemical coupling to an appropriate carrier (Mishell and Shiigi, eds, Selected Methods in Cellular Immunology, WH Freeman, San Francisco, Calif. (1980), U.S. Pat. No. 4,939,239; or mild formalin treatment (Marsh, (1971) Int. Arch. of Allergy and Appl. Immunol, 41: 199-215).
To facilitate purification and potentially increase solubility of an S. pneumoniae protein or peptide, it is possible to add an amino acid fusion moiety to the peptide backbone. For example, hexa-histidine can be added to the protein for purification by immobilized metal ion affinity chromatography (Hochuli, E. et al., (1988) Bio/Technology, 6: 1321-1325). In addition, to facilitate isolation of peptides free of irrelevant sequences, specific endoprotease cleavage sites can be introduced between the sequences of the fusion moiety and the peptide.
To potentially aid proper antigen processing of epitopes within an S. pneumoniae polypeptide, canonical protease sensitive sites can be engineered between regions, each comprising at least one epitope via recombinant or synthetic methods. For example, charged amino acid pairs, such as KK or RR, can be introduced between regions within a protein or fragment during recombinant construction thereof. The resulting peptide can be rendered sensitive to cleavage by cathepsin and/or other trypsin-like enzymes which would generate portions of the protein containing one or more epitopes. In addition, such charged amino acid residues can result in an increase in the solubility of the peptide.
Primary Methods for Screening Polypeptides and Analogs
Various techniques are known in the art for screening generated mutant gene products. Techniques for screening large gene libraries often include cloning the gene library into replicable expression vectors, transforming appropriate cells with the resulting library of vectors, and expressing the genes under conditions in which detection of a desired activity, e.g., in this case, binding to S. pneumoniae polypeptide or an interacting protein, facilitates relatively easy isolation of the vector encoding the gene whose product was detected. Each of the techniques described below is amenable to high through-put analysis for screening large numbers of sequences created, e.g., by random mutagenesis techniques.
Two Hybrid Systems
Two hybrid assays such as the system described above (as with the other screening methods described herein), can be used to identify polypeptides, e.g., fragments or analogs of a naturally-occurring S. pneumoniae polypeptide, e.g., of cellular proteins, or of randomly generated polypeptides which bind to an S. pneumoniae protein. (The S. pneumoniae domain is used as the bait protein and the library of variants are expressed as prey fusion proteins.) In an analogous fashion, a two hybrid assay (as with the other screening methods described herein), can be used to find polypeptides which bind a S. pneumoniae polypeptide.
Display Libraries
In one approach to screening assays, the candidate peptides are displayed on the surface of a cell or viral particle, and the ability of particular cells or viral particles to bind an appropriate receptor protein via the displayed product is detected in a “panning assay”. For example, the gene library can be cloned into the gene for a surface membrane protein of a bacterial cell, and the resulting fusion protein detected by panning (Ladner et al., WO 88/06630; Fuchs et al. (1991) Bio/Technology 9: 1370-1371; and Goward et al. (1992) TIBS 18: 136-140). In a similar fashion, a detectably labeled ligand can be used to score for potentially functional peptide homologs. Fluorescently labeled ligands, e.g., receptors, can be used to detect homologs which retain ligand-binding activity. The use of fluorescently labeled ligands, allows cells to be visually inspected and separated under a fluorescence microscope, or, where the morphology of the cell permits, to be separated by a fluorescence-activated cell sorter.
A gene library can be expressed as a fusion protein on the surface of a viral particle. For instance, in the filamentous phage system, foreign peptide sequences can be expressed on the surface of infectious phage, thereby conferring two significant benefits. First, since these phage can be applied to affinity matrices at concentrations well over 1013 phage per milliliter, a large number ofphage can be screened at one time. Second, since each infectious phage displays a gene product on its surface, if a particular phage is recovered from an affinity matrix in low yield, the phage can be amplified by another round of infection. The group of almost identical E. coli filamentous phages M13, fd., and f1 are most often used in phage display libraries. Either of the phage gIII or gVIII coat proteins can be used to generate fusion proteins without disrupting the ultimate packaging of the viral particle. Foreign epitopes can be expressed at the NH2-terminal end of pIII and phage bearing such epitopes recovered from a large excess of phage lacking this epitope (Ladner et al. PCT publication WO 90/02909; Garrard et al., PCT publication WO 92/09690; Marks et al. (1992) J. Biol. Chem. 267: 16007-16010; Griffiths et al. (1993) EMBO J. 12: 725-734; Clackson et al. (1991) Nature 352: 624-628; and Barbas et al. (1992) PNAS 89: 4457-4461).
A common approach uses the maltose receptor of E. coli (the outer membrane protein, LamB) as a peptide fusion partner (Charbit et al. (1986) EMBO 5, 3029-3037). Oligonucleotides have been inserted into plasmids encoding the LamB gene to produce peptides fused into one of the extracellular loops of the protein. These peptides are available for binding to ligands, e.g., to antibodies, and can elicit an immune response when the cells are administered to animals. Other cell surface proteins, e.g., OmpA (Schorr et al. (1991) Vaccines 91, pp. 387-392), PhoE (Agterberg, et al. (1990) Gene 88, 37-45), and PAL (Fuchs et al. (1991) Bio/Tech 9, 1369-1372), as well as large bacterial surface structures have served as vehicles for peptide display. Peptides can be fused to pilin, a protein which polymerizes to form the pilus-a conduit for interbacterial exchange of genetic information (Thiry et al. (1989) Appl. Environ. Microbiol. 55, 984-993). Because of its role in interacting with other cells, the pilus provides a useful support for the presentation of peptides to the extracellular environment. Another large surface structure used for peptide display is the bacterial motive organ, the flagellum. Fusion of peptides to the subunit protein flagellin offers a dense array of many peptide copies on the host cells (Kuwajima et al. (1988) Bio/Tech. 6, 1080-1083). Surface proteins of other bacterial species have also served as peptide fusion partners. Examples include the Staphylococcus protein A and the outer membrane IgA protease of Neisseria (Hansson et al. (1992) J. Bacteriol. 174, 4239-4245 and Klauser et al. (1990) EMBO J. 9, 1991-1999).
In the filamentous phage systems and the LamB system described above, the physical link between the peptide and its encoding DNA occurs by the containment of the DNA within a particle (cell or phage) that carries the peptide on its surface. Capturing the peptide captures the particle and the DNA within. An alternative scheme uses the DNA-binding protein LacI to form a link between peptide and DNA (Cull et al. (1992) PNAS USA 89: 1865-1869). This system uses a plasmid containing the LacI gene with an oligonucleotide cloning site at its 3′-end. Under the controlled induction by arabinose, a LacI-peptide fusion protein is produced. This fusion retains the natural ability of LacI to bind to a short DNA sequence known as LacO operator (LacO). By installing two copies of LacO on the expression plasmid, the LacI-peptide fusion binds tightly to the plasmid that encoded it. Because the plasmids in each cell contain only a single oligonucleotide sequence and each cell expresses only a single peptide sequence, the peptides become specifically and stablely associated with the DNA sequence that directed its synthesis. The cells of the library are gently lysed and the peptide-DNA complexes are exposed to a matrix of immobilized receptor to recover the complexes containing active peptides. The associated plasmid DNA is then reintroduced into cells for amplification and DNA sequencing to determine the identity of the peptide ligands. As a demonstration of the practical utility of the method, a large random library of dodecapeptides was made and selected on a monoclonal antibody raised against the opioid peptide dynorphin B. A cohort of peptides was recovered, all related by a consensus sequence corresponding to a six-residue portion of dynorphin B. (Cull et al. (1992) Proc. Natl. Acad. Sci. U.S.A. 89-1869).
This scheme, sometimes referred to as peptides-on-plasmids, differs in two important ways from the phage display methods. First, the peptides are attached to the C-terminus of the fusion protein, resulting in the display of the library members as peptides having free carboxy termini. Both of the filamentous phage coat proteins, pIII and pVIII, are anchored to the phage through their C-termini, and the guest peptides are placed into the outward-extending N-terminal domains. In some designs, the phage-displayed peptides are presented right at the amino terminus of the fusion protein. (Cwirla, et al. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 6378-6382) A second difference is the set of biological biases affecting the population of peptides actually present in the libraries. The LacI fusion molecules are confined to the cytoplasm of the host cells. The phage coat fusions are exposed briefly to the cytoplasm during translation but are rapidly secreted through the inner membrane into the periplasmic compartment, remaining anchored in the membrane by their C-terminal hydrophobic domains, with the N-termini, containing the peptides, protruding into the periplasm while awaiting assembly into phage particles. The peptides in the LacI and phage libraries may differ significantly as a result of their exposure to different proteolytic activities. The phage coat proteins require transport across the inner membrane and signal peptidase processing as a prelude to incorporation into phage. Certain peptides exert a deleterious effect on these processes and are underrepresented in the libraries (Gallop et al. (1994) J. Med. Chem. 37(9): 1233-1251). These particular biases are not a factor in the Lac display system.
The number of small peptides available in recombinant random libraries is enormous. Libraries of 107-109 independent clones are routinely prepared. Libraries as large as 1011 recombinants have been created, but this size approaches the practical limit for clone libraries. This limitation in library size occurs at the step of transforming the DNA containing randomized segments into the host bacterial cells. To circumvent this limitation, an in vitro system based on the display of nascent peptides in polysome complexes has recently been developed. This display library method has the potential of producing libraries 3-6 orders of magnitude larger than the currently available phage/phagemid or plasmid libraries. Furthermore, the construction of the libraries, expression of the peptides, and screening, is done in an entirely cell-free format.
In one application of this method (Gallop et al. (1994) J. Med. Chem. 37(9): 1233-1251), a molecular DNA library encoding 1012 decapeptides was constructed and the library expressed in an E. coli S30 in vitro coupled transcription/translation system. Conditions were chosen to stall the ribosomes on the mRNA, causing the accumulation of a substantial proportion of the RNA in polysomes and yielding complexes containing nascent peptides still linked to their encoding RNA. The polysomes are sufficiently robust to be affinity purified on immobilized receptors in much the same way as the more conventional recombinant peptide display libraries are screened. RNA from the bound complexes is recovered, converted to cDNA, and amplified by PCR to produce a template for the next round of synthesis and screening. The polysome display method can be coupled to the phage display system. Following several rounds of screening, cDNA from the enriched pool of polysomes was cloned into a phagemid vector. This vector serves as both a peptide expression vector, displaying peptides fused to the coat proteins, and as a DNA sequencing vector for peptide identification. By expressing the polysome-derived peptides on phage, one can either continue the affinity selection procedure in this format or assay the peptides on individual clones for binding activity in a phage ELISA, or for binding specificity in a completion phage ELISA (Barret, et al. (1992) Anal. Biochem 204, 357-364). To identify the sequences of the active peptides one sequences the DNA produced by the phagemid host.
Secondary Screening of Polypeptides and Analogs
The high through-put assays described above can be followed by secondary screens in order to identify further biological activities which will, e.g., allow one skilled in the art to differentiate agonists from antagonists. The type of a secondary screen used will depend on the desired activity that needs to be tested. For example, an assay can be developed in which the ability to inhibit an interaction between a protein of interest and its respective ligand can be used to identify antagonists from a group of peptide fragments isolated though one of the primary screens described above.
Therefore, methods for generating fragments and analogs and testing them for activity are known in the art. Once the core sequence of interest is identified, it is routine for one skilled in the art to obtain analogs and fragments.
Peptide Mimetics of S. pneumoniae Polypeptides
The invention also provides for reduction of the protein binding domains of the subject S. pneumoniae polypeptides to generate mimetics, e.g. peptide or non-peptide agents. The peptide mimetics are able to disrupt binding of a polypeptide to its counter ligand, e.g., in the case of an S. pneumoniae polypeptide binding to a naturally occurring ligand. The critical residues of a subject S. pneumoniae polypeptide which are involved in molecular recognition of a polypeptide can be determined and used to generate S. pneumoniae-derived peptidomimetics which competitively or noncompetitively inhibit binding of the S. pneumoniae polypeptide with an interacting polypeptide (see, for example, European patent applications EP-412,762A and EP-B31,080A).
For example, scanning mutagenesis can be used to map the amino acid residues of a particular S. pneumoniae polypeptide involved in binding an interacting polypeptide, peptidomimetic compounds (e.g. diazepine or isoquinoline derivatives) can be generated which mimic those residues in binding to an interacting polypeptide, and which therefore can inhibit binding of an S. pneumoniae polypeptide to an interacting polypeptide and thereby interfere with the function of S. pneumoniae polypeptide. For instance, non-hydrolyzable peptide analogs of such residues can be generated using benzodiazepine (e.g., see Freidinger et al. in Peptides: Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden, Netherlands, 1988), azepine (e.g., see Huffman et al. in Peptides: Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden, Netherlands, 1988), substituted gama lactam rings (Garvey et al. in Peptides: Chemistry and Biology, G. R. Marshall ed., ESCOM Publisher: Leiden, Netherlands, 1988), keto-methylene pseudopeptides (Ewenson et al. (1986) J Med Chem 29: 295; and Ewenson et al. in Peptides: Structure and Function (Proceedings of the 9th American Peptide Symposium) Pierce Chemical Co. Rockland, Ill., 1985), b-turn dipeptide cores (Nagai et al. (1985) Tetrahedron Lett 26: 647; and Sato et al. (1986) J Chem Soc Perkin Trans 1: 1231), and b-aminoalcohols (Gordon et al. (1985) Biochem Biophys Res Commun 126: 419; and et al. (1986) Biochem Biophys Res Commun 134: 71).
Vaccine Formulations for S. pneumoniae Nucleic Acids and Polypeptides
This invention also features vaccine compositions for protection against infection by S. pneumoniae or for treatment of S. pneumoniae infection, a gram-negative spiral microaerophilic bacterium. In one embodiment, the vaccine compositions contain one or more immunogenic components such as a surface protein from S. pneumoniae, or portion thereof, and a pharmaceutically acceptable carrier. Nucleic acids within the scope of the invention are exemplified by the nucleic acids of the invention contained in the Sequence Listing which encode S. pneumoniae surface proteins. Any nucleic acid encoding an immunogenic S. pneumoniae protein, or portion thereof, which is capable of expression in a cell, can be used in the present invention. These vaccines have therapeutic and prophylactic utilities.
One aspect of the invention provides a vaccine composition for protection against infection by S. pneumoniae which contains at least one immunogenic fragment of an S. pneumoniae protein and a pharmaceutically acceptable carrier. Preferred fragments include peptides of at least about 10 amino acid residues in length, preferably about 10-20 amino acid residues in length, and more preferably about 12-16 amino acid residues in length.
Immunogenic components of the invention can be obtained, for example, by screening polypeptides recombinantly produced from the corresponding fragment of the nucleic acid encoding the full-length S. pneumoniae protein. In addition, fragments can be chemically synthesized using techniques known in the art such as conventional Merrifield solid phase f-Moc or t-Boc chemistry.
In one embodiment, immunogenic components are identified by the ability of the peptide to stimulate T cells. Peptides which stimulate T cells, as determined by, for example, T cell proliferation or cytokine secretion are defined herein as comprising at least one T cell epitope. T cell epitopes are believed to be involved in initiation and perpetuation of the immune response to the protein allergen which is responsible for the clinical symptoms of allergy. These T cell epitopes are thought to trigger early events at the level of the T helper cell by binding to an appropriate HLA molecule on the surface of an antigen presenting cell, thereby stimulating the T cell subpopulation with the relevant T cell receptor for the epitope. These events lead to T cell proliferation, lymphokine secretion, local inflammatory reactions, recruitment of additional immune cells to the site of antigen/T cell interaction, and activation of the B cell cascade, leading to the production of antibodies. A T cell epitope is the basic element, or smallest unit of recognition by a T cell receptor, where the epitope comprises amino acids essential to receptor recognition (e.g., approximately 6 or 7 amino acid residues). Amino acid sequences which mimic those of the T cell epitopes are within the scope of this invention.
Screening immunogenic components can be accomplished using one or more of several different assays. For example, in vitro, peptide T cell stimulatory activity is assayed by contacting a peptide known or suspected of being immunogenic with an antigen presenting cell which presents appropriate MHC molecules in a T cell culture. Presentation of an immunogenic S. pneumoniae peptide in association with appropriate MHC molecules to T cells in conjunction with the necessary co-stimulation has the effect of transmitting a signal to the T cell that induces the production of increased levels of cytokines, particularly of interleukin-2 and interleukin-4. The culture supernatant can be obtained and assayed for interleukin-2 or other known cytokines. For example, any one of several conventional assays for interleukin-2 can be employed, such as the assay described in Proc. Natl. Acad. Sci USA, 86: 1333 (1989) the pertinent portions of which are incorporated herein by reference. A kit for an assay for the production of interferon is also available from Genzyme Corporation (Cambridge, Mass.).
Alternatively, a common assay for T cell proliferation entails measuring tritiated thymidine incorporation. The proliferation of T cells can be measured in vitro by determining the amount of 3H-labeled thymidine incorporated into the replicating DNA of cultured cells. Therefore, the rate of DNA synthesis and, in turn, the rate of cell division can be quantified.
Vaccine compositions of the invention containing immunogenic components (e.g., S. pneumoniae polypeptide or fragment thereof or nucleic acid encoding an S. pneumoniae polypeptide or fragment thereof) preferably include a pharmaceutically acceptable carrier. The term “pharmaceutically acceptable carrier” refers to a carrier that does not cause an allergic reaction or other untoward effect in patients to whom it is administered. Suitable pharmaceutically acceptable carriers include, for example, one or more of water, saline, phosphate buffered saline, dextrose, glycerol, ethanol and the like, as well as combinations thereof. Pharmaceutically acceptable carriers may further comprise minor amounts of auxiliary substances such as wetting or emulsifying agents, preservatives or buffers, which enhance the shelf life or effectiveness of the antibody. For vaccines of the invention containing S. pneumoniae polypeptides, the polypeptide is co-administered with a suitable adjuvant.
It will be apparent to those of skill in the art that the therapeutically effective amount of DNA or protein of this invention will depend, inter alia, upon the administration schedule, the unit dose of antibody administered, whether the protein or DNA is administered in combination with other therapeutic agents, the immune status and health of the patient, and the therapeutic activity of the particular protein or DNA.
Vaccine compositions are conventionally administered parenterally, e.g., by injection, either subcutaneously or intramuscularly. Methods for intramuscular immunization are described by Wolff et al. (1990) Science 247: 1465-1468 and by Sedegah et al. (1994) Immunology 91: 9866-9870. Other modes of administration include oral and pulmonary formulations, suppositories, and transdermal applications. Oral immunization is preferred over parenteral methods for inducing protection against infection by S. pneumoniae. Cain et. al. (1993) Vaccine 11: 637-642. Oral formulations include such normally employed excipients as, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharine, cellulose, magnesium carbonate, and the like.
The vaccine compositions of the invention can include an adjuvant, including, but not limited to aluminum hydroxide; N-acetyl-muramyl-L-threonyl-D-isoglutamine (thr-MDP); N-acetyl-nor-muramyl-L-alanyl-D-isoglutamine (CGP 11637, referred to as nor-MDP); N-acetylmuramyl-L-alanyl-D-isoglutaminyl-L-alanine-2-(1′-2′-dipalmitoyl-sn-glycero-3-hydroxyphos-phoryloxy)-ethylamine (CGP 19835A, referred to a MTP-PE); RIBI, which contains three components from bacteria; monophosphoryl lipid A; trehalose dimycoloate; cell wall skeleton (MPL+TDM+CWS) in a 2% squalene/Tween 80 emulsion; and cholera toxin. Others which may be used are non-toxic derivatives of cholera toxin, including its B subunit, and/or conjugates or genetically engineered fusions of the S. pneumoniae polypeptide with cholera toxin or its B subunit, procholeragenoid, fungal polysaccharides, including schizophyllan, muramyl dipeptide, muramyl dipeptide derivatives, phorbol esters, labile toxin of E. coli, non-S. pneumoniae bacterial lysates, block polymers or saponins.
Other suitable delivery methods include biodegradable microcapsules or immuno-stimulating complexes (ISCOMs), cochleates, or liposomes, genetically engineered attenuated live vectors such as viruses or bacteria, and recombinant (chimeric) virus-like particles, e.g., bluetongue. The amount of adjuvant employed will depend on the type of adjuvant used. For example, when the mucosal adjuvant is cholera toxin, it is suitably used in an amount of 5 mg to 50 mg, for example 10 mg to 35 mg. When used in the form of microcapsules, the amount used will depend on the amount employed in the matrix of the microcapsule to achieve the desired dosage. The determination of this amount is within the skill of a person of ordinary skill in the art.
Carrier systems in humans may include enteric release capsules protecting the antigen from the acidic environment of the stomach, and including S. pneumoniae polypeptide in an insoluble form as fusion proteins. Suitable carriers for the vaccines of the invention are enteric coated capsules and polylactide-glycolide microspheres. Suitable diluents are 0.2 N NaHCO3 and/or saline.
Vaccines of the invention can be administered as a primary prophylactic agent in adults or in children, as a secondary prevention, after successful eradication of S. pneumoniae in an infected host, or as a therapeutic agent in the aim to induce an immune response in a susceptible host to prevent infection by S. pneumoniae. The vaccines of the invention are administered in amounts readily determined by persons of ordinary skill in the art. Thus, for adults a suitable dosage will be in the range of 10 mg to 10 g, preferably 10 mg to 100 mg. A suitable dosage for adults will also be in the range of 5 mg to 500 mg. Similar dosage ranges will be applicable for children. Those skilled in the art will recognize that the optimal dose may be more or less depending upon the patient's body weight, disease, the route of administration, and other factors. Those skilled in the art will also recognize that appropriate dosage levels can be obtained based on results with known oral vaccines such as, for example, a vaccine based on an E. coli lysate (6 mg dose daily up to total of 540 mg) and with an enterotoxigenic E. coli purified antigen (4 doses of 1 mg) (Schulman et al., J. Urol. 150: 917-921 (1993); Boedecker et al., American Gastroenterological Assoc. 999: A-222 (1993)). The number of doses will depend upon the disease, the formulation, and efficacy data from clinical trials. Without intending any limitation as to the course of treatment, the treatment can be administered over 3 to 8 doses for a primary immunization schedule over 1 month (Boedeker, American Gastroenterological Assoc. 888: A-222 (1993)).
In a preferred embodiment, a vaccine composition of the invention can be based on a killed whole E. coli preparation with an immunogenic fragment of an S. pneumoniae protein of the invention expressed on its surface or it can be based on an E. coli lysate, wherein the killed E. coli acts as a carrier or an adjuvant.
It will be apparent to those skilled in the art that some of the vaccine compositions of the invention are useful only for preventing S. pneumoniae infection, some are useful only for treating S. pneumoniae infection, and some are useful for both preventing and treating S. pneumoniae infection. In a preferred embodiment, the vaccine composition of the invention provides protection against S. pneumoniae infection by stimulating humoral and/or cell-mediated immunity against S. pneumoniae. It should be understood that amelioration of any of the symptoms of S. pneumoniae infection is a desirable clinical goal, including a lessening of the dosage of medication used to treat S. pneumoniae-caused disease, or an increase in the production of antibodies in the serum or mucous of patients.
Antibodies Reactive with S. pneumoniae Polypeptides
The invention also includes antibodies specifically reactive with the subject S. pneumoniae polypeptide. Anti-protein/anti-peptide antisera or monoclonal antibodies can be made by standard protocols (See, for example, Antibodies: A Laboratory Manual ed. by Harlow and Lane (Cold Spring Harbor Press: 1988)). A mammal such as a mouse, a hamster or rabbit can be immunized with an immunogenic form of the peptide. Techniques for conferring immunogenicity on a protein or peptide include conjugation to carriers or other techniques well known in the art. An immunogenic portion of the subject S. pneumoniae polypeptide can be administered in the presence of adjuvant. The progress of immunization can be monitored by detection of antibody titers in plasma or serum. Standard ELISA or other immunoassays can be used with the immunogen as antigen to assess the levels of antibodies.
In a preferred embodiment, the subject antibodies are immunospecific for antigenic determinants of the S. pneumoniae polypeptides of the invention, e.g. antigenic determinants of a polypeptide of the invention contained in the Sequence Listing, or a closely related human or non-human mammalian homolog (e.g., 90% homologous, more preferably at least 95% homologous). In yet a further preferred embodiment of the invention, the anti-S. pneumoniae antibodies do not substantially cross react (i.e., react specifically) with a protein which is for example, less than 80% percent homologous to a sequence of the invention contained in the Sequence Listing. By “not substantially cross react”, it is meant that the antibody has a binding affinity for a non-homologous protein which is less than 10 percent, more preferably less than 5 percent, and even more preferably less than 1 percent, of the binding affinity for a protein of the invention contained in the Sequence Listing. In a most preferred embodiment, there is no cross-reactivity between bacterial and mammalian antigens.
The term antibody as used herein is intended to include fragments thereof which are also specifically reactive with S. pneumoniae polypeptides. Antibodies can be fragmented using conventional techniques and the fragments screened for utility in the same manner as described above for whole antibodies. For example, F(ab′)2 fragments can be generated by treating antibody with pepsin. The resulting F(ab′)2 fragment can be treated to reduce disulfide bridges to produce Fab′ fragments. The antibody of the invention is further intended to include bispecific and chimeric molecules having an anti-S. pneumoniae portion.
Both monoclonal and polyclonal antibodies (Ab) directed against S. pneumoniae polypeptides or S. pneumoniae polypeptide variants, and antibody fragments such as Fab′ and F(ab′)2, can be used to block the action of S. pneumoniae polypeptide and allow the study of the role of a particular S. pneumoniae polypeptide of the invention in aberrant or unwanted intracellular signaling, as well as the normal cellular function of the S. pneumoniae and by microinjection of anti-S. pneumoniae polypeptide antibodies of the present invention.
Antibodies which specifically bind S. pneumoniae epitopes can also be used in immunohistochemical staining of tissue samples in order to evaluate the abundance and pattern of expression of S. pneumoniae antigens. Anti S. pneumoniae polypeptide antibodies can be used diagnostically in immuno-precipitation and immuno-blotting to detect and evaluate S. pneumoniae levels in tissue or bodily fluid as part of a clinical testing procedure. Likewise, the ability to monitor S. pneumoniae polypeptide levels in an individual can allow determination of the efficacy of a given treatment regimen for an individual afflicted with such a disorder. The level of an S. pneumoniae polypeptide can be measured in cells found in bodily fluid, such as in urine samples or can be measured in tissue, such as produced by gastric biopsy. Diagnostic assays using anti-S. pneumoniae antibodies can include, for example, immunoassays designed to aid in early diagnosis of S. pneumoniae infections. The present invention can also be used as a method of detecting antibodies contained in samples from individuals infected by this bacterium using specific S. pneumoniae antigens.
Another application of anti-S. pneumoniae polypeptide antibodies of the invention is in the immunological screening of cDNA libraries constructed in expression vectors such as lgt11, lgt18-23, IZAP, and IORF8. Messenger libraries of this type, having coding sequences inserted in the correct reading frame and orientation, can produce fusion proteins. For instance, lgt11 will produce fusion proteins whose amino termini consist of β-galactosidase amino acid sequences and whose carboxy termini consist of a foreign polypeptide. Antigenic epitopes of a subject S. pneumoniae polypeptide can then be detected with antibodies, as, for example, reacting nitrocellulose filters lifted from infected plates with anti-S. pneumoniae polypeptide antibodies. Phage, scored by this assay, can then be isolated from the infected plate. Thus, the presence of S. pneumoniae gene homologs can be detected and cloned from other species, and alternate isoforms (including splicing variants) can be detected and cloned.
Kits Containing Nucleic Acids, Polypeptides or Antibodies of the Invention
The nucleic acid, polypeptides and antibodies of the invention can be combined with other reagents and articles to form kits. Kits for diagnostic purposes typically comprise the nucleic acid, polypeptides or antibodies in vials or other suitable vessels. Kits typically comprise other reagents for performing hybridization reactions, polymerase chain reactions (PCR), or for reconstitution of lyophilized components, such as aqueous media, salts, buffers, and the like. Kits may also comprise reagents for sample processing such as detergents, chaotropic salts and the like. Kits may also comprise immobilization means such as particles, supports, wells, dipsticks and the like. Kits may also comprise labeling means such as dyes, developing reagents, radioisotopes, fluorescent agents, luminescent or chemiluminescent agents, enzymes, intercalating agents and the like. With the nucleic acid and amino acid sequence information provided herein, individuals skilled in art can readily assemble kits to serve their particular purpose. Kits further can include instructions for use.
Bio Chips and Microarrays
The nucleic acid sequence of the present invention may be used to detect S. pneumoniae or other species of Streptococcus acid sequence using bio chip technology. Bio chips containing arrays of nucleic acid sequence can also be used to measure expression of genes of S. pneumoniae or other species of Streptococcus. For example, to diagnose a patient with a S. pneumoniae or other Streptococcus infection, a sample from a human or animal can be used as a probe on a bio chip containing an array of nucleic acid sequence from the present invention. In addition, a sample from a disease state can be compared to a sample from a non-disease state which would help identify a gene that is up-regulated or expressed in the disease state. This would provide valuable insight as to the mechanism by which the disease manifests. Changes in gene expression can also be used to identify critical pathways involved in drug transport or metabolism, and may enable the identification of novel targets involved in virulence or host cell interactions involved in maintenance of an infection. Procedures using such techniques have been described by Brown et al., 1995, Science 270: 467-470.
Bio chips can also be used to monitor the genetic changes of potential therapeutic compounds including, deletions, insertions or mismatches. Once the therapeutic is added to the patient, changes to the genetic sequence can be evaluated for its efficacy. In addition, the nucleic acid sequence of the present invention can be used to determine essential genes in cell cycling. As described in Iyer et al., 1999 (Science, 283: 83-87) genes essential in the cell cycle can be identified using bio chips. Furthermore, the present invention provides nucleic acid sequence which can be used with bio chip technology to understand regulatory networks in bacteria, measure the response to environmental signals or drugs as in drug screening, and study virulence induction. (Mons et al., 1998, Nature Biotechnology, 16: 45-48. Patents teaching this technology include U.S. Pat. Nos. 5,445,934, 5,744,305, and 5800992.
Drug Screening Assays Using S. pneumoniae Polypeptides
By making available purified and recombinant S. pneumoniae polypeptides, the present invention provides assays which can be used to screen for drugs which are either agonists or antagonists of the normal cellular function, in this case, of the subject S. pneumoniae polypeptides, or of their role in intracellular signaling. Such inhibitors or potentiators may be useful as new therapeutic agents to combat S. pneumoniae infections in humans. A variety of assay formats will suffice and, in light of the present inventions, will be comprehended by the skilled artisan.
In many drug screening programs which test libraries of compounds and natural extracts, high throughput assays are desirable in order to maximize the number of compounds surveyed in a given period of time. Assays which are performed in cell-free systems, such as may be derived with purified or semi-purified proteins, are often preferred as “primary” screens in that they can be generated to permit rapid development and relatively easy detection of an alteration in a molecular target which is mediated by a test compound. Moreover, the effects of cellular toxicity and/or bioavailability of the test compound can be generally ignored in the in vitro system, the assay instead being focused primarily on the effect of the drug on the molecular target as may be manifest in an alteration of binding affinity with other proteins or change in enzymatic properties of the molecular target. Accordingly, in an exemplary screening assay of the present invention, the compound of interest is contacted with an isolated and purified S. pneumoniae polypeptide.
Screening assays can be constructed in vitro with a purified S. pneumoniae polypeptide or fragment thereof, such as an S. pneumoniae polypeptide having enzymatic activity, such that the activity of the polypeptide produces a detectable reaction product. The efficacy of the compound can be assessed by generating dose response curves from data obtained using various concentrations of the test compound. Moreover, a control assay can also be performed to provide a baseline for comparison. Suitable products include those with distinctive absorption, fluorescence, or chemi-luminescence properties, for example, because detection may be easily automated. A variety of synthetic or naturally occurring compounds can be tested in the assay to identify those which inhibit or potentiate the activity of the S. pneumoniae polypeptide. Some of these active compounds may directly, or with chemical alterations to promote membrane permeability or solubility, also inhibit or potentiate the same activity (e.g., enzymatic activity) in whole, live S. pneumoniae cells.
Overexpression Assays
Overexpression assays are based on the premise that overproduction of a protein would lead to a higher level of resistance to compounds that selectively interfere with the function of that protein. Overexpression assays may be used to identify compounds that interfere with the function of virtually any type of protein, including without limitation enzymes, receptors, DNA- or RNA-binding proteins, or any proteins that are directly or indirectly involved in regulating cell growth.
Typically, two bacterial strains are constructed. One contains a single copy of the gene of interest, and a second contains several copies of the same gene. Identification of useful inhibitory compounds of this type of assay is based on a comparison of the activity of a test compound in inhibiting growth and/or viability of the two strains. The method involves constructing a nucleic acid vector that directs high level expression of a particular target nucleic acid. The vectors are then transformed into host cells in single or multiple copies to produce strains that express low to moderate and high levels of protein encoding by the target sequence (strain A and B, respectively). Nucleic acid comprising sequences encoding the target gene can, of course, be directly integrated into the host cell.
Large numbers of compounds (or crude substances which may contain active compounds) are screened for their effect on the growth of the two strains. Agents which interfere with an unrelated target equally inhibit the growth of both strains. Agents which interfere with the function of the target at high concentration should inhibit the growth of both strains. It should be possible, however, to titrate out the inhibitory effect of the compound in the overexpressing strain. That is, if the compound is affecting the particular target that is being tested, it should be possible to inhibit the growth of strain A at a concentration of the compound that allows strain B to grow.
Alternatively, a bacterial strain is constructed that contains the gene of interest under the control of an inducible promoter. Identification of useful inhibitory agents using this type of assay is based on a comparison of the activity of a test compound in inhibiting growth and/or viability of this strain under both inducing and non-inducing conditions. The method involves constructing a nucleic acid vector that directs high-level expression of a particular target nucleic acid. The vector is then transformed into host cells that are grown under both non-inducing and inducing conditions (conditions A and B, respectively).
Large numbers of compounds (or crude substances which may contain active compounds) are screened for their effect on growth under these two conditions. Agents that interfere with the function of the target should inhibit growth under both conditions. It should be possible, however, to titrate out the inhibitory effect of the compound in the overexpressing strain. That is, if the compound is affecting the particular target that is being tested, it should be possible to inhibit growth under condition A at a concentration that allows the strain to grow under condition B.
Ligand-Binding Assays
Many of the targets according to the invention have functions that have not yet been identified. Ligand-binding assays are useful to identify inhibitor compounds that interfere with the function of a particular target, even when that function is unknown. These assays are designed to detect binding of test compounds to particular targets. The detection may involve direct measurement of binding. Alternatively, indirect indications of binding may involve stabilization of protein structure or disruption of a biological function. Non-limiting examples of useful ligand-binding assays are detailed below.
A useful method for the detection and isolation of binding proteins is the Biomolecular Interaction Assay (BIAcore) system developed by Pharmacia Biosensor and described in the manufacturer's protocol (LKB Pharmacia, Sweden). The BIAcore system uses an affinity purified anti-GST antibody to immobilize GST-fusion proteins onto a sensor chip. The sensor utilizes surface plasmon resonance which is an optical phenomenon that detects changes in refractive indices. In accordance with the practice of the invention, a protein of interest is coated onto a chip and test compounds are passed over the chip. Binding is detected by a change in the refractive index (surface plasmon resonance).
A different type of ligand-binding assay involves scintillation proximity assays (SPA, described in U.S. Pat. No. 4,568,649).
Another type of ligand binding assay, also undergoing development, is based on the fact that proteins containing mitochondrial targeting signals are imported into isolated mitochondria in vitro (Hurt et al., 1985, Embo J. 4: 2061-2068; Eilers and Schatz, Nature, 1986, 322: 228-231). In a mitochondrial import assay, expression vectors are constructed in which nucleic acids encoding particular target proteins are inserted downstream of sequences encoding mitochondrial import signals. The chimeric proteins are synthesized and tested for their ability to be imported into isolated mitochondria in the absence and presence of test compounds. A test compound that binds to the target protein should inhibit its uptake into isolated mitochondria in vitro.
Another ligand-binding assay is the yeast two-hybrid system (Fields and Song, 1989, Nature 340: 245-246). The yeast two-hybrid system takes advantage of the properties of the GAL4 protein of the yeast Saccharomyces cerevisiae. The GAL4 protein is a transcriptional activator required for the expression of genes encoding enzymes of galactose utilization. This protein consists of two separable and functionally essential domains: an N-terminal domain which binds to specific DNA sequences (UASG); and a C-terminal domain containing acidic regions, which is necessary to activate transcription. The native GAL4 protein, containing both domains, is a potent activator of transcription when yeast are grown on galactose media. The N-terminal domain binds to DNA in a sequence-specific manner but is unable to activate transcription. The C-terminal domain contains the activating regions but cannot activate transcription because it fails to be localized to UASG. In the two-hybrid system, a system of two hybrid proteins containing parts of GAL4: (1) a GAL4 DNA-binding domain fused to a protein ‘X’ and (2) a GAL4 activation region fused to a protein ‘Y’. If X and Y can form a protein-protein complex and reconstitute proximity of the GAL4 domains, transcription of a gene regulated by UASG occurs. Creation of two hybrid proteins, each containing one of the interacting proteins X and Y, allows the activation region of UASG to be brought to its normal site of action.
The binding assay described in Fodor et al., 1991, Science 251: 767-773, which involves testing the binding affinity of test compounds for a plurality of defined polymers synthesized on a solid substrate, may also be useful.
Compounds which bind to the polypeptides of the invention are potentially useful as antibacterial agents for use in therapeutic compositions.
Pharmaceutical formulations suitable for antibacterial therapy comprise the antibacterial agent in conjunction with one or more biologically acceptable carriers. Suitable biologically acceptable carriers include, but are not limited to, phosphate-buffered saline, saline, deionized water, or the like. Preferred biologically acceptable carriers are physiologically or pharmaceutically acceptable carriers.
The antibacterial compositions include an antibacterial effective amount of active agent. Antibacterial effective amounts are those quantities of the antibacterial agents of the present invention that afford prophylactic protection against bacterial infections or which result in amelioration or cure of an existing bacterial infection. This antibacterial effective amount will depend upon the agent, the location and nature of the infection, and the particular host. The amount can be determined by experimentation known in the art, such as by establishing a matrix of dosages and frequencies and comparing a group of experimental units or subjects to each point in the matrix.
The antibacterial active agents or compositions can be formed into dosage unit forms, such as for example, creams, ointments, lotions, powders, liquids, tablets, capsules, suppositories, sprays, aerosols or the like. If the antibacterial composition is formulated into a dosage unit form, the dosage unit form may contain an antibacterial effective amount of active agent. Alternatively, the dosage unit form may include less than such an amount if multiple dosage unit forms or multiple dosages are to be used to administer a total dosage of the active agent. Dosage unit forms can include, in addition, one or more excipient(s), diluent(s), disintegrant(s), lubricant(s), plasticizer(s), colorant(s), dosage vehicle(s), absorption enhancer(s), stabilizer(s), bactericide(s), or the like.
For general information concerning formulations, see, e.g., Gilman et al. (eds.), 1990, Goodman and Gilman's: The Pharmacological Basis of Therapeutics, 8th ed., Pergamon Press; and Remington's Pharmaceutical Sciences, 17th ed., 1990, Mack Publishing Co., Easton, Pa.; Avis et al. (eds.), 1993, Pharmaceutical Dosage Forms: Parenteral Medications, Dekker, New York; Lieberman et al (eds.), 1990, Pharmaceutical Dosage Forms: Disperse Systems, Dekker, New York.
The antibacterial agents and compositions of the present invention are useful for preventing or treating S. pneumoniae infections. Infection prevention methods incorporate a prophylactically effective amount of an antibacterial agent or composition. A prophylactically effective amount is an amount effective to prevent S. pneumoniae infection and will depend upon the specific bacterial strain, the agent, and the host. These amounts can be determined experimentally by methods known in the art and as described above.
S. pneumoniae infection treatment methods incorporate a therapeutically effective amount of an antibacterial agent or composition. A therapeutically effective amount is an amount sufficient to ameliorate or eliminate the infection. The prophylactically and/or therapeutically effective amounts can be administered in one administration or over repeated administrations. Therapeutic administration can be followed by prophylactic administration, once the initial bacterial infection has been resolved.
The antibacterial agents and compositions can be administered topically or systemically. Topical application is typically achieved by administration of creams, ointments, lotions, or sprays as described above. Systemic administration includes both oral and parental routes. Parental routes include, without limitation, subcutaneous, intramuscular, intraperitoneal, intravenous, transdermal, inhalation and intranasal administration.
Exemplification
I. Cloning and Sequencing of S. pneumoniae DNA
S. pneumoniae chromosomal DNA was isolated according to a basic DNA protocol outlined in Schleif R. F. and Wensink P. C., Practical Methods in Molecular Biology, p. 98, Springer-Verlag, NY., 1981, with minor modifications. Briefly, cells were pelleted, resuspended in TE (10 mM Tris, 1 mM EDTA, pH 7.6) and GES lysis buffer (5.1 M guanidium thiocyanate, 0.1 M EDTA, pH 8.0, 0.5% N-laurylsarcosine) was added. Suspension was chilled and ammonium acetate (NH4Ac) was added to final concentration of 2.0 M. DNA was extracted, first with chloroform, then with phenol-chloroform, and reextracted with chloroform. DNA was precipitated with isopropanol, washed twice with 70% EtOH, dried and resuspended in TE.
Following isolation whole genomic S. pneumoniae DNA was nebulized (Bodenteich et al., Automated DNA Sequencing and Analysis (J. C. Venter, ed.), Academic Press, 1994) to a median size of 2000 bp. After nebulization, the DNA was concentrated and separated on a standard 1% agarose gel. Several fractions, corresponding to approximate sizes 1000-1500 bp, 1500-2000 bp, 2000-2500 bp, 2500-3000 bp, were excised from the gel and purified by the GeneClean procedure (Bio101, Inc.).
The purified DNA fragments were then blunt-ended using T4 DNA polymerase. The healed DNA was then ligated to unique BstXI-linker adapters (5′ GTCTTCACCACGGGG and 5′ GTGGTGAAGAC in 100-1000 fold molar excess). These linkers are complimentary to the BstXI-cut pMPX vectors, while the overhang is not self-complimentary. Therefore, the linkers will not concatemerize nor will the cut-vector religate itself easily. The linker-adopted inserts were separated from the unincorporated linkers on a 1% agarose gel and purified using GeneClean. The linker-adopted inserts were then ligated to each of 20 pMPX vectors to construct a series of “shotgun” subclone libraries. Blunt ended vector was used for cloning into the PUC19 vector. The vectors contain an out-of-frame lacZ gene at the cloning site which becomes in-frame in the event that an adapter-dimer is cloned, allowing these to be avoided by their blue-color.
All subsequent steps were based either on the multiplex DNA sequencing protocols outlined in Church G. M. and Kieffer-Higgins S., Science 240: 185-188, 1988 or by ABI377 automated DNA sequencing methods. Only major modifications to the protocols are highlighted. Briefly, each of the 20 vectors was then transformed into DHSa competent cells (Gibco/BRL, DH5a transformation protocol). The libraries were assessed by plating onto antibiotic plates containing ampicillin, methicillin and IPTG/Xgal. The plates were incubated overnight at 37° C. Successful transformants were then used for plating of clones and pooling into the multiplex pools. The clones were picked and pooled into 40 ml growth medium cultures. The cultures were grown overnight at 37° C. DNA was purified using the Qiagen Midi-prep kits and Tip-100 columns (Qiagen, Inc.). In this manner, 100 mg of DNA was obtained per pool.
These purified DNA samples were then sequenced either using the multiplex DNA sequencing based on chemical degradation methods (Church G. M. and Kieffer-Higgins S., Science 240: 185-188, 1988) or by Sequithrem (Epicenter Technologies) dideoxy sequencing protocols or by ABI dye-terminator chemistry. For the multiplex portion the sequencing reactions were electrophoresed and transferred onto nylon membranes by direct transfer electrophoresis from 40 cm gels (Richterich P. and Church G. M., Methods in Enzymology 218: 187-222, 1993). The DNA was covalently bound to the membranes by exposure to ultraviolet light, and hybridized with labeled oligonucleotides complimentary to tag sequences on the vectors (Church, supra). The membranes were washed to rinse off non-specifically bound probe, and exposed to X-ray film to visualize individual sequence ladders. After autoradiography, the hybridized probe was removed by incubation at 65° C., and the hybridization cycle repeated with another tag sequence until the membrane had been probed 41 times. Thus, each gel produced a large number of films, each containing new sequencing information. Whenever a new blot was processed, it was initially probed for an internal standard sequence added to each of the pools. Digital images of the films were generated using a laser-scanning densitometer (Molecular Dynamics, Sunnyvale, Calif.). The digitized images were processed on computer workstations (VaxStation 4000's) using the program REPLICA™ (Church et al., Automated DNA Sequencing and Analysis (J. C. Venter, ed.), Academic Press, 1994). Image processing included lane straightening, contrast adjustment to smooth out intensity differences, and resolution enhancement by iterative gaussian deconvolution. The sequences were then converted to an SCF format so that processing and assembly could proceed on UNIX machines. The ABI dye terminator sequence reads were run on ABI377 machines and the data was directly transferred to UNIX machines following lane tracking of the gels. All multiplex and ABI reads were assembled using PHRAP (P. Green, Abstracts of DOE Human Genome Program Contractor-Grantee Workshop V, January 1996, p. 157) with default parameters and not using quality scores. The initial assembly was done at 7fold coverage and yielded 511 contigs. Short read length fragments of 200 bp or less found on the ends of contigs facing in the appropriate direction were used to extend off the end of the contigs. These reads were then resequenced with primers using ABI technology to give sequences with a read length of 500 or more bases. This allowed end extensions to be performed without ordering new primers. In addition, missing mates (sequences from clones that only gave one strand reads) were identified and sequenced with ABI technology to allow the identification of additional overlapping contigs.
End-sequencing of randomly picked genomic lambda was also performed. Sequencing on a both sides was done for all lambda sequences. The lambda library backbone helped to verify the integrity of the assembly and allowed closure of some of the physical gaps.
To identify S. pneumoniae polypeptides the complete genomic sequence of S. pneumoniae were analyzed essentially as follows: First, all possible stop-to-stop open reading frames (ORFs) greater than 180 nucleotides in all six reading frames were translated into amino acid sequences. Second, the identified ORFs were analyzed for homology to known (archeabacter, prokaryotic and eukaryotic) protein sequences. Third, the predicted coding regions of the sequences and start codons were evaluated with the programs GENEMARK™ (Borodovsky and McIninch, 1993, Comp. Chem. 17: 123) and Glimmer (Fraser et al, Nature, 1997).
Identification, Cloning and Expression of S. pneumoniae Nucleic Acids
Expression and purification of the S. pneumoniae polypeptides of the invention can be performed essentially as outlined below.
To facilitate the cloning, expression and purification of membrane and secreted proteins from S. pneumoniae, a gene expression system, such as the pET System (Novagen), for cloning and expression of recombinant proteins in E. coli, is selected. Also, a DNA sequence encoding a peptide tag, the His-Tag, is fused to the 3′ end of DNA sequences of interest in order to facilitate purification of the recombinant protein products. The 3′ end is selected for fusion in order to avoid alteration of any 5′ terminal signal sequence.
PCR Amplification and Cloning of Nucleic Acids Containing ORF's Encoding Enzymes
Nucleic acids chosen (for example, from the nucleic acids set forth in SEQ ID NO: 1-SEQ ID NO: 2661) for cloning from the 14453 strain of S. pneumoniae are prepared for amplification cloning by polymerase chain reaction (PCR). Synthetic oligonucleotide primers specific for the 5′ and 3′ ends of open reading frames (ORFs) are designed and purchased from GibcoBRL Life Technologies (Gaithersburg, Md., USA). All forward primers (specific for the 5′ end of the sequence) are designed to include an NcoI cloning site at the extreme 5′ terminus. These primers are designed to permit initiation of protein translation at a methionine residue followed by a valine residue and the coding sequence for the remainder of the native S. pneumoniae DNA sequence. All reverse primers (specific for the 3′ end of any S. pneumoniae ORF) include a EcoRI site at the extreme 5′ terminus to permit cloning of each S. pneumoniae sequence into the reading frame of the pET-28b. The pET-28b vector provides sequence encoding an additional 20 carboxy-terminal amino acids including six histidine residues (at the extreme C-terminus), which comprise the His-Tag.
Genomic DNA prepared from strain 14453 of S. pneumoniae is used as the source of template DNA for PCR amplification reactions (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). To amplify a DNA sequence containing an S. pneumoniae ORF, genomic DNA (50 nanograms) is introduced into a reaction vial containing 2 mM MgCl2, 1 micromolar synthetic oligonucleotide primers (forward and reverse primers) complementary to and flanking a defined S. pneumoniae ORF, 0.2 mM of each deoxynucleotide triphosphate; dATP, dGTP, dCTP, dTTP and 2.5 units of heat stable DNA polymerase (Amplitaq, Roche Molecular Systems, Inc., Branchburg, N.J., USA) in a final volume of 100 microliters.
Upon completion of thermal cycling reactions, each sample of amplified DNA is washed and purified using the Qiaquick Spin PCR purification kit (Qiagen, Gaithersburg, Md., USA). All amplified DNA samples are subjected to digestion with the restriction endonucleases, e.g., NcoI and EcoRI (New England BioLabs, Beverly, Mass., USA) (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). DNA samples are then subjected to electrophoresis on 1.0% NuSeive (FMC BioProducts, Rockland, Me. USA) agarose gels. DNA is visualized by exposure to ethidium bromide and long wave uv irradiation. DNA contained in slices isolated from the agarose gel is purified using the Bio 101 GeneClean Kit protocol (Bio 101 Vista, Calif., USA).
Cloning of S. pneumoniae Nucleic Acids into an Expression Vector
The pET-28b vector is prepared for cloning by digestion with endonucleases, e.g., NcoI and EcoRI (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). The pET-28a vector, which encodes a His-Tag that can be fused to the 5′ end of an inserted gene, is prepared by digestion with appropriate restriction endonucleases.
Following digestion, DNA inserts are cloned (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994) into the previously digested pET-28b expression vector. Products of the ligation reaction are then used to transform the BL21 strain of E. coli (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994) as described below.
Transformation of Competent Bacteria with Recombinant Plasmids
Competent bacteria, E coli strain BL21 or E. coli strain BL21 (DE3), are transformed with recombinant pET expression plasmids carrying the cloned S. pneumoniae sequences according to standard methods (Current Protocols in Molecular, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994). Briefly, 1 microliter of ligation reaction is mixed with 50 microliters of electrocompetent cells and subjected to a high voltage pulse, after which, samples are incubated in 0.45 milliliters SOC medium (0.5% yeast extract, 2.0% tryptone, 10 mM NaCl, 2.5 mM KCl, 10 mM MgCl2, 10 mM MgSO4 and 20, mM glucose) at 37° C. with shaking for 1 hour. Samples are then spread on LB agar plates containing 25 microgram/ml kanamycin sulfate for growth overnight. Transformed colonies of BL21 are then picked and analyzed to evaluate cloned inserts as described below.
Identification Of Recombinant Expression Vectors with S. pneumoniae Nucleic Acids
Individual BL21 clones transformed with recombinant pET-28b S. pneumoniae ORFs are analyzed by PCR amplification of the cloned inserts using the same forward and reverse primers, specific for each S. pneumoniae sequence, that were used in the original PCR amplification cloning reactions. Successful amplification verifies the integration of the S. pneumoniae sequences in the expression vector (Current Protocols in Molecular Biology, John Wiley and Sons, Inc., F. Ausubel et al., eds., 1994).
Isolation and Preparation of Nucleic Acids from Transformants
Individual clones of recombinant pET-28b vectors carrying properly cloned S. pneumoniae ORFs are picked and incubated in 5 mls of LB broth plus 25 microgram/ml kanamycin sulfate overnight. The following day plasmid DNA is isolated and purified using the Qiagen plasmid purification protocol (Qiagen Inc., Chatsworth, Calif., USA).
Expression Of Recombinant S. pneumoniae Sequences in E. coli
The pET vector can be propagated in any E. coli K-12 strain e.g. HMS 174, HB101, JM109, DH5, etc. for the purpose of cloning or plasmid preparation. Hosts for expression include E. coli strains containing a chromosomal copy of the gene for T7 RNA polymerase. These hosts are lysogens of bacteriophage DE3, a lambda derivative that carries the lacI gene, the lacUV5 promoter and the gene for T7 RNA polymerase. T7 RNA polymerase is induced by addition of isopropyl-B-D-thiogalactoside (IPTG), and the T7 RNA polymerase transcribes any target plasmid, such as pET-28b, carrying its gene of interest. Strains used include: BL21(DE3) (Studier, F. W., Rosenberg, A. H., Dunn, J. J., and Dubendorff, J. W. (1990) Meth. Enzymol. 185, 60-89).
To express recombinant S. pneumoniae sequences, 50 nanograms of plasmid DNA isolated as described above is used to transform competent BL21(DE3) bacteria as described above (provided by Novagen as part of the pET expression system kit). The lacZ gene (beta-galactosidase) is expressed in the pET-System as described for the S. pneumoniae recombinant constructions. Transformed cells are cultured in SOC medium for 1 hour, and the culture is then plated on LB plates containing 25 micrograms/ml kanamycin sulfate. The following day, bacterial colonies are pooled and grown in LB medium containing kanamycin sulfate (25 micrograms/ml) to an optical density at 600 nM of 0.5 to 1.0 O.D. units, at which point, 1 millimolar IPTG was added to the culture for 3 hours to induce gene expression of the S. pneumoniae recombinant DNA constructions.
After induction of gene expression with IPTG, bacteria are pelleted by centrifugation in a Sorvall RC-3B centrifuge at 3500×g for 15 minutes at 4° C. Pellets are resuspended in 50 milliliters of cold 10 mM Tris-HCl, pH 8.0, 0.1 M NaCl and 0.1 mM EDTA (STE buffer). Cells are then centrifuged at 2000×g for 20 min at 4° C. Wet pellets are weighed and frozen at −80° C. until ready for protein purification.
A variety of methodologies known in the art can be utilized to purify the isolated proteins. (Current Protocols in Protein Science, John Wiley and Sons, Inc., J. E. Coligan et al., eds., 1995). For example, the frozen cells may be thawed, resupended in buffer and ruptured by several passages through a small volume microfluidizer (Model M-110S, Microfluidics International Corporation, Newton, Mass.). The resultant homogenate may be centrifuged to yield a clear supernatant (crude extract) and following filtration the crude extract may be fractionated over columns. Fractions may be monitored by absorbance at OD280 nm. and peak fractions may analyzed by SDS-PAGE.
The concentrations of purified protein preparations may be quantified spectrophotometrically using absorbance coefficients calculated from amino acid content (Perkins, S. J. 1986 Eur. J. Biochem. 157, 169-180). Protein concentrations are also measured by the method of Bradford, M. M. (1976) Anal. Biochem. 72, 248-254, and Lowry, O. H., Rosebrough, N., Farr, A. L. & Randall, R. J. (1951) J. Biol. Chem. 193, pages 265-275, using bovine serum albumin as a standard.
SDS-polyacrylamide gels of various concentrations may be purchased from BioRad (Hercules, Calif., USA), and stained with Coomassie blue. Molecular weight markers may include rabbit skeletal muscle myosin (200 kDa), E. coli (-galactosidase (116 kDa), rabbit muscle phosphorylase B (97.4 kDa), bovine serum albumin (66.2 kDa), ovalbumin (45 kDa), bovine carbonic anhydrase (31 kDa), soybean trypsin inhibitor (21.5 kDa), egg white lysozyme (14.4 kDa) and bovine aprotinin (6.5 kDa).
Equivalents
While this invention has been particularly shown and described with references to preferred embodiments thereof, it will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the scope of the invention encompassed by the appended claims.
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ORF NAMENT IDAA IDAA LNNT LNSCOREP-VALUEDESCRIPTION
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SPX0001126621113335522.20E−74[GI:2804700]87
ORF NAMENT IDAA IDAA LNNT LNSCOREP-VALUEDESCRIPTION
SPX0001126621113335522.20E-74[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX0002226631735198853.60E-120[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX0003326641093272811.40E-34[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX0004426651905709487.40E-131[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX000552666122366NO-HIT6
SPX00066266740112038157.40E-125[LN:RS1_LEULA]116
[AC:P50889:P71450]
[GN:RPS1]
[OR:Leuconostoc lactis]
[DE:40S RIBOSOMAL PROTEIN S1]
[SP:P50889:P71450]
SPX00077266879237892.90E-05[LN:E64801]77
[AC:E64801]
[PN:hypothetical protein b0663]
[OR:Escherichia coli]
SPX00088266977231NO-HIT6
SPX0009926702156458326.30E-114[LN:PCP_STRPY]149
[AC:Q01328]
[GN:PCP]
[OR:Streptococcus pyogenes]
[EC:3.4.19.3]
[DE:PEPTIDASE) (PYROGLUTAMYL-PEPTIDASE I) (PGP-I) (PYRASE)]
[SP:Q01328]
SPX00101026713089242343.90E-61[LN:A81402]119
[AC:A81402]
[PN:probable integral membrane protein Cj0553 [imported]]
[GN:Cj0553]
[OR:Campylobacter jejuni]
SPX00111126722377112081.30E-37[GI:6002226]128
[LN:SC51A]
[AC:AL121596]
[PN:possible integral membrane protein]
[GN:SCF51A.18c]
[OR:Streptomyces coelicolor A3(2)]
SPX00121226732357052131.30E-53[GI:2804687]114
[LN:AF030359]
[AC:AF030359]
[PN:oligopeptide binding protein]
[GN:aliA]
[OR:Streptococcus pneumoniae]
SPX0013132674341102313599.60E-184[GI:6979306]190
[LN:AF164204]
[AC:AF164204]
[PN:branched-chain amino acid aminotransferase]
[GN:bcaT]
[FN:catalyzes the first reaction in the catabolism]
[OR:Lactococcus lactis subsp. cremoris]
SPX0014142675824247241430[GI:6851038]105
[LN:SPPARCETP]
[AC:Z67739]
[PN:DNA topoisomerase IV]
[GN:parC]
[OR:Streptococcus pneumoniae]
SPX0015152676648194433180[GI:6851037]105
[LN:SPPARCETP]
[AC:Z67739]
[PN:DNA topoisomerase IV]
[GN:parE]
[OR:Streptococcus pneumoniae]
SPX001616267721464210732.50E-150[LN:YPAE_STRPN]127
[AC:Q54916]
[OR:Streptococcus pneumoniae]
[DE:HYPOTHETICAL 23.0 KD PROTEIN IN PARE 5′REGION (ORF2)]
[SP:Q54916]
SPX0017172678410123010448.20E-270[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX00181826792788345919.50E-139[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX00191926801915734222.30E-53[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX0020202681341021245.30E-12[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX002121268231995710023.80E-138[LN:F70009]141
[AC:F70009]
[PN:conserved hypothetical protein yufQ]
[GN:yufQ]
[CL:probable ribose ABC transporter rbsC-2]
[OR:Bacillus subtilis]
SPX002222268336210863853.70E-85[LN:E70009]97
[AC:E70009]
[PN:conserved hypothetical protein yufP]
[GN:yufP]
[OR:Bacillus subtilis]
SPX0023232684512153616232.30E-217[LN:D70009]174
[AC:D70009]
[PN:probable ABC transporter yufO]
[GN:yufO]
[CL:Bacillus subtilis probable ABC transporter yufO:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX0024242685140420831.80E-06[LN:G72493]92
[AC:G72493]
[PN:hypothetical protein APE2590]
[GN:APE2590]
[OR:Aeropyrum pernix]
SPX002525268636410923548.80E-82[LN:YUFN_BACSU]117
[AC:O05252]
[GN:YUFN]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL LIPOPROTEIN YUFN PRECURSOR]
[SP:O05252]
SPX00262626871303903245.40E-40[GI:6478520]100
[LN:AF187304]
[AC:AF187304]
[PN:cytidine deaminase]
[GN:cdd]
[OR:Bacillus caldolyticus]
SPX00272726881003002762.40E-33[LN:D75424]136
[AC:D75424]
[PN:deoxyribose-phosphate aldolase]
[GN:DR1205]
[CL:deoxyribose-phosphate aldolase]
[OR:Deinococcus radiodurans]
SPX002828268961183NO-HIT6
SPX00292926901193573443.30E-42[LN:DEOC_BACSU]109
[AC:P39121]
[GN:DRA]
[OR:Bacillus subtilis]
[EC:4.1.2.4]
[DE:(DEOXYRIBOALDOLASE)]
[SP:P39121]
SPX003030269142612789219.70E-147“[LN:PDP_BACST]144
[AC:P77836]
[GN:PYN]
[OR:Bacillus stearothermophilus]
[EC:2.4.2.2]
[DE:PYRIMIDINE-NUCLEOSIDE PHOSPHORYLASE, (PYNP)]
[SP:P77836]”
SPX00313126921975912502.00E-56[LN:S59955]113
[AC:S59955]
[PN:hypothetical protein 202]
[CL:hypothetical protein MJ0882]
[OR:Staphylococcus aureus]
SPX003232269373219NO-HIT6
SPX0033332694100300NO-HIT6
SPX00343426953179513453.80E-79[GI:6960352]134
[LN:STYSTMF1]
[AC:AF170176]
[PN:96% identity over 316 amino acids with E. coli]
[GN:coaA]
[OR:Salmonella typhimurium LT2]
SPX003535269679237988.40E-17[LN:R3EC20]214
[AC:A30425:A02748:S40547:G64722:S07374]
[PN:ribosomal protein S20/L26 [validated]
:ribosomal protein L26:ribosomal protein S20]
[GN:rpsT]
[CL:Escherichia coli ribosomal protein S20]
[OR:Escherichia coli]
SPX00363626971755252706.30E-50[GI:6434823]86
[LN:SPU78969]
[AC:U78969]
[PN:FlaR]
[GN:flaR]
[OR:Streptococcus pyogenes]
SPX003737269823771110424.10E-140[LN:DEOD_STRTR]116
[AC:Q56037]
[GN:DEOD]
[OR:Streptococcus thermophilus]
[EC:2.4.2.1]
[DE:(PNP) (FRAGMENT)]
[SP:Q56037]
SPX00383826991715132711.10E-30[GI:6729344]150
[LN:AB029317]
[AC:AB029317]
[PN:intermedilysin]
[GN:ily]
[OR:Streptococcus intermedius]
[SR:Streptococcus intermedius (strain:UNS46) DNA]
SPX00393927001925761172.80E-07“[LN:PXN1_XENLA]137
[AC:P49263]
[GN:PXN1]
[OR:Xenopus laevis]
[SR:,African clawed frog]
[DE:PENTRAXIN FUSION PROTEIN PRECURSOR]
[SP:P49263]”
SPX0040402701136408920.00026“[LN:CP23_CHICK]135
[AC:P23614]
[OR:Gallus gallus]
[SR:,Chicken]
[DE:23 KD CORTICAL CYTOSKELETON-ASSOCIATED PROTEIN (CAP-23)]
[SP:P23614]”
SPX00414127022708103951.40E-105[LN:DEOD_BACSU]100
[AC:P46354]
[GN:DEOD:PNP]
[OR:Bacillus subtilis]
[EC:2.4.2.1]
[DE:(PNP)]
[SP:P46354]
SPX0042422703181543NO-HIT6
SPX004343270440412127362.30E-199“[LN:DEOB_LACLC]181
[AC:O32808]
[GN:DEOB]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[EC:5.4.2.7]
[DE:PHOSPHOPENTOMUTASE, (PHOSPHODEOXYRIBOMUTASE)]
[SP:O32808]”
SPX00444427052477412061.40E-52[LN:G69180]168
[AC:G69180]
[PN:ribose 5-phosphate isomerase]
[GN:MTH608]
[CL:Haemophilus influenzae ribose-5-phosphate isomerase]
[OR:Methanobacterium thermoautotrophicum]
SPX004545270662186NO-HIT6
SPX00464627072918733865.80E-99[LN:YFOL_STRTR]86
[AC:P96051]
[OR:Streptococcus thermophilus]
[DE:(ORF1091)]
[SP:P96051]
SPX004747270830792110493.00E-140[LN:FOLD_STRTR]121
[AC:P96050]
[GN:FOLD]
[OR:Streptococcus thermophilus]
[EC:1.5.1.5:3.5.4.9]
[DE:(EC 3.5.4.9)]]
[SP:P96050]
SPX004848270972216995.40E-08[LN:G72510]92
[AC:G72510]
[PN:hypothetical protein APE2061]
[GN:APE2061]
[OR:Aeropyrum pernix]
SPX00494927102457357967.00E-105[LN:H69334]162
[AC:H69334]
[PN:glutamine transport protein glnQ]
[GN:glnQ]
[CL:inner membrane protein malK:ATP-binding cassette homology]
[OR:Archaeoglobus fulgidus]
SPX0050502711128384885.60E-05[LN:D72757]92
[AC:D72757]
[PN:hypothetical protein APE0049]
[GN:APE0049]
[OR:Aeropyrum pernix]
SPX00515127122286843141.10E-52“[LN:H69278]151
[AC:H69278]
[PN:glutamine ABC transporter, permease protein (glnP) homolog]
[CL:histidine permease protein M]
[OR:Archaeoglobus fulgidus]”
SPX005252271377231898.60E-09[LN:G69865]87
[AC:G69865]
[PN:hypothetical protein ykuJ]
[GN:ykuJ]
[OR:Bacillus subtilis]
SPX0053532714753225926410[GI:4103470]84
[LN:AF023421]
[AC:AF023421]
[PN:ClpE]
[GN:clpE]
[OR:Lactococcus lactis]
SPX0054542715832491169.50E-10[GI:4098132]83
[LN:MBU73653]
[AC:U73653]
[PN:63 kDa protein]
[OR:Mycobacterium bovis]
SPX005555271661183NO-HIT6
SPX005656271770210NO-HIT6
SPX00575727181143424772.00E-73[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX00585827191163485696.90E-75[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX00595927201414231015.60E-07[LN:A70315]147
[AC:A70315]
[PN:AP4A hydrolase]
[GN:apfA]
[CL:Methanococcus jannaschii mutator protein mutT:mutT domain homology]
[OR:Aquifex aeolicus]
SPX0060602721100300NO-HIT6
SPX00616127221985945973.80E-95[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX0062622723882643081.70E-38[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX0063632724341021262.60E-12[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX00646427251173512105.10E-24“[LN:JC1151]89
[AC:JC1151]
[PN:hypothetical protein, 20.3K]
[OR:Agrobacterium tumefaciens]”
SPX00656527261023061545.60E-19[GI:722339]100
[LN:AXU22323]
[AC:U22323]
[PN:unknown]
[OR:Acetobacter xylinus]
[SR:Acetobacter xylinum]
SPX006666272789267NO-HIT6
SPX006767272857617282855.20E-53[LN:G70002]87
[AC:G70002]
[PN:hypothetical protein ytwP]
[GN:ytwP]
[OR:Bacillus subtilis]
SPX0068682729649194733220[GI:1490397]95
[LN:SPGYRBORF]
[AC:Z67740]
[PN:DNA gyrase]
[GN:gyrB]
[OR:Streptococcus pneumoniae]
SPX00696927301915737092.40E-93[GI:1052803]81
[LN:SPGYRBG]
[AC:X83917]
[GN:orflgyrb]
[OR:Streptococcus pneumoniae]
SPX00707027311855551189.00E-28“[LN:D70177]211
[AC:D70177]
[PN:4-methyl-5(b-hydroxyethyl)-thiazole monophosphate biosynthesis protein (thiJ) homolog]
[CL:signal transduction protein DJ-1]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX007171273241712513981.00E-50[LN:S22738]86
[AC:S22738:S22728]
[PN:hypothetical protein]
[OR:Streptococcus salivarius]
SPX007272273381724512033.80E-66[LN:DING_BACSU]122
[AC:P54394]
[GN:DING]
[OR:Bacillus subtilis]
[DE:PROBABLE ATP-DEPENDENT HELICASE DING HOMOLOG]
[SP:P54394]
SPX00737327343109301896.20E-42[LN:G69979]85
[AC:G69979]
[PN:proteinase homolog yrrN]
[GN:yrrN]
[OR:Bacillus subtilis]
SPX007474273596288NO-HIT6
SPX0075752736445133522024.50E-301“[LN:CIAH_STRPN]120
[AC:Q54955]
[GN:CIAH]
[OR:Streptococcus pneumoniae]
[EC:2.7.3.-]
[DE:SENSOR PROTEIN CIAH,]
[SP:Q54955]”
SPX007676273722567511301.70E-152[LN:CIAR_STRPN]124
[AC:Q54954]
[GN:CIAR]
[OR:Streptococcus pneumoniae]
[DE:TRANSCRIPTIONAL REGULATORY PROTEIN CIAR]
[SP:Q54954]
SPX0077772738849254716530[GI:5524752]105
[LN:STH007700]
[AC:AJ007700]
[PN:aminopeptidase N]
[GN:pepN]
[OR:Streptococcus thermophilus]
SPX00787827391474411761.80E-20[LN:T35570]113
[AC:T35570]
[PN:hypothetical protein SC6G4.19c SC6G4.19c]
[GN:SC6G4.19c]
[OR:Streptomyces coelicolor]
SPX0079792740292876808.00E-10[LN:PPSA_PYRFU]131
[AC:P42850:Q59672]
[GN:PPSA]
[OR:Pyrococcus furiosus]
[EC:2.7.9.2]
[DE:DIKINASE) (PEP SYNTHASE)]
[SP:P42850:Q59672]
SPX0080802741243729NO-HIT6
SPX00818127421604801131.60E-07[LN:C72513]92
[AC:C72513]
[PN:hypothetical protein APE2080]
[GN:APE2080]
[OR:Aeropyrum pernix]
SPX008282274376228NO-HIT6
SPX00838327442336992313.20E-28[LN:GNO_GLUOX]104
[AC:P50199]
[GN:GNO]
[OR:Gluconobacter oxydans]
[EC:1.1.1.69]
[DE:REDUCTASE)]
[SP:P50199]
SPX008484274589267NO-HIT6
SPX00858527463099272102.40E-41[LN:YDHF_ECOLI]135
[AC:P76187]
[GN:YDHF]
[OR:Escherichia coli]
[DE:HYPOTHETICAL OXIDOREDUCTASE IN SODC-NEMA INTERGENIC REGION]
[SP:P76187]
SPX00868627472728161143.70E-09[GI:3043880]94
[LN:LLU95841]
[AC:U95841]
[PN:transmembrane protein Tmp6]
[OR:Lactococcus lactis]
SPX0087872748722161461.50E-15[GI:3582220]114
[LN:AE001272]
[AC:AE001272]
[PN:conserved hypothetical protein]
[GN:ORF00047]
[OR:Lactococcus lactis]
SPX008888274979237NO-HIT6
SPX0089892750822462692.80E-32[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX009090275168020407346.10E-239[LN:SYM_BACST]108
[AC:P23920]
[GN:METS]
[OR:Bacillus stearothermophilus]
[EC:6.1.1.10]
[DE:(METRS)]
[SP:P23920]
SPX009191275242012602872.30E-62[LN:E69858]97
[AC:E69858]
[PN:conserved hypothetical protein yknZ]
[GN:yknZ]
[OR:Bacillus subtilis]
SPX00929227532347026639.00E-86[GI:2822199]120
[LN:SCU96166]
[AC:U96166:AF227987]
[PN:ATP-binding cassette protein]
[GN:tptC]
[OR:Streptococcus cristatus]
SPX009393275440012001445.60E-36[LN:C69858]97
[AC:C69858]
[PN:conserved hypothetical protein yknX]
[GN:yknX]
[OR:Bacillus subtilis]
SPX009494275544913477301.70E-192“[LN:S41386]182
[AC:S41386]
[PN:glutathione reductase (NADPH),]
[CL:dihydrolipoamide dehydrogenase:dihydrolipoamide dehydrogenase homology]
[OR:Streptococcus thermophilus]
[EC:1.6.4.2]”
SPX00959527561795372186.90E-30[LN:H72334]78
[AC:H72334]
[PN:bioY protein]
[GN:TM0799]
[OR:Thermotoga maritima]
SPX0096962757112336NO-HIT6
SPX0097972758802401711.50E-18[LN:Y352_TREPA]108
[AC:O83371]
[GN:TP0352]
[OR:Treponema pallidum]
[DE:HYPOTHETICAL PROTEIN TP0352]
[SP:O83371]
SPX0098982759107321NO-HIT6
SPX00999927601133391091.40E-12[GI:4098081]128
[LN:LLU73336]
[AC:U73336]
[PN:anaerobic ribonucleotide reductase]
[GN:nrdD]
[OR:Lactococcus lactis subsp. cremoris]
SPX010010027612407203721.30E-85[LN:TRMD_BACSU]142
[AC:O31741]
[GN:TRMD]
[OR:Bacillus subtilis]
[EC:2.1.1.31]
[DE:METHYLTRANSFERASE) (TRNA [GM37]
METHYLTRANSFERASE)]
[SP:O31741]
SPX010110127621735192925.20E-61[LN:RIMM_BACSU]119
[AC:O31740]
[GN:RIMM]
[OR:Bacillus subtilis]
[DE:PROBABLE 16S RRNA PROCESSING PROTEIN RIMM]
[SP:O31740]
SPX01021022763267801NO-HIT6
SPX01031032764802401419.70E-15[LN:C69880]147
[AC:C69880]
[PN:conserved hypothetical protein ylqC]
[GN:ylqC]
[CL:Bacillus conserved hypothetical protein ylqC]
[OR:Bacillus subtilis]
SPX01041042765912733155.10E-39[LN:C47154]176
[AC:C47154:S11366:G69700]
[PN:ribosomal protein S16 (BS17) rpsP:ribosomal protein BS17]
[GN:rpsP]
[CL:Escherichia coli ribosomal protein S16]
[OR:Bacillus subtilis]
SPX0105105276670210NO-HIT6
SPX01061062767135405NO-HIT6
SPX0107107276871213NO-HIT6
SPX010810827692688042433.60E-38[LN:T41399]140
[AC:T41399]
[PN:probable cyclophilin-related peptidyl prolyl cis-trans isomerase]
[GN:SPCC553.04]
[OR:Schizosaccharomyces pombe]
SPX01091092770120360835.110E-05[GI:1773206]60
[LN:ECU82664]
[AC:U82664]
[OR:Escherichia coli]
SPX01101102771514154215023.70E-258[LN:D69813]188
[AC:D69813]
[PN:ABC transporter (ATP-binding protein) homolog yfmM]
[GN:yfmM]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX01111112772161483882.20E-11[GI:7110140]100
[LN:AF155139]
[AC:AF155139:AF019976]
[PN:VanZF]
[GN:vanZF]
[OR:Paenibacillus popilliae]
SPX0112112277336210864521.30E-135[LN:YLON_BACSU]137
[AC:O34617]
[GN:YLON]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 41.6 KD PROTEIN IN FMT-SPOVM INTERGENIC REGION]
[SP:O34617]
SPX011311327741775311523.20E-25[LN:F70023]136
[AC:F70023]
[PN:hypothetical protein yutD]
[GN:yutD]
[CL:Bacillus subtilis hypothetical protein yutD]
[OR:Bacillus subtilis]
SPX0114114277520260610344.90E-138[GI:5758312]152
[LN:AF162664]
[AC:AF162664]
[PN:manganese co-factored superoxide dismutase]
[GN:sodA]
[FN:removes superoxide]
[OR:Streptococcus pneumoniae]
SPX0115115277634610389522.60E-127[GI:2765186]92
[LN:SASODA]
[AC:Y12224]
[PN:hypothetical protein]
[OR:Streptococcus agalactiae]
SPX0116116277731293616163.20E-220[GI:5578893]116
[LN:SPN131985]
[AC:AJ131985]
[PN:dihydroorotate dehydrogenase]
[GN:pyrDA]
[OR:Streptococcus pneumoniae]
SPX01171172778397119113993.90E-187[LN:METK_STAAU]135
[AC:P50307]
[GN:METK]
[OR:Staphylococcus aureus]
[EC:2.5.1.6]
[DE:ADENOSYLTRANSFERASE) (ADOMET SYNTHETASE)]
[SP:P50307]
SPX0118118277944813449721.00E-140[LN:YQFR_BACSU]130
[AC:P54475]
[GN:YQFR]
[OR:Bacillus subtilis]
[DE:PROBABLE RNA HELICASE IN CCCA-SODA INTERGENIC REGION]
[SP:P54475]
SPX01191192780272816NO-HIT6
SPX0120120278188264NO-HIT6
SPX0121121278272721817354.60E-182[GI:4098489]91
[LN:SMU78600]
[AC:U78600]
[PN:putative ptsG protein]
[OR:Streptococcus mutans]
SPX012212227833129363302.80E-63[LN:G69627]88
[AC:G69627]
[PN:cell-division protein ftsX]
[GN:ftsX]
[OR:Bacillus subtilis]
SPX0123123278469207NO-HIT6
SPX012412427852316937989.90E-106[LN:D69627]176
[AC:D69627]
[PN:cell-division ATP-binding protein ftsE]
[GN:ftsE]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX0125125278675225941.10E-07[LN:A71007]95
[AC:A71007]
[PN:hypothetical protein PH1351]
[GN:PH1351]
[OR:Pyrococcus horikoshii]
SPX012612627873079219366.80E-124[LN:RF2_BACSU]128
[AC:P28367:O34444]
[GN:PRFB]
[OR:Bacillus subtilis]
[DE:PEPTIDE CHAIN RELEASE FACTOR 2 (RF-2)]
[SP:P28367:O34444]
SPX012712727882196572793.40E-41[LN:H72290]96
[AC:H72290]
[PN:conserved hypothetical protein]
[GN:TM1140]
[OR:Thermotoga maritima]
SPX012812827892377117117.60E-93[LN:T35757]212
[AC:T35757]
[PN:probable branched chain amino acid transport ATP-binding protein]
[GN:SC7H2.26]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Streptomyces coelicolor]
SPX01291292790672011096.60E-10[LN:G72485]92
[AC:G72485]
[PN:hypothetical protein APE2527]
[GN:APE2527]
[OR:Aeropyrum pernix]
SPX013013027912557653874.20E-90“[LN:F72290]206
[AC:F72290]
[PN:branched chain amino acid ABC transporter, ATP-binding protein]
[GN:TM1138]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Thermotoga maritima]”
SPX013113127923199573341.10E-63[LN:E81303]164
[AC:E81303]
[PN:probable branched-chain amino-acid ABC transport system permease protein Cj1016c [imported]]
[GN:livM:Cj1016c]
[OR:Campylobacter jejuni]
SPX013213227932938793251.30E-90“[LN:D72290]163
[AC:D72290]
[PN:branched chain amino acid ABC transporter, permease protein]
[GN:TM1136]
[CL:leucine transport protein livH]
[OR:Thermotoga maritima]”
SPX0133133279438711611935.70E-39[LN:H81303]166
[AC:H81303]
[PN:branched-chain amino-acid ABC transport system periplasmic binding protein Cj1019c [imported]]
[GN:livJ:Cj1019c]
[OR:Campylobacter jejuni]
SPX01341342795150450NO-HIT6
SPX01351352796832491162.40E-11[LN:D69874]97
[AC:D69874]
[PN:conserved hypothetical protein ylbG]
[GN:ylbG]
[OR:Bacillus subtilis]
SPX013613627971975919338.10E-124[LN:CLPP_STRSL]119
[AC:P36398]
[GN:CLPP]
[OR:Streptococcus salivarius]
[EC:3.4.21.92]
[DE:(ENDOPEPTIDASE CLP)]
[SP:P36398]
SPX013713727982176519615.20E-129[LN:UPP_STRSL]124
[AC:P36399]
[GN:UPP]
[OR:Streptococcus salivarius]
[EC:2.4.2.9]
[DE:PYROPHOSPHORYLASE) (UPRTASE)]
[SP:P36399]
SPX0138138279954162O-HIT6
SPX013913928001564682654.40E-49[LN:CME2_BACSU]106
[AC:P32393]
[GN:COMEB:COME2]
[OR:Bacillus subtilis]
[DE:COME OPERON PROTEIN 2]
[SP:P32393]
SPX014014028011865581141.10E-07[LN:G70325]102
[AC:G70325]
[PN:transcription regulator TetR/AcrR family]
[GN:acrR3]
[OR:Aquifex aeolicus]
SPX014114128022828468132.60E-107[GI:4580621]77
[LN:AF118389]
[AC:AF118389]
[PN:unknown]
[OR:Streptococcus suis]
SPX0142142280339211763301.60E-83[GI:2293312]83
[LN:AF008220]
[AC:AF008220]
[PN:YtfP]
[GN:ytfP]
[OR:Bacillus subtilis]
SPX014314328041524561066.50E-12[LN:G70031]121
[AC:G70031]
[PN:mutator MutT protein homolog yvcI]
[GN:yvcI]
[CL:mutT domain homology]
[OR:Bacillus subtilis]
SPX014414428051735198762.10E-115[GI:6179679]137
[LN:SPN239034]
[AC:AJ239034]
[PN:regulator of pmrA]
[GN:mta]
[FN:regulator of pmrA expression]
[OR:Streptococcus pneumoniae]
SPX0145145280649014708055.40E-151[LN:F69825]144
[AC:F69825]
[PN:sodium-dependent transporter homolog yhdH]
[GN:yhdH]
[CL:gamma-aminobutyric acid transporter]
[OR:Bacillus subtilis]
SPX0146146280731594511653.00E-155[LN:MANA_STRMU]118
[AC:Q59935]
[GN:PMI]
[OR:Streptococcus mutans]
[EC:5.3.1.8]
[DE:(PMI) (PHOSPHOHEXOMUTASE)]
[SP:Q59935]
SPX01471472808134402NO-HIT6
SPX014814828091103302701.80E-43[LN:JE0396]121
[AC:JE0396]
[PN:phospho-beta-galactosidase II]
[CL:Agrobacterium beta-glucosidase]
[OR:Lactobacillus gasseri]
SPX0149149281089267NO-HIT6
SPX015015028112186541541.00E-20[GI:722339]100
[LN:AXU22323]
[AC:U22323]
[PN:unknown]
[OR:Acetobacter xylinus]
[SR:Acetobacter xylinum]
SPX01511512812116348NO-HIT6
SPX01521522813592177630330“[LN:POXB_STRPN]141
[AC:Q54970]
[GN:SPXB]
[OR:Streptococcus pneumoniae]
[EC:1.2.3.3]
[DE:PYRUVATE OXIDASE, (PYRUVIC OXIDASE) (POX)]
[SP:Q54970]”
SPX01531532814672011492.30E-14[GI:1513069]147
[LN:LMU15554]
[AC:U15554]
[PN:P-type adenosine triphosphatase]
[GN:ctpA]
[FN:involved in cation transport]
[OR:Listeria monocytogenes]
SPX0154154281573321996488.80E-202[GI:1513069]147
[LN:LMU15554]
[AC:U15554]
[PN:P-type adenosine triphosphatase]
[GN:ctpA]
[FN:involved in cation transport]
[OR:Listeria monocytogenes]
SPX01551552816852551072.40E-09[LN:H72624]92
[AC:H72624]
[PN:hypothetical protein APE1456]
[GN:APE1456]
[OR:Aeropyrum pernix]
SPX0156156281761183NO-HIT6
SPX01571572818124372706.10E-06“[LN:H69267]183
[AC:H69267]
[PN:cytochrome-c oxidase, chain II AF0144]
[CL:cytochrome-c oxidase chain II:cytochrome-c oxidase chain II homology]
[OR:Archaeoglobus fulgidus]
[EC:1.9.3.1]”
SPX015815828191424262401.00E-28[LN:COPY_ENTHR]118
[AC:Q47839]
[GN:COPY]
[OR:Enterococcus hirae]
[DE:COPAB ATPASES METAL-FIST TYPE REPRESSOR]
[SP:Q47839]
SPX015915928202698073084.00E-99[GI:6707002]96
[LN:AF109218]
[AC:AF109218:U96108]
[PN:ThiD]
[GN:thiD]
[OR:Staphylococcus carnosus]
SPX016016028212116332458.10E-55[LN:D75087]210
[AC:D75087]
[PN:thiamin phosphate pyrophosphorylase (thie) PAB1645]
[GN:PAB1645]
[CL:probable thiamin-phosphate pyrophosphorylase:thiamin-phosphate pyrophosphorylase homology]
[OR:Pyrococcus abyssi]
SPX016116128222698072282.70E-27[LN:THIM_ECOLI]144
[AC:P76423]
[GN:THIM]
[OR:Escherichia coli]
[EC:2.7.1.50]
[DE:HYDROXYETHYLTHIAZOLE KINASE) (THZ KINASE) (TH KINASE)]
[SP:P76423]
SPX01621622823175525NO-HIT6
SPX016316328242316933842.00E-48[LN:TENA_BACSU]108
[AC:P25052]
[GN:TENA]
[OR:Bacillus subtilis]
[DE:TRANSCRIPTIONAL ACTIVATOR TENA]
[SP:P25052]
SPX016416428252176511121.10E-13[GI:1296823]78
[LN:LHPEPIGN]
[AC:Z56283]
[GN:orf2]
[OR:Lactobacillus helveticus]
SPX0165165282646213862794.50E-59[GI:1296822]78
[LN:LHPEPIGN]
[AC:Z56283]
[GN:orf1]
[OR:Lactobacillus helveticus]
SPX016616628271875612032.20E-27[LN:A69859]87
[AC:A69859]
[PN:hypothetical protein ykoE]
[GN:ykoE]
[OR:Bacillus subtilis]
SPX0167167282875225NO-HIT6
SPX0168168282969207NO-HIT6
SPX016916928302106305204.10E-72[GI:6707004]96
[LN:AF109218]
[AC:AF109218:U96108]
[PN:ThiE]
[GN:thiE]
[OR:Staphylococcus carnosus]
SPX017017028312688045234.60E-67[GI:6707003]96
[LN:AF109218]
[AC:AF109218:U96108]
[PN:ThiM]
[GN:thiM]
[OR:Staphylococcus carnosus]
SPX017117128321374111142.00E-08[LN:H71057]95
[AC:H71057]
[PN:hypothetical protein PH1158]
[GN:PH1158]
[OR:Pyrococcus horikoshii]
SPX0172172283382246NO-HIT6
SPX01731732834752252031.90E-23[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX017417428352236691276.60E-15“[LN:PT18_YEAST]141
[AC:P25362]
[GN:PET18:HIT2:YCR020C:YCR20C]
[OR:Saccharomyces cerevisiae]
[SR:,Baker′s yeast]
[DE:PET18 PROTEIN]
[SP:P25362]”
SPX01751752836379113713795.20E-216[GI:2239174]116
[LN:SILCT]
[AC:Y07622]
[PN:lactate oxidase]
[GN:lctO]
[FN:lactate utilisation]
[OR:Streptococcus iniae]
SPX01761762837497149111571.60E-228“[LN:SYK_BACSU]144
[AC:P37477]
[GN:LYSS]
[OR:Bacillus subtilis]
[EC:6.1.1.6]
[DE:LYSYL-TRNA SYNTHETASE, (LYSINE--TRNA LIGASE) (LYSRS)]
[SP:P37477]”
SPX017717728382276813512.10E-70“[LN:D71849]195
[AC:D71849]
[PN:amino acid ABC transporter, permease protein]
[GN:jhp1096]
[CL:histidine permease protein M]
[OR:Helicobacter pylori]
[SR:strain J99, , strain J99]
[SR:strain J99, ]”
SPX017817828391273812792.10E-35“[LN:B64666]133
[AC:B64666]
[PN:glutamine ABC transporter, permease protein]
[CL:histidine permease protein M]
[OR:Helicobacter pylori]”
SPX01791792840962882494.10E-30“[LN:B64666]133
[AC:B64666]
[PN:glutamine ABC transporter, permease protein]
[CL:histidine permease protein M]
[OR:Helicobacter pylori]”
SPX0180180284171213925.90E-05[GI:4163988]114
[LN:AF082511]
[AC:AF082511]
[PN:putative ATP-binding protein MglA]
[GN:mglA]
[OR:Treponema denticola]
SPX018118128421695075315.00E-70[LN:H81391]131
[AC:H81391]
[PN:amino-acid ABC transporter ATP-binding protein Cj0469 [imported]]
[GN:Cj0469]
[OR:Campylobacter jejuni]
SPX0182182284367201723.30E-07[LN:G72510]92
[AC:G72510]
[PN:hypothetical protein APE2061]
[GN:APE2061]
[OR:Aeropyrum pernix]
SPX01831832844812431325.50E-12[GI:4204972]111
[LN:LLU60994]
[AC:U60994]
[FN:transport systems for basic amino acids and]
[OR:Leuconostoc lactis]
SPX018418428451855555311.40E-67[LN:C81373]153
[AC:C81373]
[PN:probable amino-acid transporter periplasmic solute-binding protein Cj0982c [imported]]
[GN:Cj0982c]
[OR:Campylobacter jejuni]
SPX018518528462166483536.60E-51[LN:YYBJ_BACSU]95
[AC:P37494]
[GN:YYBJ]
[OR:Bacillus subtilis]
[DE:INTERGENIC REGION]
[SP:P37494]
SPX01861862847235705NO-HIT6
SPX0187187284868204NO-HIT6
SPX01881882849269807NO-HIT6
SPX01891892850255765NO-HIT6
SPX01901902851117351NO-HIT6
SPX0191191285221163310571.30E-140[GI:4009484]124
[LN:AF068902]
[AC:AF068902]
[PN:orotate phosphoribosyltransferase PyrE]
[GN:pyrE]
[OR:Streptococcus pneumoniae]
SPX0192192285323470211731.80E-157[GI:4009483]117
[LN:AF068902]
[AC:AF068902]
[PN:orotidine-5′-decarboxylase PyrF]
[GN:pyrF]
[OR:Streptococcus pneumoniae]
SPX0193193285467201NO-HIT6
SPX01941942855400120019463.00E-251[GI:4009482]114
[LN:AF068902]
[AC:AF068902]
[PN:cell division protein DivIB]
[GN:divIB]
[OR:Streptococcus pneumoniae]
SPX019519528561484441102.20E-07“[GI:6473880]180
[LN:AB027890]
[AC:AB027890]
[PN:Hypothetical protein]
[GN:SPBC3D5.14C]
[OR:Schizosaccharomyces pombe]
[SR:Schizosaccharomyces pombe (strain:968 h90) DNA, clone:TA46]]
SPX01961962857353105917801.40E-242[GI:4009481]131
[LN:AF068902]
[AC:AF068902]
[PN:undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc]
[GN:murG]
[OR:Streptococcus pneumoniae]
SPX01971972858451135322061.20E-297[GI:4009480]120
[LN:AF068902]
[AC:AF068902]
[PN:D-glutamic acid adding enzyme MurD]
[GN:murD]
[OR:Streptococcus pneumoniae]
SPX0198198285921464210621.20E-142[GI:4009479]83
[LN:AF068902]
[AC:AF068902]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX01991992860674202222630[GI:4009478]83
[LN:AF068902]
[AC:AF068902]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX02002002861135405861.80E-05[GI:7576923]109
[LN:AF242367]
[AC:AF242367]
[PN:lactococcin 972]
[GN:lclA]
[OR:Lactococcus lactis subsp. lactis]
SPX0201201286273219NO-HIT6
SPX0202202286385255892.50E-05[LN:T20916]98
[AC:T20916]
[PN:hypothetical protein F14F8.3]
[GN:F14F8.3]
[OR:Caenorhabditis elegans]
SPX02032032864621186317060[LN:TYPA_BACSU]115
[AC:O07631]
[GN:TYPA]
[OR:Bacillus subtilis]
[DE:GTP-BINDING PROTEIN TYPA/BIPA HOMOLOG]
[SP:O07631]
SPX020420428652427261543.00E-34[GI:7328274]103
[LN:SAY14816]
[AC:Y14816]
[PN:hypothetical protein]
[GN:ORF231]
[OR:Staphylococcus aureus]
SPX0205205286666198NO-HIT6
SPX020620628671273811743.80E-28[LN:YQHL_BACSU]141
[AC:P54510]
[GN:YQHL]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 14.6 KD PROTEIN IN GCVT-SPOIIIAA INTERGENIC REGION]
[SP:P54510]
SPX02072072868742221581.80E-17[LN:T44786]87
[AC:T44786]
[PN:hypothetical protein 1 [imported]]
[OR:Bacillus megaterium]
SPX0208208286930390912415.30E-168[LN:T44638]172
[AC:T44638]
[PN:capsular polysaccharide biosynthesis protein cpsY [imported]]
[GN:cpsY]
[CL:probable transcription regulator lsyR]
[OR:Streptococcus agalactiae]
SPX020920928702527564765.30E-66[LN:YQJQ_BACSU]103
[AC:P54554]
[GN:YQJQ]
[OR:Bacillus subtilis]
[EC:1.-.-.-]
[DE:(EC 1.-.-.-)]
[SP:P54554]
SPX021021028713109303689.50E-98[LN:YQJK_BACSU]137
[AC:P54548]
[GN:YQJK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 34.0 KD PROTEIN IN GLNQ-ANSR INTERGENIC REGION]
[SP:P54548]
SPX02112112872208624NO-HIT6
SPX0212212287341312397921.40E-103[LN:B69888]187
[AC:B69888]
[PN:GTP-binding protein proteinase modulator homolog ynbA]
[GN:ynbA]
[CL:GTP-binding protein hflX:translation elongation factor Tu homology]
[OR:Bacillus subtilis]
SPX021321328743129363177.10E-70[LN:G69657]159
[AC:G69657]
[PN:tRNA isopentenylpyrophosphate transferase miaA]
[GN:miaA]
[CL:delta(2)-isopentenylpyrophosphate transferase]
[OR:Bacillus subtilis]
SPX0214214287563189NO-HIT6
SPX02152152876661981296.10E-12“[LN:TYSY_LACLA]160
[AC:P19368]
[GN:THYA]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.1.1.45]
[DE:THYMIDYLATE SYNTHASE, (TS)]
[SP:P19368]]
SPX021621628772216633181.20E-39[GI:7328278]103
[LN:SAY14816]
[AC:Y14816]
[PN:hypothetical protein]
[GN:ORF242]
[OR:Staphylococcus aureus]
SPX021721728782126366914.80E-91[LN:B69997]130
[AC:B69997]
[PN:conserved hypothetical protein ytmQ]
[GN:ytmQ]
[CL:hypothetical protein HI0340]
[OR:Bacillus subtilis]
SPX0218218287989267NO-HIT6
SPX021921928801033092156.90E-25[LN:YLXS_BACSU]137
[AC:P32726]
[GN:YLXS]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 17.6 KD PROTEIN IN NUSA 5′REGION (P15A) (ORF1)]
[SP:P32726]
SPX0220220288137911377156.00E-122[GI:2634032]111
[LN:BSUB0009]
[AC:Z99112:AL009126]
[GN:nusA]
[FN:transcription termination]
[OR:Bacillus subtilis]
SPX02212212882982942201.70E-25[LN:YLXR_BACSU]144
[AC:P32728]
[GN:YLXR]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 10.4 KD PROTEIN IN NUSA-INFB INTERGENIC REGION (ORF3)]
[SP:P32728]
SPX022222228831003002593.80E-31“[LN:YLXQ_ENTFC]144
[AC:P55768]
[OR:Enterococcus faecium]
[SR:,Streptococcus faecium]
[DE:PROBABLE RIBOSOMAL PROTEIN IN INFB 5′REGION]
[SP:P55768]]
SPX02232232884165495NO-HIT6
SPX02242242885931279327680[GI:3947714]142
[LN:SAAJ3164]
[AC:AJ003164]
[PN:initiation factor IF2]
[GN:infB]
[FN:translation initiation factor]
[OR:Streptococcus agalactiae]
SPX0225225288682246NO-HIT6
SPX022622628871173514782.00E-61[GI:3947715]136
[LN:SAAJ3164]
[AC:AJ003164]
[PN:ribosome binding factor A]
[GN:rbfA]
[FN:ribosome maturation]
[OR:Streptococcus agalactiae]
SPX022722728882607802173.30E-40[LN:T35040]110
[AC:T35040]
[PN:hypothetical protein SC4G2.05 SC4G2.05]
[GN:SC4G2.05]
[OR:Streptomyces coelicolor]
SPX0228228288984252NO-HIT6
SPX0229229289074222NO-HIT6
SPX02302302891651952022.70E-24[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX02312312892782341024.60E-08[LN:A69271]140
[AC:A69271]
[PN:hypothetical protein AF0169]
[CL:Archaeoglobus fulgidus hypothetical protein AF0169]
[OR:Archaeoglobus fulgidus]
SPX0232232289344513351231.30E-41[LN:B69271]84
[AC:B69271]
[PN:hypothetical protein AF0170]
[OR:Archaeoglobus fulgidus]
SPX0233233289485255NO-HIT6
SPX02342342895132396NO-HIT6
SPX0235235289669207NO-HIT6
SPX02362362897150450NO-HIT6
SPX023723728981865581482.10E-18[LN:YP20_BACLI]106
[AC:P05332]
[GN:P20]
[OR:Bacillus licheniformis]
[DE:HYPOTHETICAL P20 PROTEIN]
[SP:P05332]
SPX02382382899321963NO-HIT6
SPX02392392900884265215940“[LN:SYV_BACSU]144
[AC:Q05873]
[GN:VALS]
[OR:Bacillus subtilis]
[EC:6.1.1.9]
[DE:VALYL-TRNA SYNTHETASE, (VALINE--TRNA LIGASE) (VALRS)]
[SP:Q05873]]
SPX024024029012527566427.80E-85“[LN:B71947]145
[AC:B71947]
[PN:hypothetical protein jhp0330]
[GN:jhp0330]
[OR:Helicobacter pylori]
[SR:strain J99, , strain J99]
[SR:strain J99, ]]
SPX02412412902268804911.80E-05“[LN:Y4LH_RHISN]128
[AC:P55548]
[GN:Y4LH]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:HYPOTHETICAL 22.4 KD PROTEIN Y4LH]
[SP:P55548]]
SPX02422422903952853873.10E-49[GI:1490399]90
[LN:SPPARCETP]
[AC:Z67739]
[PN:DNA transposase]
[OR:Streptococcus pneumoniae]
SPX024324329041023063232.70E-40[GI:1490399]90
[LN:SPPARCETP]
[AC:Z67739]
[PN:DNA transposase]
[OR:Streptococcus pneumoniae]
SPX02442442905912733152.50E-39[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX02452452906922761353.80E-13[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX024624629074221266NO-HIT6
SPX0247247290839911971099.90E-10[GI:6689196]109
[LN:SCE20]
[AC:AL136058]
[PN:putative helicase]
[GN:SCE20.37]
[OR:Streptomyces coelicolor A3(2)]
SPX0248248290998294NO-HIT6
SPX024924929102808404892.30E-81[LN:LICT_BACSU]116
[AC:P39805]
[GN:LICT:N15A]
[OR:Bacillus subtilis]
[DE:TRANSCRIPTION ANTITERMINATOR LICT]
[SP:P39805]
SPX0250250291161318395348.10E-147“[LN:PTBA_BACSU]149
[AC:P40739:Q45661]
[GN:BGLP:N17C]
[OR:Bacillus subtilis]
[EC:2.7.1.69]
[DE:ENZYME II, ABC COMPONENT), (EII-BGL)]
[SP:P40739:Q45661]]
SPX02512512912472141610463.70E-228“[LN:ABGA_CLOLO]127
[AC:Q46130]
[GN:ABGA]
[OR:Clostridium longisporum]
[EC:3.2.1.86]
[DE:6-PHOSPHO-BETA-GLUCOSIDASE,]
[SP:Q46130]]
SPX0252252291334910476563.10E-156[LN:SYFA_BACSU]139
[AC:P17921:P94539]
[GN:PHES]
[OR:Bacillus subtilis]
[EC:6.1.1.20]
[DE:-TRNA LIGASE ALPHA CHAIN) (PHERS)]
[SP:P17921:P94539]
SPX02532532914331993NO-HIT6
SPX025425429151705103331.80E-41“[LN:YPIP_LACDL]141
[AC:P46543]
[OR:Lactobacillus delbrueckii]
[SR:,subsplactis]
[DE:HYPOTHETICAL 19.8 KD PROTEIN IN PEPI 3′REGION]
[SP:P46543]]
SPX0255255291680124033122.20E-132“[LN:SYFB_SYNY3]154
[AC:P74296]
[GN:PHET:SLL1553]
[OR:Synechocystis sp]
[SR:,strain PCC 6803]
[EC:6.1.1.20]
[DE:TRNA LIGASE BETA CHAIN) (PHERS)]
[SP:P74296]]
SPX02562562917296888NO-HIT6
SPX025725729181494474374.90E-55[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX02582582919892672452.00E-28[LN:Y659_HAEIN]112
[AC:P44030]
[GN:HI0659]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI0659]
[SP:P44030]
SPX0259259292099297NO-HIT6
SPX02602602921750225013096.60E-297“[LN:C81326]175
[AC:C81326]
[PN:5-methyltetrahydropteroyltriglutamate-- homocystei methyltransferase, Cj1201 [imported]]
[GN:metE:Cj1201]
[OR:Campylobacter jejuni]
[EC:2.1.1.14]]
SPX026126129222898672613.90E-77“[LN:D81326]147
[AC:D81326]
[PN:5,10-methylenetetrahydrofolate reductase, Cj1202 [imported]]
[GN:metF:Cj1202]
[OR:Campylobacter jejuni]
[EC:1.7.99.5]]
SPX0262262292390270NO-HIT6
SPX02632632924738221413233.80E-298[LN:PNPA_BACSU]151
[AC:P50849]
[GN:PNPA:COMR]
[OR:Bacillus subtilis]
[EC:2.7.7.8]
[DE:PHOSPHORYLASE) (PNPASE) (VEGETATIVE PROTEIN 15) (VEG15)]
[SP:P50849]
SPX026426429252066184931.20E-63[GI:6899995]110
[LN:CST130879]
[AC:AJ130879]
[PN:serine acetyltransferase]
[GN:cysE]
[OR:Clostridium sticklandii]
SPX026526529262958851133.80E-07[LN:E69786]190
[AC:E69786]
[PN:ribosomal-protein-alanine N-acetyltransfer homolog ydiD]
[GN:ydiD]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]
[OR:Bacillus subtilis]
SPX02662662927152456NO-HIT6
SPX0267267292844813445709.00E-167[GI:6899996]112
[LN:CST130879]
[AC:AJ130879]
[PN:cysteinyl tRNA synthetase]
[GN:cysRS]
[OR:Clostridium sticklandii]
SPX026826829291293873166.30E-39[LN:C69742]97
[AC:C69742]
[PN:conserved hypothetical protein yazC]
[GN:yazC]
[OR:Bacillus subtilis]
SPX026926929302958852243.10E-30[LN:LRPR_STREQ]105
[AC:Q54087]
[GN:LRP]
[OR:Streptococcus equisimilis]
[DE:LEUCINE RICH PROTEIN]
[SP:Q54087]
SPX0270270293188264NO-HIT6
SPX02712712932200600NO-HIT6
SPX0272272293352156873.30E-06[LN:D75542]90
[AC:D75542]
[PN:hypothetical protein]
[GN:DR0254]
[OR:Deinococcus radiodurans]
SPX02732732934822462471.10E-29[LN:F81737]131
[AC:F81737]
[PN:hypothetical protein TC0129 [imported]]
[GN:TC0129]
[OR:Chlamydia muridarum:Chlamydia trachomatis MoPn]
SPX02742742935782341434.90E-15[LN:F71245]95
[AC:F71245]
[PN:hypothetical protein PHS004]
[GN:PHS004]
[OR:Pyrococcus horikoshii]
SPX0275275293672216NO-HIT6
SPX0276276293763189682.40E-07[LN:C64571]134
[AC:C64571]
[PN:hypothetical protein HP0411]
[CL:Helicobacter pylori hypothetical protein HP0411]
[OR:Helicobacter pylori]
SPX027727729383129361942.60E-36“[GI:773349]142
[LN:BSU20445]
[AC:U20445]
[PN:BirA protein]
[GN:birA]
[FN:biotin protein ligase, biotin operon repressor]
[OR:Bacillus subtilis]]
SPX027827829392878612551.70E-56[LN:MSMR_STRMU]110
[AC:Q00753]
[GN:MSMR]
[OR:Streptococcus mutans]
[DE:MSM OPERON REGULATORY PROTEIN]
[SP:Q00753]
SPX02792792940721216325280“[LN:AGAL_STRMU]128
[AC:P27756]
[GN:AGA]
[OR:Streptococcus mutans]
[EC:3.2.1.22]
[DE:ALPHA-GALACTOSIDASE, (MELIBIASE)]
[SP:P27756]]
SPX02802802941420126011062.40E-180[LN:MSME_STRMU]121
[AC:Q00749]
[GN:MSME]
[OR:Streptococcus mutans]
[DE:MULTIPLE SUGAR-BINDING PROTEIN PRECURSOR]
[SP:Q00749]
SPX0281281294282246NO-HIT6
SPX0282282294328986711881.40E-166[LN:MSMF_STRMU]142
[AC:Q00750]
[GN:MSMF]
[OR:Streptococcus mutans]
[DE:MULTIPLE SUGAR-BINDING TRANSPORT SYSTEM PERMEASE PROTEIN MSMF]
[SP:Q00750]
SPX0283283294427883411743.40E-164[LN:MSMG_STRMU]142
[AC:Q00751]
[GN:MSMG]
[OR:Streptococcus mutans]
[DE:MULTIPLE SUGAR-BINDING TRANSPORT SYSTEM PERMEASE PROTEIN MSMG]
[SP:Q00751]
SPX02842842945482144621546.70E-294“[LN:A27626]110
[AC:A27626]
[PN:sucrose phosphorylase,]
[CL:gtfA protein]
[OR:Streptococcus mutans]
[EC:2.4.1.7]]
SPX028528529463981194NO-HIT6
SPX02862862947134402NO-HIT6
SPX02872872948662198633410[LN:AMIA_STRPN]142
[AC:P18791:P18792]
[GN:AMIA]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE-BINDING PROTEIN AMIA PRECURSOR]
[SP:P18791:P18792]
SPX02882882949499149725380[LN:AMIC_STRPN]129
[AC:P18793]
[GN:AMIC]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN AMIC]
[SP:P18793]
SPX0289289295030992715641.10E-217[LN:AMID_STRPN]129
[AC:P18794]
[GN:AMID]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN AMID]
[SP:P18794]
SPX02902902951356106818062.10E-245[LN:AMIE_STRPN]132
[AC:P18765]
[GN:AMIE]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN AMIE]
[SP:P18765]
SPX02912912952113339NO-HIT6
SPX0292292295330992715345.40E-208[LN:AMIF_STRPN]132
[AC:P18766]
[GN:AMIF]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE TRANSPORT ATP-BINDING PROTEIN AMIF]
[SP:P18766]
SPX02932932954419125720391.30E-284[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX02942942955962882741.10E-34[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX029529529561735198406.50E-114[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX029629629572377114712.40E-60[LN:TRER_BACSU]120
[AC:P39796]
[GN:TRER]
[OR:Bacillus subtilis]
[DE:TREHALOSE OPERON TRANSCRIPTIONAL REPRESSOR]
[SP:P39796]
SPX0297297295865619683837.20E-135[LN:PTTB_ECOLI]114
[AC:P36672]
[GN:TREB]
[OR:Escherichia coli]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EII-TRE)]
[SP:P36672]
SPX02982982959542162616172.00E-272[GI:2208998]102
[LN:SSU35633]
[AC:U35633]
[PN:dextran glucosidase DexS]
[GN:dexS]
[OR:Streptococcus suis]
SPX02992992960601801252.30E-12[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX03003002961842521044.40E-09[GI:6899236]116
[LN:AE002123]
[AC:AE002123:AF222894]
[PN:conserved hypothetical]
[GN:UU265]
[OR:Ureaplasma urealyticum]
SPX030130129622657954762.60E-84[GI:2462097]95
[LN:BCBCTLGLR]
[AC:Y10927]
[PN:glutamate racemase]
[GN:bcglr]
[OR:Bacillus cereus]
SPX030230229632978912739.10E-35[LN:C69986]165
[AC:C69986]
[PN:conserved hypothetical protein ysnA]
[GN:ysnA]
[CL:Methanococcus jannaschii conserved hypothetical protein MJ0226]
[OR:Bacillus subtilis]
SPX03033032964742221581.60E-15[LN:YGGV_ECOLI]143
[AC:P52061]
[GN:YGGV]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 21.0 KD PROTEIN IN GSHB-ANSB INTERGENIC REGION (O197)]
[SP:P52061]
SPX030430429651745222298.10E-27[LN:YSNB_BACSU]136
[AC:P94559]
[GN:YSNB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 19.2 KD PROTEIN IN RPH-ILVB INTERGENIC REGION]
[SP:P94559]
SPX03053052966154462758.30E-08[LN:A69866]136
[AC:A69866]
[PN:hypothetical protein ykuL]
[GN:ykuL]
[CL:Bacillus subtilis hypothetical protein ykuL]
[OR:Bacillus subtilis]
SPX03063062967247741610.0006[LN:A75153]164
[AC:A75153]
[PN:integrase/recombinase xerd PAB0255]
[GN:xerD-like:PAB0255]
[CL:probable site-specific integrase/recombinase XerC]
[OR:Pyrococcus abyssi]
SPX030730729682437292331.60E-40[LN:YPUG_BACSU]145
[AC:P35154]
[GN:YPUG]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 29.6 KD PROTEIN IN RIBT-DACB INTERGENIC REGION (ORFX7)]
[SP:P35154]
SPX030830829691905702162.00E-28[LN:Y214_MYCPN]106
[AC:P75477]
[OR:Mycoplasma pneumoniae]
[DE:HYPOTHETICAL PROTEIN MG214 HOMOLOG]
[SP:P75477]
SPX030930929702417236605.60E-86[LN:RLUB_BACSU]138
[AC:P35159]
[GN:RLUB]
[OR:Bacillus subtilis]
[EC:4.2.1.70]
[DE:(PSEUDOURIDYLATE SYNTHASE) (URACIL HYDROLYASE)]
[SP:P35159]
SPX03103102971812431661.10E-32[LN:G72251]139
[AC:G72251]
[PN:conserved hypothetical protein]
[GN:TM1462]
[CL:conserved hypothetical protein HI1000]
[OR:Thermotoga maritima]
SPX03113112972175525NO-HIT6
SPX031231229733229662182.70E-57[LN:E69763]146
[AC:E69763]
[PN:probable ferrichrome ABC transporter yclQ]
[GN:yclQ]
[CL:iron(III) dicitrate transport protein]
[OR:Bacillus subtilis]
SPX031331329742517537022.90E-92[LN:D69763]194
[AC:D69763]
[PN:ferrichrome ABC transporter (ATP-binding p) homolog yclP]
[GN:yclP]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX0314314297567201896.60E-07[LN:G72510]92
[AC:G72510]
[PN:hypothetical protein APE2061]
[GN:APE2061]
[OR:Aeropyrum pernix]
SPX031531529763199574748.60E-64[LN:C69763]146
[AC:C69763]
[PN:ferrichrome ABC transporter (permease) homolog yclO]
[GN:yclO]
[CL:ferrichrome ABC transporter]
[OR:Bacillus subtilis]
SPX031631629773209606252.80E-84[LN:B69763]153
[AC:B69763]
[PN:ferrichrome ABC transporter (permease) homolog yclN]
[GN:yclN]
[CL:vitamin B12 transport protein btuC]
[OR:Bacillus subtilis]
SPX031731729781364082883.50E-36[GI:6707010]98
[LN:AF109295]
[AC:AF109295:AF022796]
[PN:GalE]
[GN:galE]
[OR:Staphylococcus carnosus]
SPX03183182979812431646.20E-18[GI:3703059]105
[LN:AF082009]
[AC:AF082009]
[PN:UDP-galactose-4-epimerase]
[GN:galE]
[OR:Lactococcus lactis]
SPX0319319298035410623888.30E-143“[LN:PEPA_LACLC]162
[AC:Q48677]
[GN:PEPA]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[EC:3.4.11.7]
[DE:GLUTAMYL-AMINOPEPTIDASE,]
[SP:Q48677]]
SPX0320320298199297NO-HIT6
SPX0321321298263189NO-HIT6
SPX03223222983148444870.00059[GI:2791904]78
[LN:SSK3MECA1]
[AC:Y13052]
[GN:ORF145]
[OR:Staphylococcus sciuri]
SPX03233232984255765NO-HIT6
SPX0324324298524372912118.40E-163[GI:5579394]117
[LN:AF162655]
[AC:AF162655]
[PN:choline transporter]
[GN:proV]
[FN:ATPase]
[OR:Streptococcus pneumoniae]
SPX032532529862987NO-HIT6
SPX0326326298731193314342.40E-200[LN:T44634]100
[AC:T44634]
[PN:choline transporter [imported]]
[GN:proWX]
[OR:Streptococcus pneumoniae]
SPX0327327298821063010423.30E-137[LN:T44634]100
[AC:T44634]
[PN:choline transporter [imported]]
[GN:proWX]
[OR:Streptococcus pneumoniae]
SPX032832829892708101251.90E-15[LN:YA7B_HAEIN]130
[AC:Q57425:P96338]
[GN:HI1077.1]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI1077.1]
[SP:Q57425:P96338]
SPX032932929901795371508.10E-17[GI:5881867]139
[LN:SC5G9]
[AC:AL117385]
[PN:putative tetR-family transcriptional regulator]
[GN:SC5G9.19c]
[OR:Streptomyces coelicolor A3(2)]
SPX033033029913009002025.60E-39[GI:1944409]151
[LN:D87026]
[AC:D87026:D28136]
[PN:membrane protein]
[OR:Bacillus stearothermophilus]
[SR:Bacillus stearothermophilus (strain:TRBE14) DNA]
SPX033133129921183542823.60E-34[LN:B69970]144
[AC:B69970]
[PN:transcription regulator MerR family homolog yraB]
[GN:yraB]
[CL:transcription repressor glnR]
[OR:Bacillus subtilis]
SPX0332332299334610384033.80E-82[LN:T44975]146
[AC:T44975]
[PN:dehydrogenase [imported]]
[CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology]
[OR:Haloferax volcanii]
SPX0333333299433610087294.00E-144[GI:4097439]90
[LN:STU61402]
[AC:U61402]
[PN:GalR]
[GN:galR]
[OR:Streptococcus thermophilus]
SPX03343342995393117916743.10E-227[GI:4097440]125
[LN:STU61402]
[AC:U61402]
[PN:galactokinase]
[GN:galK]
[FN:galactose metabolism]
[OR:Streptococcus thermophilus]
SPX03353352996494148216121.90E-230[GI:4097441]139
[LN:STU61402]
[AC:U61402]
[PN:gal-1-P uridylyltransferase]
[GN:galT]
[FN:galactose metabolism]
[OR:Streptococcus thermophilus]
SPX033633629971354054671.10E-60[GI:1196924]81
[LN:STRDPN2A]
[AC:M14339]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX0337337299829688814616.00E-199[LN:MT21_STRPN]137
[AC:P04043]
[GN:DPNM]
[OR:Streptococcus pneumoniae]
[EC:2.1.1.72]
[DE:METHYLTRANSFERASE DPNII 1) (M.DPNII 1)]
[SP:P04043]
SPX0338338299925777113662.60E-183[LN:MT22_STRPN]137
[AC:P09358]
[GN:DPNA]
[OR:Streptococcus pneumoniae]
[EC:2.1.1.72]
[DE:METHYLTRANSFERASE DPNII 2) (M.DPNII 2)]
[SP:P09358]
SPX0339339300028986714925.50E-202[LN:T2D2_STRPN]108
[AC:P09357]
[GN:DPNB]
[OR:Streptococcus pneumoniae]
[EC:3.1.21.4]
[DE:(R.DPNII)]
[SP:P09357]
SPX034034030011193574621.20E-61[GI:6978345]81
[LN:STRDPN2A]
[AC:M14339]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX034134130022838494368.70E-87[LN:YUNK_BACSU]136
[AC:O32140]
[GN:YUNK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 44.9 KD PROTEIN IN HOM-MRGA INTERGENIC REGION]
[SP:O32140]
SPX034234230031945827863.40E-105[GI:7160242]120
[LN:SPN272465]
[AC:AJ272465]
[PN:xanthine phosphoribosyltransferase]
[GN:xpt]
[OR:Streptococcus pneumoniae]
SPX0343343300458174797.70E-11[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX03443443005802401135.90E-10[LN:C75408]90
[AC:C75408]
[PN:hypothetical protein]
[GN:DR1341]
[OR:Deinococcus radiodurans]
SPX0345345300627682814328.60E-192“[LN:EXOA_STRPN]122
[AC:P21998]
[GN:EXOA]
[OR:Streptococcus pneumoniae]
[EC:3.1.11.2]
[DE:EXODEOXYRIBONUCLEASE,]
[SP:P21998]]
SPX0346346300776228NO-HIT6
SPX0347347300890270NO-HIT6
SPX034834830091775311329.60E-19[LN:F69972]128
[AC:F69972]
[PN:probable membrane protein yrbG]
[GN:yrbG]
[CL:probable membrane protein ycaP]
[OR:Bacillus subtilis]
SPX03493493010792371295.90E-21[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX0350350301158217466851.90E-170[LN:A69829]188
[AC:A69829]
[PN:ABC transporter (ATP-binding protein) homolog yheI]
[GN:yheI]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX035135130122948823646.80E-49[LN:H69828]188
[AC:H69828]
[PN:ABC transporter (ATP-binding protein) homolog yheH]
[GN:yheH]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX0352352301369207820.00022[LN:H69828]188
[AC:H69828]
[PN:ABC transporter (ATP-binding protein) homolog yheH]
[GN:yheH]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX035335330142647923833.90E-79[LN:H69828]188
[AC:H69828]
[PN:ABC transporter (ATP-binding protein) homolog yheH]
[GN:yheH]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX035435430152326966321.10E-83[GI:6601354]115
[LN:AF164515]
[AC:AF164515]
[PN:putative glycosyltransferase Cps7F]
[GN:cps7F]
[OR:Streptococcus suis]
SPX0355355301640912279734.70E-214[GI:6601355]86
[LN:AF164515]
[AC:AF164515]
[PN:Cps7G]
[GN:cps7G]
[OR:Streptococcus suis]
SPX0356356301763189NO-HIT6
SPX0357357301889267NO-HIT6
SPX0358358301970921271074.60E-08[GI:2952545]109
[LN:AF051898]
[AC:AF051898]
[PN:coronin binding protein]
[GN:DB10]
[OR:Dictyostelium discoideum]
SPX0359359302082246NO-HIT6
SPX0360360302169207NO-HIT6
SPX0361361302295285NO-HIT6
SPX03623623023962882896.60E-34[GI:43589]103
[LN:HILIC3]
[AC:X57315]
[PN:UDP-galactose-4-epimerase]
[GN:galE]
[OR:Haemophilus influenzae]
SPX0363363302466198NO-HIT6
SPX03643643025220660NO-HIT6
SPX0365365302635610682862.20E-30“[LN:Y4FP_RHISN]162
[AC:P55454]
[GN:Y4FP]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:PROBABLE ABC TRANSPORTER PERIPLASMIC BINDING PROTEIN Y4FP PRECURSOR]
[SP:P55454]]
SPX0366366302733710113953.30E-90“[LN:A70180]237
[AC:A70180]
[PN:spermidine/putrescine ABC transporter, ATP-binding protein (potA) homolog]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]
”””
SPX0367367302856416924331.50E-93“[LN:Y4FN_RHISN]141
[AC:P55452]
[GN:Y4FN]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:PROBABLE ABC TRANSPORTER PERMEASE PROTEIN Y4FN]
[SP:P55452]”
SPX036836830292377111924.80E-28[LN:Y647_HAEIN]126
[AC:Q57424:O05028]
[GN:HI0647]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI0647]
[SP:Q57424:O05028]
SPX03693693030103309NO-HIT6
SPX0370370303133410021443.70E-25[LN:CCPA_BACME]145
[AC:P46828]
[GN:CCPA]
[OR:Bacillus megaterium]
[DE:GLUCOSE-RESISTANCE AMYLASE REGULATOR (CATABOLITE CONTROL PROTEIN)]
[SP:P46828]
SPX0371371303266198NO-HIT6
SPX0372372303369207NO-HIT6
SPX03733733034488146411002.50E-173“[LN:TRPE_LACLA]168
[AC:Q02001]
[GN:TRPE]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.3.27]
[DE:ANTHRANILATE SYNTHASE COMPONENT I,]
[SP:Q02001]”
SPX03743743035672011086.30E-10[LN:C72489]92
[AC:C72489]
[PN:hypothetical protein APE2554]
[GN:APE2554]
[OR:Aeropyrum pernix]
SPX037537530361895674408.80E-75“[LN:TRPG_LACLA]146
[AC:Q02003]
[GN:TRPG]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.3.27]
[DE:TRANSFERASE)]
[SP:Q02003]”
SPX03763763037335100510089.70E-134“[LN:TRPD_LACLA]173
[AC:Q02000]
[GN:TRPD]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.4.2.18]
[DE:ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE,]
[SP:Q02000]”
SPX037737730382567684466.20E-107“[LN:TRPC_LACLA]178
[AC:Q01999]
[GN:TRPC]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.1.48]
[DE:INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE, (IGPS)]
[SP:Q01999]”
SPX037837830392106302253.50E-49“[LN:TRPF_LACLA]185
[AC:Q02002]
[GN:TRPF]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:5.3.1.24]
[DE:N-(5′-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE, (PRAI)]
[SP:Q02002]”
SPX0379379304040812249309.00E-225“[LN:TRPB_LACLA]165
[AC:Q01998]
[GN:TRPB]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.2.1.20]
[DE:TRYPTOPHAN SYNTHASE BETA CHAIN,]
[SP:Q01998]”
SPX0380380304127883411375.00E-153[GI:5231181]117
[LN:AF157817]
[AC:AF157817]
[PN:tryptophan synthase alpha chain]
[GN:trpA]
[OR:Streptococcus pneumoniae]
SPX0381381304268204NO-HIT6
SPX03823823043244732NO-HIT6
SPX038338330443841152922.70E-13[LN:H70940]116
[AC:H70940]
[PN:probable helix-turn-helix motif at aa 18-39]
[GN:Rv2017]
[OR:Mycobacterium tuberculosis]
SPX038438430452206601091.00E-14[LN:B72220]124
[AC:B72220]
[PN:type IV prepilin peptidase]
[GN:TM1696]
[CL:type IV prepilin peptidase]
[OR:Thermotoga maritima]
SPX03853853046149447920.00011[LN:E72312]169
[AC:E72312]
[PN:conserved hypothetical protein]
[GN:TM0968]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ]
[OR:Thermotoga maritima]
SPX038638630471043121381.30E-12“[GI:6332767]194
[LN:AB033763]
[AC:AB033763:AB014419:AB014429:AB014439]
[PN:hypothetical protein]
[OR:Staphylococcus aureus]
[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”
SPX0387387304868204988.10E-08[GI:2772940]116
[LN:AF034574]
[AC:AF034574]
[PN:putative cruciform DNA binding protein]
[GN:Gv1]
[OR:Glomus versiforme]
SPX038838830492036095158.70E-64[GI:727436]61
[LN:LLU23376]
[AC:U23376]
[OR:Lactococcus lactis]
SPX03893893050191573NO-HIT6
SPX0390390305151315391936.90E-35“[GI:6782400]171
[LN:STC133440]
[AC:AJ133440]
[PN:multigene regulator protein Mgc, putative]
[GN:mgc]
[FN:gene regulatory function, putative]
[OR:Streptococcus dysgalactiae]”
SPX0391391305233410021853.80E-46[LN:SCRR_STRMU]137
[AC:Q54430]
[GN:SCRR]
[OR:Streptococcus mutans]
[DE:SUCROSE OPERON REPRESSOR (SCR OPERON REGULATORY PROTEIN)]
[SP:Q54430]
SPX039239230533159453762.50E-89[LN:A69653]125
[AC:A69653]
[PN:transmembrane lipoprotein lplB]
[GN:lplB]
[CL:inner membrane protein ugpA]
[OR:Bacillus subtilis]
SPX039339330543069184501.20E-73[LN:LPLC_BACSU]90
[AC:P39129]
[GN:LPLC]
[OR:Bacillus subtilis]
[DE:LPLC PROTEIN]
[SP:P39129]
SPX0394394305553916171672.90E-15[GI:4056657]136
[LN:AF098273]
[AC:AF098273]
[PN:peripheral protein]
[GN:glucuronic acid catabolism operon]
[OR:Bacillus stearothermophilus]
SPX03953953056141423NO-HIT6
SPX0396396305744013203052.30E-76“[LN:RAFD_ECOLI]125
[AC:P16553]
[GN:RAFD]
[OR:Escherichia coli]
[EC:3.2.1.26]
[DE:RAFFINOSE INVERTASE, (INVERTASE)]
[SP:P16553]”
SPX0397397305842412727227.10E-167[LN:D69981]163
[AC:D69981]
[PN:conserved hypothetical protein yrvN]
[GN:yrvN]
[CL:Haemophilus influenzae conserved hypothetical protein HI1590]
[OR:Bacillus subtilis]
SPX0398398305974222NO-HIT6
SPX0399399306060180NO-HIT6
SPX0400400306184252NO-HIT6
SPX04014013062151453924.90E-09[LN:T13557]146
[AC:T13557]
[PN:hypothetical protein 17]
[CL:Archaeoglobus fulgidus conserved hypothetical protein AF1072]
[OR:Bacillus phage phi-105]
SPX04024023063157471NO-HIT6
SPX040340330643631089NO-HIT6
SPX0404404306534510351308.00E-15[GI:758793]72
[LN:ECU23723]
[AC:U23723]
[FN:unknown]
[OR:Escherichia coli]
SPX040540530667482244680.00048[GI:758794]72
[LN:ECU23723]
[AC:U23723]
[FN:unknown]
[OR:Escherichia coli]
SPX040640630673401020NO-HIT6
SPX040740730683179513951.40E-81“[LN:T43740]215
[AC:T43740]
[PN:probable ribosomal protein L11 methyltransferase, [imported]
:hypothetical protein 35]
[CL:ribosomal protein L11 methyltransferase:bioC homology]
[OR:Listeria monocytogenes]
[EC:2.1.1.-]”
SPX040840830692487444611.90E-64[LN:T43741]104
[AC:T43741]
[PN:conserved hypothetical protein orf29 [imported]]
[OR:Listeria monocytogenes]
SPX0409409307059917973002.10E-57“[LN:PEPF_BACSU]123
[AC:O31605]
[GN:YJBG]
[OR:Bacillus subtilis]
[EC:3.4.24.-]
[DE:OLIGOENDOPEPTIDASE F HOMOLOG,]
[SP:O31605]”
SPX041041030712266783121.80E-58[LN:D69780]87
[AC:D69780]
[PN:hypothetical protein ydfF]
[GN:ydfF]
[OR:Bacillus subtilis]
SPX041141130722176513941.40E-54[LN:G69803]188
[AC:G69803]
[PN:ABC transporter (ATP-binding protein) homolog yfiL]
[GN:yfiL]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX041241230732557653464.20E-44“[LN:NODJ_RHILV]126
[AC:P06755]
[GN:NODJ]
[OR:Rhizobium leguminosarum]
[SR:,biovar viciae]
[DE:NODULATION PROTEIN J]
[SP:P06755]”
SPX04134133074264792NO-HIT6
SPX041441430752106302573.90E-39“[LN:A69428]130
[AC:A69428]
[PN:glycerol uptake facilitator, MIP channel (glpF) homolog]
[CL:nodulin-26]
[OR:Archaeoglobus fulgidus]”
SPX0415415307660180NO-HIT6
SPX041641630771915734671.10E-60[LN:D69868]128
[AC:D69868]
[PN:conserved hypothetical protein ykvM]
[GN:ykvM]
[CL:hypothetical protein ykvM]
[OR:Bacillus subtilis]
SPX041741730781053151931.80E-43[GI:5640117]129
[LN:LMO133006]
[AC:AJ133006]
[PN:thioredoxin]
[GN:trxA]
[FN:thiol:disulfide interchange]
[OR:Listeria monocytogenes]
SPX04184183079101303NO-HIT6
SPX0419419308067201NO-HIT6
SPX0420420308175225NO-HIT6
SPX042142130823189544332.70E-56[LN:YQJA_BACSU]137
[AC:P54538]
[GN:YQJA]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 37.1 KD PROTEIN IN BMRU-ANSR INTERGENIC REGION]
[SP:P54538]
SPX042242230832878617451.50E-100[LN:YGJU_HAEIN]114
[AC:P45246]
[GN:HI1545]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL SYMPORTER HI1545]
[SP:P45246]
SPX04234233084752251534.00E-15[LN:YGJU_ECOLI]143
[AC:P42602]
[GN:YGJU]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 43.5 KD PROTEIN IN EBGC-UXAA INTERGENIC REGION (O414)]
[SP:P42602]
SPX042442430851404201632.90E-17“[GI:2828366]128
[LN:AB010789]
[AC:AB010789]
[OR:Lactococcus lactis]
[SR:Lactococcus lactis (sub_species:lactis, strain:01-7) DNA]”
SPX04254253086661981021.80E-07[LN:A69867]174
[AC:A69867]
[PN:conserved hypothetical protein ykuT]
[GN:ykuT]
[CL:Escherichia coli hypothetical 30.9K protein (sbm-fba intergenic region)]
[OR:Bacillus subtilis]
SPX0426426308759177NO-HIT6
SPX042742730883039092701.70E-35[GI:5123526]112
[LN:AF036485]
[AC:AF036485:AF036486:AF036487:U93364]
[PN:hypothetical protein]
[OR:Plasmid pNZ4000]
SPX042842830891765283269.70E-41[LN:YQEG_BACSU]137
[AC:P54452]
[GN:YQEG]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 20.1 KD PROTEIN IN NUCB-AROD INTERGENIC REGION]
[SP:P54452]
SPX04294293090369110710371.30E-164[LN:YQEH_BACSU]137
[AC:P54453]
[GN:YQEH]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 41.0 KD PROTEIN IN NUCB-AROD INTERGENIC REGION]
[SP:P54453]
SPX043043030911043122115.20E-24[LN:YQEI_BACSU]138
[AC:P54454]
[GN:YQEI]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 10.8 KD PROTEIN IN AROD-COMER INTERGENIC REGION]
[SP:P54454]
SPX043143130922056154911.30E-63[LN:YQEJ_BACSU]138
[AC:P54455]
[GN:YQEJ]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 22.2 KD PROTEIN IN AROD-COMER INTERGENIC REGION]
[SP:P54455]
SPX043243230931985943752.90E-47[LN:YQEK_BACSU]138
[AC:P54456]
[GN:YQEK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 21.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION]
[SP:P54456]
SPX043343330941675011104.90E-10[GI:7160132]119
[LN:SC5C11]
[AC:AL158060]
[PN:putative isochorismatase.]
[GN:SC5C11.12]
[OR:Streptomyces coelicolor A3(2)]
SPX043443430951183542677.00E-32[LN:YQEL_BACSU]138
[AC:P54457]
[GN:YQEL]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 13.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION]
[SP:P54457]
SPX043543530962477412874.60E-55[LN:YQEM_BACSU]138
[AC:P54458]
[GN:YQEM]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 28.3 KD PROTEIN IN AROD-COMER INTERGENIC REGION]
[SP:P54458]
SPX04364363097188564NO-HIT6
SPX0437437309836610982229.30E-38[LN:B69875]97
[AC:B69875]
[PN:conserved hypothetical protein ylbM]
[GN:ylbM]
[OR:Bacillus subtilis]
SPX0438438309963189NO-HIT6
SPX043943931009162748861.00E-10[GI:1890605]77
[LN:RMEXPGNS]
[AC:Z79692]
[PN:ORF25]
[OR:Sinorhizobium meliloti]
SPX04404403101537161115472.30E-211[GI:6984124]81
[LN:AF228345]
[AC:AF228345]
[PN:unknown]
[OR:Listeria monocytogenes]
SPX044144131022096276141.40E-80[LN:B69878]139
[AC:B69878]
[PN:guanylate kinase homolog yloD]
[GN:yloD]
[CL:guanylate kinase:guanylate kinase homology]
[OR:Bacillus subtilis]
SPX04424423103105315911.00E-09[LN:C69878]87
[AC:C69878]
[PN:hypothetical protein yloH]
[GN:yloH]
[OR:Bacillus subtilis]
SPX0443443310479923979532.70E-237[LN:PRIA_BACSU]136
[AC:P94461:O34941]
[GN:PRIA]
[OR:Bacillus subtilis]
[DE:PRIMOSOMAL PROTEIN N′(REPLICATION FACTOR Y)]
[SP:P94461:O34941]
SPX044444431053129364341.70E-64[GI:1772500]105
[LN:BSPRIADFS]
[AC:Y10304]
[PN:Met-tRNAi formyl transferase]
[GN:fmt]
[OR:Bacillus subtilis]
SPX044544531061765282481.40E-39[GI:1772501]71
[LN:BSPRIADFS]
[AC:Y10304]
[GN:sun]
[OR:Bacillus subtilis]
SPX044644631071394171301.30E-09[GI:4210751]93
[LN:LLA132604]
[AC:AJ132604]
[PN:sunL protein]
[GN:sunL]
[OR:Lactococcus lactis]
SPX044744731082336996062.70E-80[GI:4210751]93
[LN:LLA132604]
[AC:AJ132604]
[PN:sunL protein]
[GN:sunL]
[OR:Lactococcus lactis]
SPX044844831092477413711.50E-85[GI:4210752]134
[LN:LLA132604]
[AC:AJ132604]
[PN:pppL protein]
[GN:pppL]
[FN:putative phosphoprotein phosphatase]
[OR:Lactococcus lactis]
SPX0449449311066019809851.70E-128[GI:4210753]91
[LN:LLA132604]
[AC:AJ132604]
[PN:hypothetical protein]
[OR:Lactococcus lactis]
SPX0450450311168204NO-HIT6
SPX0451451311274222NO-HIT6
SPX045245231131705101251.80E-09[LN:YJJP_ECOLI]143
[AC:P39402]
[GN:YJJP]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 30.5 KD PROTEIN IN DNAT-BGLJ INTERGENIC REGION (F277)]
[SP:P39402]
SPX04534533114112336944.60E-07[LN:G81321]121
[AC:G81321]
[PN:probable integral membrane protein Cj1165c [imported]]
[GN:Cj1165c]
[OR:Campylobacter jejuni]
SPX04544543115672012173.80E-24[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX045545531161303903627.00E-46[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX0456456311796288NO-HIT6
SPX0457457311839111737751.30E-101[GI:4096796]67
[LN:SCU40157]
[AC:U40157]
[OR:Staphylococcus carnosus]
SPX0458458311942512753548.70E-92[LN:MVAA_PSEMV]106
[AC:P13702]
[GN:MVAA]
[OR:Pseudomonas mevalonii]
[EC:1.1.1.88]
[DE:REDUCTASE)]
[SP:P13702]
SPX0459459312032296611081.00E-150[LN:SCRR_STRMU]137
[AC:Q54430]
[GN:SCRR]
[OR:Streptococcus mutans]
[DE:SUCROSE OPERON REPRESSOR (SCR OPERON REGULATORY PROTEIN)]
[SP:Q54430]
SPX04604603121485145516913.60E-229“[LN:S68598]189
[AC:S68598]
[PN:sucrose-6-phosphate hydrolase ScrB]
[GN:scrB]
[CL:sucrose-6-phosphate hydrolase]
[OR:Streptococcus sobrinus]
[SR:strain 6715, , strain 6715]
[SR:strain 6715, ]”
SPX0461461312277231NO-HIT6
SPX0462462312366198NO-HIT6
SPX0463463312462818847176.70E-255“[LN:S68599]177
[AC:S68599]
[PN:phosphotransferase system enzyme II,, sucrose-specific:sucrose-specific enzyme II:sucrose-specific enzyme II]
[GN:scrA]
[OR:Streptococcus sobrinus]”
SPX046446431252968887013.80E-158“[LN:SCRK_STRMU]109
[AC:Q07211]
[GN:SCRK]
[OR:Streptococcus mutans]
[EC:2.7.1.4]
[DE:FRUCTOKINASE,]
[SP:Q07211]”
SPX0465465312671213NO-HIT6
SPX046646631272006001032.90E-07[LN:YDJZ_ECOLI]136
[AC:P76221]
[GN:YDJZ]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 26.2 KD PROTEIN IN XTHA-GDHA INTERGENIC REGION]
[SP:P76221]
SPX04674673128752252001.30E-21[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX0468468312984252NO-HIT6
SPX04694693130762281873.50E-21[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX047047031312988944601.20E-78[GI:3688825]81
[LN:AF084104]
[AC:AF084104]
[PN:NatA]
[GN:natA]
[OR:Bacillus firmus]
SPX0471471313240012002004.70E-36[GI:1150487]89
[LN:LSLASAMPT]
[AC:Z54312]
[PN:unknown]
[GN:orf414]
[OR:Lactobacillus sakei]
SPX0472472313356168NO-HIT6
SPX04734733134283849NO-HIT6
SPX047447431352417234601.50E-58“[LN:G71842]238
[AC:G71842]
[PN:probable ABC transporter, ATP-binding protein]
[GN:jhp1141]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Helicobacter pylori]
[SR:strain J99, , strain J99]
[SR:strain J99, ]”
SPX0475475313670210954.40E-07[LN:E72756]92
[AC:E72756]
[PN:hypothetical protein APE0042]
[GN:APE0042]
[OR:Aeropyrum pernix]
SPX047647631371223662563.70E-30[GI:5822822]129
[LN:AB024564]
[AC:AB024564]
[PN:YHCF]
[GN:yhcF]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA]
SPX047747731381584744058.00E-51[LN:E72221]139
[AC:E72221]
[PN:conserved hypothetical protein]
[GN:TM1707]
[CL:conserved hypothetical protein HI0943]
[OR:Thermotoga maritima]
SPX047847831393901170NO-HIT6
SPX047947931402998973002.40E-58[LN:DNAI_BACSU]101
[AC:P06567]
[GN:DNAI]
[OR:Bacillus subtilis]
[DE:PRIMOSOMAL PROTEIN DNAI]
[SP:P06567]
SPX048048031412387142393.90E-35“[LN:CHRR_PSESP]110
[AC:P96977]
[GN:CHRR]
[OR:Pseudomonas sp]
[SR:,strain G-1]
[DE:CR(VI) REDUCTASE]
[SP:P96977]”
SPX04814813142437131119861.10E-270“[GI:6681650]174
[LN:AB016077]
[AC:AB016077]
[PN:phosphoglycerate dehydrogenase]
[GN:pgdA]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:MT8148) DNA, clone:pYT570]”
SPX04824823143115345NO-HIT6
SPX04834833144118354NO-HIT6
SPX0484484314564192NO-HIT6
SPX048548531462848521033.00E-11[GI:4102023]134
[LN:AF007761]
[AC:AF007761]
[PN:MutR]
[GN:mutR]
[FN:positive transcriptional regulator of mutA]
[OR:Streptococcus mutans]
SPX04864863147131393NO-HIT6
SPX04874873148264792NO-HIT6
SPX04884883149226678NO-HIT6
SPX048948931502116332823.20E-42[LN:YYBJ_BACSU]95
[AC:P37494]
[GN:YYBJ]
[OR:Bacillus subtilis]
[DE:INTERGENIC REGION]
[SP:P37494]
SPX0490490315196288NO-HIT6
SPX0491491315283825149890[LN:SECA_LISMO]118
[AC:P47847]
[GN:SECA]
[OR:Listeria monocytogenes]
[DE:PREPROTEIN TRANSLOCASE SECA SUBUNIT]
[SP:P47847]
SPX0492492315334410321567.30E-47[GI:7380801]136
[LN:NMA7Z2491]
[AC:AL162758:AL157959]
[PN:phospho-2-dehydr-3-deoxyheptonate aldolase]
[GN:aroG]
[OR:Neisseria meningitidis]
SPX049349331542156451783.50E-34[LN:AROF_ECOLI]157
[AC:P00888]
[GN:AROF]
[OR:Escherichia coli]
[EC:4.1.2.15]
[DE:SYNTHETASE) (3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE)]
[SP:P00888]
SPX04944943155111333NO-HIT6
SPX04954953156892671322.60E-14[GI:7380801]136
[LN:NMA7Z2491]
[AC:AL162758:AL157959]
[PN:phospho-2-dehydr-3-deoxyheptonate aldolase]
[GN:aroG]
[OR:Neisseria meningitidis]
SPX049649631571213631771.70E-30“[LN:H69772]137
[AC:H69772]
[PN:holo-[acyl-carrier-protein]
synthase,]
[GN:ydcB]
[CL:holo-ACP synthase]
[OR:Bacillus subtilis]
[EC:2.7.8.7]”
SPX04974973158368110418521.10E-252[GI:5759209]101
[LN:AF171873]
[AC:AF171873]
[PN:alanine racemase]
[GN:alr]
[OR:Streptococcus pneumoniae]
SPX04984983159672201633570“[LN:RECG_STRPN]137
[AC:Q54900]
[GN:RECG:MMSA]
[OR:Streptococcus pneumoniae]
[EC:3.6.1.-]
[DE:ATP-DEPENDENT DNA HELICASE RECG,]
[SP:Q54900]”
SPX04994993160892672632.70E-32[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX0500500316168204NO-HIT6
SPX050150131623279814471.40E-92[GI:2353697]117
[LN:AF001926]
[AC:AF001926]
[PN:xylan esterase 1]
[GN:axe1]
[OR:Thermoanaerobacterium sp. ′JW/SL YS485′]
SPX050250231632066183551.20E-44[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX050350331641685041721.10E-15[GI:4101572]122
[LN:AF004842]
[AC:AF004842]
[PN:major royal jelly protein MRJP5]
[GN:MRJP5]
[OR:Apis mellifera]
[SR:honeybee]
SPX05045043165762283713.40E-50[LN:T30286]89
[AC:T30286:S26297]
[PN:hypothetical protein 76]
[OR:Streptococcus pneumoniae]
SPX05055053166938281443780“[LN:NANA_STRPN]155
[AC:Q59959:Q54722]
[GN:NANA]
[OR:Streptococcus pneumoniae]
[EC:3.2.1.18]
[DE:SIALIDASE A PRECURSOR, (NEURAMINIDASE A)]
[SP:Q59959:Q54722]”
SPX0506506316772216NO-HIT6
SPX050750731681514537736.10E-103[GI:1163111]68
[LN:SPU43526]
[AC:U43526]
[OR:Streptococcus pneumoniae]
SPX05085083169446133823070[GI:1163112]68
[LN:SPU43526]
[AC:U43526]
[OR:Streptococcus pneumoniae]
SPX0509509317029588515422.00E-218[GI:1163113]68
[LN:SPU43526]
[AC:U43526]
[OR:Streptococcus pneumoniae]
SPX0510510317127883413753.80E-192[GI:1163114]68
[LN:SPU43526]
[AC:U43526]
[OR:Streptococcus pneumoniae]
SPX0511511317225476212501.40E-167“[LN:NANB_STRPN]141
[AC:Q54727]
[GN:NANB]
[OR:Streptococcus pneumoniae]
[EC:3.2.1.18]
[DE:SIALIDASE B PRECURSOR, (NEURAMINIDASE B)]
[SP:Q54727]”
SPX051251231731263783331.60E-40[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX051351331742116337627.90E-101[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX05145143175467140123630“[LN:NANB_STRPN]141
[AC:Q54727]
[GN:NANB]
[OR:Streptococcus pneumoniae]
[EC:3.2.1.18]
[DE:SIALIDASE B PRECURSOR, (NEURAMINIDASE B)]
[SP:Q54727]”
SPX05155153176368110418381.30E-249[LN:YJHC_STRPN]131
[AC:Q54728]
[OR:Streptococcus pneumoniae]
[DE:HYPOTHETICAL PROTEIN IN NANB 3′REGION (ORF-5) (FRAGMENT)]
[SP:Q54728]
SPX05165163177130390NO-HIT6
SPX051751731782336993311.90E-64“[LN:C70180]125
[AC:C70180]
[PN:conserved hypothetical protein BB0644]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX0518518317950615188392.60E-178“[LN:D70180]167
[AC:D70180]
[PN:phosphotransferase system enzyme II,, glucose-specific, factor II]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]
[EC:2.7.1.69]”
SPX0519519318044313291101.90E-09[GI:6137033]132
[LN:SCF11]
[AC:AL132662]
[PN:putative sugar transporter sugar binding]
[GN:SCF11.11]
[OR:Streptomyces coelicolor A3(2)]
SPX052052031812968882111.60E-50“[LN:E72357]140
[AC:E72357]
[PN:sugar ABC transporter, permease protein]
[GN:TM0596]
[CL:inner membrane protein malF]
[OR:Thermotoga maritima]”
SPX052152131822808404341.10E-65“[LN:F72379]143
[AC:F72379]
[PN:sugar ABC transporter, permease protein]
[GN:TM0430]
[CL:maltose transport protein malG]
[OR:Thermotoga maritima]”
SPX052252231831514531092.60E-13[LN:YJGK_ECOLI]144
[AC:P39335]
[GN:YJGK]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 17.3 KD PROTEIN IN PYRL-ARGI INTERGENIC REGION (O153B)]
[SP:P39335]
SPX05235233184118354NO-HIT6
SPX0524524318566198NO-HIT6
SPX05255253186215645NO-HIT6
SPX052652631872206608301.30E-109[GI:2385360]100
[LN:CTSIALIDA]
[AC:Y08695]
[PN:putative acylneuraminate lyase]
[OR:Clostridium tertium]
SPX05275273188100300680.00016[GI:42131]55
[LN:ECNPL]
[AC:X03345]
[OR:Escherichia coli]
SPX052852831892958854232.50E-53[LN:YNGA_CLOPE]129
[AC:P26832]
[OR:Clostridium perfringens]
[DE:HYPOTHETICAL PROTEIN IN NAGH 5′REGION (ORFA) (FRAGMENT)]
[SP:P26832]
SPX052952931902838491702.10E-25[LN:Y143_HAEIN]112
[AC:P44540]
[GN:HI0143]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI0143]
[SP:P44540]
SPX05305303191681204333650[GI:4009463]116
[LN:AF068901]
[AC:AF068901]
[PN:penicillin-binding protein 2b]
[GN:pbp2b]
[OR:Streptococcus pneumoniae]
SPX053153131921193575245.00E-69[GI:49383]143
[LN:SPPBP2BH]
[AC:Z21808]
[PN:internal region of the penicillin-binding]
[FN:penicillin-resistantance]
[OR:Streptococcus pneumoniae]
SPX053253231931715136254.80E-83[GI:4009464]90
[LN:AF068901]
[AC:AF068901]
[PN:RecM]
[GN:recM]
[OR:Streptococcus pneumoniae]
SPX05335333194348104417661.30E-239[GI:4009465]103
[LN:AF068901]
[AC:AF068901]
[PN:D-Ala-D-Ala ligase]
[GN:ddl]
[OR:Streptococcus pneumoniae]
SPX05345343195458137422780[GI:4009466]111
[LN:AF068901]
[AC:AF068901]
[PN:D-Ala-D-Ala adding enzyme]
[GN:murF]
[OR:Streptococcus pneumoniae]
SPX0535535319644913474033.50E-76[GI:5822769]109
[LN:AB024553]
[AC:AB024553]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA]
SPX053653631971925769541.80E-127[GI:4009467]90
[LN:AF068901]
[AC:AF068901]
[PN:MutT]
[GN:mutT]
[OR:Streptococcus pneumoniae]
SPX0537537319819959710031.80E-140[GI:4009468]83
[LN:AF068901]
[AC:AF068901]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX0538538319987261NO-HIT6
SPX05395393200458137422660[GI:4009469]112
[LN:AF068901]
[AC:AF068901]
[PN:cell division protein FtsA]
[GN:ftsA]
[OR:Streptococcus pneumoniae]
SPX05405403201419125720944.10E-280[GI:4009470]112
[LN:AF068901]
[AC:AF068901]
[PN:cell division protein FtsZ]
[GN:ftsZ]
[OR:Streptococcus pneumoniae]
SPX05415413202792371782.40E-19[LN:A71218]95
[AC:A71218]
[PN:hypothetical protein PH0004]
[GN:PH0004]
[OR:Pyrococcus horikoshii]
SPX0542542320322467211016.20E-148[GI:4009471]90
[LN:AF068901]
[AC:AF068901]
[PN:YlmE]
[GN:ylmE]
[OR:Streptococcus pneumoniae]
SPX054354332041805409201.10E-122[GI:4009472]90
[LN:AF068901]
[AC:AF068901]
[PN:YlmF]
[GN:ylmF]
[OR:Streptococcus pneumoniae]
SPX05445443205882644311.50E-58[GI:4009473]90
[LN:AF068901]
[AC:AF068901]
[PN:YlmG]
[GN:ylmG]
[OR:Streptococcus pneumoniae]
SPX0545545320626278613182.10E-179[GI:4009474]90
[LN:AF068901]
[AC:AF068901]
[PN:YlmH]
[GN:ylmH]
[OR:Streptococcus pneumoniae]
SPX0546546320726378912971.90E-171[GI:4009475]116
[LN:AF068901]
[AC:AF068901]
[PN:cell division protein DivIVA]
[GN:divIVA]
[OR:Streptococcus pneumoniae]
SPX05475473208931279348400[GI:4009476]112
[LN:AF068901]
[AC:AF068901]
[PN:isoleucine-tRNA synthetase]
[GN:ileS]
[OR:Streptococcus pneumoniae]
SPX0548548320962186820.00016“[LN:A56034]120
[AC:A56034]
[PN:insulin activator factor]
[CL:human insulin activator factor]
[OR:Homo sapiens]
[SR:, man]”
SPX05495493210872611922.20E-20“[LN:A56034]120
[AC:A56034]
[PN:insulin activator factor]
[CL:human insulin activator factor]
[OR:Homo sapiens]
[SR:, man]”
SPX0550550321163189NO-HIT6
SPX0551551321272216NO-HIT6
SPX0552552321323169312011.00E-160[GI:5578891]107
[LN:SPN131985]
[AC:AJ131985]
[PN:phosphoglyceromutase]
[GN:gpmA]
[OR:Streptococcus pneumoniae]
SPX0553553321480424122322.70E-95[GI:5912520]124
[LN:SCF12]
[AC:AL117669]
[PN:putative large secreted protein]
[GN:SCF12.20c]
[OR:Streptomyces coelicolor A3(2)]
SPX055455432152377116427.20E-84“[LN:B69477]179
[AC:B69477]
[PN:ABC transporter, ATP-binding protein homolog]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Archaeoglobus fulgidus]”
SPX0555555321692527751061.10E-16[LN:C69477]84
[AC:C69477]
[PN:hypothetical protein AF1820]
[OR:Archaeoglobus fulgidus]
SPX055655632171735198781.10E-117[GI:4193357]137
[LN:AF055088]
[AC:AF055088:AF055087]
[PN:putative hydrophobic transmembrane protein]
[GN:psaD]
[OR:Streptococcus pneumoniae]
SPX0557557321831093015792.30E-209[GI:3258602]150
[LN:SPU40786]
[AC:U40786]
[PN:surface antigen A variant precursor]
[GN:psaA]
[FN:putative fimbrial adhesin]
[OR:Streptococcus pneumoniae]
SPX0558558321928384911718.00E-165[LN:P29K_STRGC]127
[AC:P42361]
[OR:Streptococcus gordonii challis]
[DE:29 KD MEMBRANE PROTEIN IN PSAA 5′REGION (ORF1)]
[SP:P42361]
SPX0559559322025275612082.80E-164[GI:4193356]115
[LN:AF055088]
[AC:AF055088:AF055087]
[PN:ATP-binding cassette]
[GN:psaB]
[OR:Streptococcus pneumoniae]
SPX05605603221651195314770[GI:5139244]104
[LN:AF116532]
[AC:AF116532]
[PN:endopeptidase O]
[GN:pepO]
[OR:Streptococcus parasanguinis]
SPX056156132222106301812.90E-36[LN:YQGX_BACSU]138
[AC:P54501]
[GN:YQGX]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 23.2 KD PROTEIN IN SODA-COMGA INTERGENIC REGION]
[SP:P54501]
SPX05625623223672011312.00E-13[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX0563563322481243NO-HIT6
SPX05645643225741222316010[LN:RELA_STREQ]111
[AC:Q54089]
[GN:RELA:REL]
[OR:Streptococcus equisimilis]
[EC:2.7.6.5]
[DE:PROTEIN)]
[SP:Q54089]
SPX0565565322681243700.0001[LN:Q3ECS7]163
[AC:A30374:Q90796]
[PN:hypothetical 77K protein (spoT 3′region)]
[CL:Escherichia coli hypothetical 77K protein (spoT 3′region)]
[OR:Escherichia coli]
SPX056656632271484445852.40E-76[LN:S39974]123
[AC:S39974]
[PN:hypothetical protein]
[CL:conserved hypothetical protein HI0670]
[OR:Streptococcus equisimilis]
SPX0567567322876228NO-HIT6
SPX05685683229141423NO-HIT6
SPX05695693230236708NO-HIT6
SPX057057032311404204337.90E-56[GI:6694218]105
[LN:AF182402]
[AC:AF182402]
[PN:metalloregulator RmtA]
[GN:rmtA]
[OR:Streptococcus gordonii]
SPX05715713232802403074.00E-38[GI:6694218]105
[LN:AF182402]
[AC:AF182402]
[PN:metalloregulator RmtA]
[GN:rmtA]
[OR:Streptococcus gordonii]
SPX057257232332818431252.00E-13[LN:G75297]167
[AC:G75297]
[PN:conserved hypothetical protein]
[GN:DR2233]
[CL:probable phosphoesterase MJ0912:phosphoesterase core homology]
[OR:Deinococcus radiodurans]
SPX0573573323465195NO-HIT6
SPX057457432351053151427.90E-15[LN:D70063]87
[AC:D70063]
[PN:hypothetical protein ywnA]
[GN:ywnA]
[OR:Bacillus subtilis]
SPX05755753236732191292.40E-12[LN:D70063]87
[AC:D70063]
[PN:hypothetical protein ywnA]
[GN:ywnA]
[OR:Bacillus subtilis]
SPX05765763237101303NO-HIT6
SPX057757732383581074NO-HIT6
SPX0578578323922667811461.70E-157[GI:5830520]104
[LN:SPAJ6391]
[AC:AJ006391]
[PN:response regulator]
[GN:rr01]
[OR:Streptococcus pneumoniae]
SPX0579579324032597516283.20E-226[GI:5830521]102
[LN:SPAJ6391]
[AC:AJ006391]
[PN:histidine kinase]
[GN:hk01]
[OR:Streptococcus pneumoniae]
SPX05805803241661198311492.20E-274[LN:SYT1_BACSU]118
[AC:P18255:P06570]
[GN:THRS:THRSV]
[OR:Bacillus subtilis]
[EC:6.1.1.3]
[DE:(THRRS)]
[SP:P18255:P06570]
SPX05815813242130390NO-HIT6
SPX0582582324397291NO-HIT6
SPX0583583324470210NO-HIT6
SPX058458432452106303711.30E-60[LN:E70063]87
[AC:E70063]
[PN:hypothetical protein ywnB]
[GN:ywnB]
[OR:Bacillus subtilis]
SPX05855853246902703111.10E-38[LN:F69700]214
[AC:F69700:S11365:S70690]
[PN:ribosomal protein S15 (rpsO):ribosomal protein BS18]
[GN:rpsO]
[CL:Escherichia coli ribosomal protein S15:eubacterial ribosomal protein S15 homology]
[OR:Bacillus subtilis]
SPX0586586324775225NO-HIT6
SPX058758732481594772431.30E-38[GI:1916729]94
[LN:AF134905]
[AC:AF134905:U76550]
[PN:CadD]
[GN:cadD]
[OR:Staphylococcus aureus]
SPX058858832492507501651.10E-23[LN:E69826]117
[AC:E69826]
[PN:1-acylglycerol-3-phosphate O-acyltransfera homolog yhdO]
[GN:yhdO]
[OR:Bacillus subtilis]
SPX0589589325077923374141.80E-126“[LN:CTPE_MYCTU]160
[AC:O08365]
[GN:CTPE:RV0908:MTCY21C12.02]
[OR:Mycobacterium tuberculosis]
[EC:3.6.1.-]
[DE:PROBABLE CATION-TRANSPORTING ATPASE E,]
[SP:O08365]”
SPX0590590325177231NO-HIT6
SPX0591591325248814641229.60E-23[GI:1480429]88
[LN:BSU18943]
[AC:U18943:X99465]
[GN:MtlR]
[OR:Bacillus stearothermophilus]
SPX05925923253143429600.00018[GI:2317740]108
[LN:AF013987]
[AC:AF013987]
[PN:nitrogen regulatory IIA protein]
[GN:ptsN]
[OR:Vibrio cholerae]
SPX059359332541514532235.60E-24“[LN:HRSA_ECOLI]106
[AC:P54745]
[GN:HRSA]
[OR:Escherichia coli]
[EC:2.7.1.69]
[DE:HRSA PROTEIN,]
[SP:P54745]”
SPX059459432551043122361.30E-27“[LN:PTWB_ECOLI]110
[AC:P32673]
[GN:FRWB]
[OR:Escherichia coli]
[EC:2.7.1.69]
[DE:II, B COMPONENT),]
[SP:P32673]”
SPX0595595325636911073988.00E-60“[LN:PTFB_XANCP]141
[AC:P23355]
[GN:FRUA]
[OR:Xanthomonas campestris]
[SR:,pvcampestris]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EII-FRU)]
[SP:P23355]”
|
SPX059659632572326965606.50E-74“[LN:ALSE_ECOLI]127
[AC:P32719]
[GN:ALSE]
[OR:Escherichia coli]
[EC:5.1.3.-]
[DE:D-ALLULOSE-6-PHOSPHATE 3-EPIMERASE,]
[SP:P32719]”
SPX05975973258657197113712.00E-292“[LN:TKT_STRPN]127
[AC:P22976]
[GN:RECP]
[OR:Streptococcus pneumoniae]
[EC:2.2.1.1]
[DE:PROBABLE TRANSKETOLASE, (TK)]
[SP:P22976]”
SPX059859832591915734222.30E-53[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX059959932601915734222.30E-53[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX060060032612788345871.60E-140[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX06016013262177531NO-HIT6
SPX060260232631394171381.40E-10[LN:T35180]160
[AC:T35180]
[PN:hypothetical protein SC5A7.31]
[GN:SC5A7.31]
[CL:Streptomyces coelicolor hypothetical protein SC5A7.31]
[OR:Streptomyces coelicolor]
SPX060360332642266786121.10E-79[GI:1813343]114
[LN:D78182]
[AC:D78182]
[GN:ORF3]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:Xc) DNA]
SPX060460432652667983445.40E-120[GI:1813344]114
[LN:D78182]
[AC:D78182]
[GN:ORF4]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:Xc) DNA]
SPX0605605326636811043354.50E-71[LN:YURR_BACSU]143
[AC:O32159]
[GN:YURR]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 39.4 KD OXIDOREDUCTASE IN HOM-MRGA INTERGENIC REGION]
[SP:O32159]
SPX0606606326764192NO-HIT6
SPX06076073268340102011677.10E-156[LN:GALE_BACSU]113
[AC:P55180]
[GN:GALE]
[OR:Bacillus subtilis]
[EC:5.1.3.2]
[DE:GALACTOSE 4-EPIMERASE)]
[SP:P55180]
SPX060860832693189544417.80E-87[LN:CSBB_BACSU]90
[AC:Q45539]
[GN:CSBB]
[OR:Bacillus subtilis]
[DE:CSBB PROTEIN]
[SP:Q45539]
SPX06096093270222666NO-HIT6
SPX0610610327169207550.00029“[LN:FER_MOOTH]117
[AC:P00203]
[OR:Moorella thermoacetica]
[SR:,Clostridium thermoaceticum]
[DE:FERREDOXIN]
[SP:P00203]”
SPX06116113272159477NO-HIT6
SPX061261232732246724136.00E-74[LN:KCY_BACSU]107
[AC:P38493]
[GN:CMK:JOFC]
[OR:Bacillus subtilis]
[EC:2.7.4.14]
[DE:(CMP KINASE)]
[SP:P38493]
SPX061361332741133394325.60E-55[LN:PHNA_ECOLI]89
[AC:P16680]
[GN:PHNA]
[OR:Escherichia coli]
[DE:PHNA PROTEIN]
[SP:P16680]
SPX06146143275210630NO-HIT6
SPX06156153276762281923.60E-23[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX061661632773841152686.80E-05[LN:C81266]108
[AC:C81266]
[PN:probable efflux protein Cj1687 [imported]]
[GN:Cj1687]
[OR:Campylobacter jejuni]
SPX061761732782507503094.30E-69[LN:TRUA_BACSU]141
[AC:P70973]
[GN:TRUA]
[OR:Bacillus subtilis]
[EC:4.2.1.70]
[DE:I) (PSEUDOURIDINE SYNTHASE I) (URACIL HYDROLYASE)]
[SP:P70973]
SPX061861832792587741553.70E-39[LN:THID_BACSU]113
[AC:P39610]
[GN:THID:IPA-52R]
[OR:Bacillus subtilis]
[EC:2.7.4.7]
[DE:(HMP-P KINASE)]
[SP:P39610]
SPX06196193280154462695.80E-12[LN:G75153]93
[AC:G75153]
[PN:hypothetical protein PAB2090]
[GN:PAB2090]
[OR:Pyrococcus abyssi]
SPX062062032811915734222.30E-53[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX06216213282912732882.30E-35[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX062262232831985945839.30E-95[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX06236233284159477NO-HIT6
SPX06246243285361108310161.20E-136[GI:2323341]103
[LN:AF014460]
[AC:AF014460]
[PN:PepQ]
[FN:hydrolysis of Leu-Pro]
[OR:Streptococcus mutans]
SPX062562532862617831475.10E-36[LN:T31439]91
[AC:T31439]
[PN:probable cobyric acid synthase CobQ]
[OR:Heliobacillus mobilis]
SPX0626626328744813441371.30E-46[LN:T31440]110
[AC:T31440]
[PN:UDP-N-acetylmuramyl tripeptide synthetase homolog murC]
[OR:Heliobacillus mobilis]
SPX0627627328843913177974.80E-136[LN:YKGC_ECOLI]94
[AC:P77212]
[GN:YKGC]
[OR:Escherichia coli]
[DE:INTERGENIC REGION]
[SP:P77212]
SPX062862832892918737113.70E-137[GI:7107009]96
[LN:AF168363]
[AC:AF168363]
[PN:oxalate:formate antiporter]
[OR:Lactococcus lactis]
SPX06296293290822461935.00E-21[GI:7107009]96
[LN:AF168363]
[AC:AF168363]
[PN:oxalate:formate antiporter]
[OR:Lactococcus lactis]
SPX06306303291525157513291.80E-184[GI:4409804]116
[LN:AF091502]
[AC:AF091502]
[PN:autoaggregation-mediating protein]
[GN:aggH]
[OR:Lactobacillus reuteri]
SPX063163132922637895473.10E-74[LN:CODY_BACSU]126
[AC:P39779]
[GN:CODY]
[OR:Bacillus subtilis]
[DE:CODY PROTEIN (VEGETATIVE PROTEIN 286B) (VEG286B)]
[SP:P39779]
SPX06326323293692071741.30E-18[LN:C70008]136
[AC:C70008]
[PN:pyrazinamidase/nicotinamidase homolog yueJ]
[GN:yueJ]
[CL:hypothetical protein b1011]
[OR:Bacillus subtilis]
SPX063363332941524562531.50E-30[LN:C70008]136
[AC:C70008]
[PN:pyrazinamidase/nicotinamidase homolog yueJ]
[GN:yueJ]
[CL:hypothetical protein b1011]
[OR:Bacillus subtilis]
SPX06346343295782343281.70E-40[GI:600072]96
[LN:SEDEXB]
[AC:X72832]
[PN:ABC transporter]
[GN:abc]
[OR:Streptococcus equisimilis]
SPX06356353296521561132.50E-10[LN:E72756]92
[AC:E72756]
[PN:hypothetical protein APE0042]
[GN:APE0042]
[OR:Aeropyrum pernix]
SPX063663632972858557311.70E-136[LN:MSMK_STRMU]138
[AC:Q00752]
[GN:MSMK]
[OR:Streptococcus mutans]
[DE:MULTIPLE SUGAR-BINDING TRANSPORT ATP-BINDING PROTEIN MSMK]
[SP:Q00752]
SPX063763732982537594853.90E-95[LN:Y095_HAEIN]126
[AC:Q57060:O05007]
[GN:HI0095]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI0095]
[SP:Q57060:O05007]
SPX063863832991775316032.90E-79“[LN:B69587]194
[AC:B69587]
[PN:adenine phosphoribosyltransferase,:AMP pyrophosphorylase:transphosphoribosidase]
[GN:apt]
[CL:adenine phosphoribosyltransferase]
[OR:Bacillus subtilis]
[EC:2.4.2.7]”
SPX063963933003159455676.90E-116[LN:C72324]134
[AC:C72324]
[PN:homoserine O-succinyltransferase]
[GN:TM0881]
[CL:homoserine succinyltransferase]
[OR:Thermotoga maritima]
SPX064064033012266783575.50E-90[GI:1813342]114
[LN:D78182]
[AC:D78182]
[GN:ORF2]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:Xc) DNA]
SPX06416413302125375NO-HIT6
SPX064264233032537598641.30E-113“[LN:TPIS_LACDE]159
[AC:O32757]
[GN:TPIA:TPI]
[OR:Lactobacillus delbrueckii]
[SR:,subspbulgaricus]
[EC:5.3.1.1]
[DE:TRIOSEPHOSPHATE ISOMERASE, (TIM)]
[SP:O32757]”
SPX06436433304502150627280“[GI:4218526]153
[LN:SPAJ9639]
[AC:AJ009639]
[PN:1,4-beta-N-acetylmuramidase]
[GN:lytC]
[FN:lysis of cell wall peptidoglycan]
[OR:Streptococcus pneumoniae]”
SPX064464433051735198002.60E-105[GI:3513547]83
[LN:AF055720]
[AC:AF055720]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX06456453306213639NO-HIT6
SPX064664633071695078822.00E-118[GI:2196662]135
[LN:HSZ84379]
[AC:Z84379]
[PN:dihydrofolate reductase]
[GN:dfr]
[FN:trimethoprim resistance]
[OR:Streptococcus pneumoniae]
SPX0647647330869207NO-HIT6
SPX06486483309411123312514.80E-206[GI:7546983]93
[LN:AF236863]
[AC:AF236863]
[PN:protease ClpX]
[GN:clpX]
[OR:Lactococcus lactis]
SPX064964933101965888079.70E-107[GI:7546984]102
[LN:AF236863]
[AC:AF236863]
[PN:hypothetical GTP-binding protein]
[OR:Lactococcus lactis]
SPX065065033111273813922.30E-49“[LN:ALDR_LACLA]143
[AC:O34133]
[GN:ALDR]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:PUTATIVE REGULATOR ALDR]
[SP:O34133]”
SPX065165133122978913372.00E-91[GI:7328270]91
[LN:SAY14324]
[AC:Y14324]
[PN:hypothetical protein]
[OR:Staphylococcus aureus]
SPX065265233133269782681.30E-62[LN:YVCK_BACSU]136
[AC:O06974]
[GN:YVCK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 34.7 KD PROTEIN IN CRH-TRXB INTERGENIC REGION]
[SP:O06974]
SPX065365333143049124245.50E-81[GI:7328272]65
[LN:SAY14324]
[AC:Y14324]
[OR:Staphylococcus aureus]
SPX065465433153239694225.00E-99[LN:B70015]154
[AC:B70015]
[PN:thioredoxin reductase homolog yumC]
[GN:yumC]
[CL:thioredoxin reductase:thioredoxin reductase homology]
[OR:Bacillus subtilis]
SPX065565533162728164198.50E-81[LN:H69744]128
[AC:H69744]
[PN:conserved hypothetical protein ybbP]
[GN:ybbP]
[CL:hypothetical protein ybbP]
[OR:Bacillus subtilis]
SPX065665633172607801042.70E-10[LN:A69745]87
[AC:A69745]
[PN:hypothetical protein ybbR]
[GN:ybbR]
[OR:Bacillus subtilis]
SPX0657657331864192NO-HIT6
SPX0658658331945113536552.00E-180[GI:3892895]107
[LN:SAARGFEMD]
[AC:Y15477]
[PN:phosphoglucosamine-mutase]
[GN:glmM]
[OR:Staphylococcus aureus]
SPX06596593320121363NO-HIT6
SPX066066033212838492396.50E-25[LN:DEGV_BACSU]90
[AC:P32436]
[GN:DEGV]
[OR:Bacillus subtilis]
[DE:DEGV PROTEIN]
[SP:P32436]
SPX066166133222567686146.50E-89“[LN:DAPB_BACSU]124
[AC:P42976]
[GN:DAPB]
[OR:Bacillus subtilis]
[EC:1.3.1.26]
[DE:DIHYDRODIPICOLINATE REDUCTASE,]
[SP:P42976]”
SPX0662662332340012006018.40E-92“[LN:PAPS_BACSU]119
[AC:P42977]
[GN:PAPS]
[OR:Bacillus subtilis]
[EC:2.7.7.19]
[DE:POLY(A) POLYMERASE, (PAP)]
[SP:P42977]”
SPX0663663332462418726691.80E-162[LN:A69814]188
[AC:A69814]
[PN:ABC transporter (ATP-binding protein) homolog yfmR]
[GN:yfmR]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX06646643325144432NO-HIT6
SPX0665665332639411826291.90E-82[LN:YEAB_BACSU]158
[AC:P46348:O05001]
[GN:YEAB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 31.8 KD PROTEIN IN GABP-GUAA INTERGENIC REGION (ORFX)]
[SP:P46348:O05001]
SPX0666666332789926976011.20E-189“[LN:S77052]218
[AC:S77052]
[PN:cation-transporting ATPase, pacL-1:protein sll0672:protein sll0672]
[GN:pacL-1]
[CL:Na+/K+-transporting ATPase alpha chain:ATPase nucleotide-binding domain homology]
[OR:Synechocystis sp.]”
SPX0667667332897291NO-HIT6
SPX0668668332983249730.00016[LN:H72624]92
[AC:H72624]
[PN:hypothetical protein APE1456]
[GN:APE1456]
[OR:Aeropyrum pernix]
SPX066966933302647927132.30E-105[LN:YGHU_ECOLI]135
[AC:Q46845]
[GN:YGHU]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 34.2 KD PROTEIN IN GSP-HYBG INTERGENIC REGION]
[SP:Q46845]
SPX067067033311524563683.30E-46“[LN:DEF_CLOBE]136
[AC:O08450]
[GN:DEF:FMS]
[OR:Clostridium beijerinckii]
[SR:,Clostridium MP]
[EC:3.5.1.31]
[DE:DEFORMYLASE)]
[SP:O08450]”
SPX067167133325321596NO-HIT6
SPX0672672333360180NO-HIT6
SPX067367333342437294731.20E-60[GI:4580623]77
[LN:AF118389]
[AC:AF118389]
[PN:unknown]
[OR:Streptococcus suis]
SPX067467433352106301112.10E-12[GI:6562870]116
[LN:SCM1]
[AC:AL133422]
[PN:putative secreted protein.]
[GN:SCM1.21]
[OR:Streptomyces coelicolor A3(2)]
SPX06756753336163489680.00021[LN:YPMB_BACSU]137
[AC:P54396]
[GN:YPMB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 17.9 KD PROTEIN IN DING-ASPB INTERGENIC REGION]
[SP:P54396]
SPX06766763337396118814002.80E-187[GI:6465901]106
[LN:AF035157]
[AC:AF035157]
[PN:aspartate aminotransferase]
[GN:aspC]
[OR:Lactococcus lactis]
SPX067767733381243721781.90E-27[LN:T03486]87
[AC:T03486]
[PN:conserved hypothetical protein]
[OR:Rhodobacter capsulatus]
SPX0678678333944813447031.60E-180[LN:SYN_BACSU]98
[AC:P39772]
[GN:ASNS]
[OR:Bacillus subtilis]
[EC:6.1.1.22]
[DE:(ASNRS)]
[SP:P39772]
SPX06796793340129387NO-HIT6
SPX06806803341972912367.30E-39[LN:RS6_BACSU]107
[AC:P21468]
[GN:RPSF]
[OR:Bacillus subtilis]
[DE:30S RIBOSOMAL PROTEIN S6 (BS9)]
[SP:P21468]
SPX068168133421574714815.20E-71[GI:6716352]136
[LN:AF145054]
[AC:AF145054:AF001793:AF118440:U89246]
[PN:ORF9]
[GN:orf9]
[OR:Streptococcus thermophilus bacteriophage 7201]
SPX06826823343872611341.30E-13[LN:RS18_BACST]120
[AC:P10806]
[GN:RPSR]
[OR:Bacillus stearothermophilus]
[DE:30S RIBOSOMAL PROTEIN S18 (BS21)]
[SP:P10806]
SPX06836833344112336NO-HIT6
SPX0684684334546714012707.50E-47[GI:4678225]137
[LN:AC007135]
[AC:AC007135:AE002093]
[PN:cyclophilin-like protein]
[GN:At2g36130]
[OR:Arabidopsis thaliana]
[SR:thale cress]
SPX06856853346842521726.10E-19[LN:YABR_BACSU]140
[AC:P37560]
[GN:YABR]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 14.2 KD PROTEIN IN DIVIC-SPOIIE INTERGENIC REGION]
[SP:P37560]
SPX0686686334787261961.40E-15[LN:YABB_BACSU]137
[AC:P37543]
[GN:YABB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]
[SP:P37543]
SPX06876873348672011093.00E-09[LN:YABB_BACSU]137
[AC:P37543]
[GN:YABB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]
[SP:P37543]
SPX068868833491293872671.40E-39[LN:YABB_BACSU]137
[AC:P37543]
[GN:YABB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 28.3 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]
[SP:P37543]
SPX06896893350932792241.50E-26[LN:A69742]127
[AC:A69742]
[PN:conserved hypothetical protein yazA]
[GN:yazA]
[CL:hypothetical protein 312]
[OR:Bacillus subtilis]
SPX06906903351601801435.60E-14[GI:1743856]115
[LN:SGU57759]
[AC:U57759]
[PN:intrageneric coaggregation-relevant adhesin]
[OR:Streptococcus gordonii]
SPX069169133522226669552.60E-126[GI:1743856]115
[LN:SGU57759]
[AC:U57759]
[PN:intrageneric coaggregation-relevant adhesin]
[OR:Streptococcus gordonii]
SPX06926923353171513NO-HIT6
SPX069369333541053151401.80E-21[GI:2952534]79
[LN:AF051356]
[AC:AF051356]
[PN:unknown]
[OR:Streptococcus mutans]
SPX0694694335595285NO-HIT6
SPX0695695335665195740.00038[GI:2772940]116
[LN:AF034574]
[AC:AF034574]
[PN:putative cruciform DNA binding protein]
[GN:Gv1]
[OR:Glomus versiforme]
SPX0696696335750415121721.50E-35[LN:MURE_BACSU]122
[AC:Q03523]
[GN:MURE]
[OR:Bacillus subtilis]
[EC:6.3.2.13]
[DE:DIAMINOPIMELATE-ADDING ENZYME)]
[SP:Q03523]
SPX069769733581925761729.40E-16[LN:MURE_BACSU]122
[AC:Q03523]
[GN:MURE]
[OR:Bacillus subtilis]
[EC:6.3.2.13]
[DE:DIAMINOPIMELATE-ADDING ENZYME)]
[SP:Q03523]
SPX0698698335954116231872.90E-75[LN:G69992]95
[AC:G69992]
[PN:spore cortex protein homolog ytgP]
[GN:ytgP]
[OR:Bacillus subtilis]
SPX06996993360653195933350[LN:ALIB_STRPN]128
[AC:Q51933]
[GN:ALIB]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE-BINDING PROTEIN ALIB PRECURSOR]
[SP:Q51933]
SPX070070033611855552822.00E-38[GI:1125685]104
[LN:SADNAS55]
[AC:X87104]
[GN:mdr]
[FN:multiple grug resistance]
[OR:Staphylococcus aureus]
SPX070170133621805401799.60E-18[LN:S58356]166
[AC:S66651:S58356]
[PN:pepT protein]
[GN:pepT]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Staphylococcus epidermidis]
SPX070270233631825464444.80E-55[GI:1262136]116
[LN:SAPBP4GEN]
[AC:X91786]
[PN:ATP-binding cassette transporter A]
[GN:abcA]
[OR:Staphylococcus aureus]
SPX0703703336436510956812.80E-123[LN:A69847]143
[AC:A69847]
[PN:cystathionine gamma-synthase homolog yjcI]
[GN:yjcI]
[CL:O-succinylhomoserine (thiol)-lyase]
[OR:Bacillus subtilis]
SPX0704704336538911675821.60E-99“[LN:PATB_BACSU]121
[AC:Q08432]
[GN:PATB]
[OR:Bacillus subtilis]
[EC:2.6.1.-]
[DE:PUTATIVE AMINOTRANSFERASE B,]
[SP:Q08432]”
SPX07057053366103330995521.00E-129[GI:1769947]68
[LN:BCX98455]
[AC:X98455]
[GN:SNF]
[OR:Bacillus cereus]
SPX07067063367206618NO-HIT6
SPX0707707336844513354912.00E-154[LN:MURC_BACSU]127
[AC:P40778]
[GN:MURC]
[OR:Bacillus subtilis]
[EC:6.3.2.8]
[DE:ACETYLMURANOYL-L-ALANINE SYNTHETASE)]
[SP:P40778]
SPX07087083369155465NO-HIT6
SPX07097093370119357567.70E-05“[LN:A64491]192
[AC:A64491]
[PN:N-terminal acetyltransferase complex, subunit ARD1 homolog]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]
[OR:Methanococcus jannaschii]”
SPX0710710337171213NO-HIT6
SPX0711711337250215061852.10E-43[LN:E69979]110
[AC:E69979]
[PN:folate metabolism homolog yrrL]
[GN:yrrL]
[CL:yceG protein]
[OR:Bacillus subtilis]
SPX071271233731614832713.60E-55[LN:GREA_BACSU]121
[AC:P80240]
[GN:GREA]
[OR:Bacillus subtilis]
[DE:GREA) (GENERAL STRESS PROTEIN 20M) (GSP20M)]
[SP:P80240]
SPX07137133374611831212.50E-12[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX071471433751634891521.50E-24[LN:S31638]77
[AC:S31638]
[PN:hypothetical protein]
[OR:Lactobacillus curvatus]
SPX0715715337666198NO-HIT6
SPX0716716337770210890.0001[GI:4966270]81
[LN:CELK09H11]
[AC:U97002]
[GN:K09H11.1]
[OR:Caenorhabditis elegans]
SPX071771733781484444197.50E-56[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX071871833791644924841.40E-63[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX07197193380672013313.00E-44“[LN:S49404]185
[AC:S49404:S38206]
[PN:H+-transporting ATP synthase, chain c]
[GN:atpC]
[CL:H+-transporting ATP synthase lipid-binding protein]
[OR:Streptococcus pneumoniae]
[EC:3.6.1.34]”
SPX0720720338123971712055.00E-168“[LN:ATP6_STRPN]139
[AC:Q59954]
[GN:ATPB:ATPA]
[OR:Streptococcus pneumoniae]
[EC:3.6.1.34]
[DE:ATP SYNTHASE A CHAIN, (PROTEIN 6)]
[SP:Q59954]”
SPX072172133821654957692.90E-100“[LN:ATPF_STRPN]153
[AC:Q59952:Q59955]
[GN:ATPF:ATPB]
[OR:Streptococcus pneumoniae]
[EC:3.6.1.34]
[DE:ATP SYNTHASE B CHAIN, (SUBUNIT I)]
[SP:Q59952:Q59955]”
SPX072272233831795375098.40E-66[GI:4100654]126
[LN:AF001955]
[AC:AF001955]
[PN:proton-translocating ATPase delta subunit]
[GN:uncH]
[OR:Streptococcus sanguinis]
SPX07237233384502150623470[GI:4100655]126
[LN:AF001955]
[AC:AF001955]
[PN:proton-translocating ATPase alpha subunit]
[GN:uncA]
[OR:Streptococcus sanguinis]
SPX0724724338529387910111.70E-169[GI:4100656]116
[LN:AF001955]
[AC:AF001955]
[PN:proton-translocating ATPase gamma subunit]
[OR:Streptococcus sanguinis]
SPX07257253386469140722870[GI:4100657]125
[LN:AF001955]
[AC:AF001955]
[PN:proton-translocating ATPase beta subunit]
[GN:uncD]
[OR:Streptococcus sanguinis]
SPX072672633871404205811.40E-76[GI:4100658]128
[LN:AF001955]
[AC:AF001955]
[PN:proton-translocating ATPase epsilon subunit]
[GN:uncC]
[OR:Streptococcus sanguinis]
SPX072772733882517531752.70E-42[GI:6746427]90
[LN:AF179847]
[AC:AF179847]
[PN:putative transposase]
[OR:Lactococcus lactis]
SPX0728728338965195NO-HIT6
SPX072972933901825461071.20E-15[GI:3849798]118
[LN:U91581]
[AC:U91581:U04057]
[PN:putative transposase]
[GN:tpase]
[OR:Lactococcus lactis subsp. lactis]
SPX0730730339133810144441.50E-117[GI:3242228]73
[LN:LLCADHE]
[AC:AJ001007]
[GN:orfB]
[OR:Lactococcus lactis]
SPX0731731339278234NO-HIT6
SPX07327323393389116711411.60E-158[GI:4098497]95
[LN:SMU78604]
[AC:U78604]
[PN:putative membrane protein]
[OR:Streptococcus mutans]
SPX0733733339441012304576.20E-71“[GI:473901]128
[LN:LACALS]
[AC:L16975]
[OR:Lactococcus lactis]
[SR:Lactococcus lactis (strain DSM 20384, sub_species lactis) DNA]”
SPX073473433952146423511.70E-45“[LN:A72357]146
[AC:A72357]
[PN:amino acid ABC transporter, permease protein]
[GN:TM0592]
[CL:histidine permease protein M]
[OR:Thermotoga maritima]”
SPX073573533962106303672.90E-65[GI:1649037]116
[LN:STU73111]
[AC:U73111]
[PN:glutamine transport ATP-binding protein GLNQ]
[OR:Salmonella typhimurium]
SPX0736736339727983714114.70E-188[GI:5929889]90
[LN:AF165218]
[AC:AF165218]
[PN:AatB]
[GN:aatB]
[OR:Streptococcus pneumoniae]
SPX073773733981163485781.80E-76[GI:5929888]88
[LN:AF165218]
[AC:AF165218]
[PN:Bta]
[GN:bta]
[OR:Streptococcus pneumoniae]
SPX07387383399573171929030[GI:5929887]88
[LN:AF165218]
[AC:AF165218]
[PN:Pgm]
[GN:pgm]
[OR:Streptococcus pneumoniae]
SPX073973934001093271298.30E-12[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX074074034011003002455.10E-30[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX0741741340295285NO-HIT6
SPX0742742340385255NO-HIT6
SPX0743743340471213NO-HIT6
SPX074474434053711113NO-HIT6
SPX07457453406174522721.10E-05“[LN:I38170]87
[AC:I38170]
[PN:gene hr44 protein]
[GN:hr44]
[OR:Homo sapiens]
[SR:, man]”
SPX074674634072908703352.40E-72[LN:B72254]135
[AC:B72254]
[PN:glycerol uptake facilitator protein]
[GN:TM1429]
[CL:glycerol facilitator protein]
[OR:Thermotoga maritima]
SPX07477473408399119720226.40E-273[LN:EFTU_STROR]108
[AC:P33170]
[GN:TUF]
[OR:Streptococcus oralis]
[DE:ELONGATION FACTOR TU (EF-TU)]
[SP:P33170]
SPX074874834091283841041.80E-06[LN:H71023]95
[AC:H71023]
[PN:hypothetical protein PH1485]
[GN:PH1485]
[OR:Pyrococcus horikoshii]
SPX07497493410138414996.40E-06[LN:S31840]82
[AC:S31840]
[PN:probable transposase]
[OR:Bacillus stearothermophilus]
SPX0750750341162186NO-HIT6
SPX075175134122186541633.90E-21[GI:722339]100
[LN:AXU22323]
[AC:U22323]
[PN:unknown]
[OR:Acetobacter xylinus]
[SR:Acetobacter xylinum]
SPX0752752341336110832722.20E-72[LN:C69813]153
[AC:C69813]
[PN:RNA helicase homolog yfmL]
[GN:yfmL]
[CL:unassigned DEAD/H box helicases:DEAD/H box helicase homology]
[OR:Bacillus subtilis]
SPX0753753341435410621973.10E-44[LN:YGJR_ECOLI]164
[AC:P42599:P42600:P76661]
[GN:YGJR]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 36.2 KD PROTEIN IN EBGC-UXAA INTERGENIC REGION]
[SP:P42599:P42600:P76661]
SPX0754754341562186770.00028“[LN:S67482]152
[AC:S67482:S52150]
[PN:serine O-acetyltransferase,, cytosolic:serine acetyltransferase:serine acetyltransferase]
[OR:Arabidopsis thaliana]”
SPX07557553416126378NO-HIT6
SPX0756756341748114434855.60E-59“[LN:G69849]118
[AC:G69849]
[PN:endo-1,4-beta-xylanase homolog yjeA]
[GN:yjeA]
[CL:nodB homology]
[OR:Bacillus subtilis]”
SPX075775734182567683575.70E-83[LN:C70040]129
[AC:C70040]
[PN:plant-metabolite dehydrogenase homolog yvgN]
[GN:yvgN]
[CL:aldehyde reductase]
[OR:Bacillus subtilis]
SPX0758758341977231NO-HIT6
SPX07597593420254762NO-HIT6
SPX0760760342130691811873.50E-159[LN:SYGA_BACSU]112
[AC:P54380]
[GN:GLYQ]
[OR:Bacillus subtilis]
[EC:6.1.1.14]
[DE:ALPHA CHAIN) (GLYRS)]
[SP:P54380]
SPX07617613422679203713346.50E-179[LN:SYGB_BACSU]111
[AC:P54381]
[GN:GLYS]
[OR:Bacillus subtilis]
[EC:6.1.1.14]
[DE:BETA CHAIN) (GLYRS)]
[SP:P54381]
SPX07627623423862582181.20E-24[LN:E69894]87
[AC:E69894]
[PN:hypothetical protein ynzC]
[GN:ynzC]
[OR:Bacillus subtilis]
SPX076376334244151245975.10E-08[LN:YIEF_ECOLI]136
[AC:P31465]
[GN:YIEF]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 20.4 KD PROTEIN IN TNAB-BGLB INTERGENIC REGION]
[SP:P31465]
SPX0764764342579237NO-HIT6
SPX076576534262026061102.80E-13[LN:YIEF_ECOLI]136
[AC:P31465]
[GN:YIEF]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 20.4 KD PROTEIN IN TNAB-BGLB INTERGENIC REGION]
[SP:P31465]
SPX076676634273089241723.10E-41[LN:APBE_TREPA]134
[AC:O83774]
[GN:APBE:TP0796]
[OR:Treponema pallidum]
[DE:THIAMINE BIOSYNTHESIS LIPOPROTEIN APBE PRECURSOR]
[SP:O83774]
SPX0767767342891273NO-HIT6
SPX07687683429460138023420[GI:4416519]88
[LN:AF014458]
[AC:AF014458]
[PN:NADH oxidase]
[OR:Streptococcus pneumoniae]
SPX0769769343029889414113.40E-191[LN:YG47_HAEIN]112
[AC:P45293]
[GN:HI1647]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI1647]
[SP:P45293]
SPX07707703431782341253.00E-12[LN:F71007]150
[AC:F71007]
[PN:hypothetical protein PH1356]
[GN:PH1356]
[CL:Pyrococcus horikoshii hypothetical protein PH1356]
[OR:Pyrococcus horikoshii]
SPX07717713432631891571.20E-15[LN:F72782]92
[AC:F72782]
[PN:hypothetical protein APE0247]
[GN:APE0247]
[OR:Aeropyrum pernix]
SPX07727723433521561594.30E-16[LN:F72782]92
[AC:F72782]
[PN:hypothetical protein APE0247]
[GN:APE0247]
[OR:Aeropyrum pernix]
SPX077377334341945827202.40E-95[LN:YG48_HAEIN]112
[AC:P45294]
[GN:HI1648]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI1648]
[SP:P45294]
SPX077477434352166481835.00E-34[LN:YA37_TREPA]108
[AC:O84000]
[GN:TP1037]
[OR:Treponema pallidum]
[DE:HYPOTHETICAL PROTEIN TP1037]
[SP:O84000]
SPX07757753436151453NO-HIT6
SPX07767763437165495942.80E-12[LN:G81269]111
[AC:G81269]
[PN:probable acetyltransferase Cj1715 [imported]]
[GN:Cj1715]
[OR:Campylobacter jejuni]
SPX077777734381775311671.80E-29[GI:3694956]119
[LN:AF091508]
[AC:AF091508]
[PN:O-6-methylguanine DNA methyltransferase]
[GN:ogt]
[OR:Salmonella muenster]
SPX077877834391193572722.10E-32[LN:B70021]124
[AC:B70021]
[PN:arsenate reductase homolog yusI]
[GN:yusI]
[CL:hypothetical protein yjbD]
[OR:Bacillus subtilis]
SPX07797793440126378NO-HIT6
SPX078078034412678012842.10E-54[LN:YXEN_BACSU]100
[AC:P54953]
[GN:YXEN:LP9F]
[OR:Bacillus subtilis]
[DE:INTERGENIC REGION]
[SP:P54953]
SPX078178134422487444685.80E-82[GI:666983]102
[LN:BSPAAT]
[AC:X77636]
[PN:putative ATP binding subunit]
[GN:ORF3]
[OR:Bacillus subtilis]
SPX0782782344379237NO-HIT6
SPX0783783344474222NO-HIT6
SPX078478434452667985424.60E-98“[LN:TRXB_LISMO]120
[AC:O32823]
[GN:TRXB]
[OR:Listeria monocytogenes]
[EC:1.6.4.5]
[DE:THIOREDOXIN REDUCTASE,]
[SP:O32823]”
SPX078578534462547623221.30E-58“[LN:YACO_BACSU]139
[AC:Q06753]
[GN:YACO]
[OR:Bacillus subtilis]
[EC:2.1.1.-]
[DE:HYPOTHETICAL TRNA/RRNA METHYLTRANSFERASE YACO,]
[SP:Q06753]”
SPX078678634472046123944.10E-93“[GI:806487]140
[LN:LACLPAGAP]
[AC:L36907]
[FN:unknown]
[OR:Lactococcus lactis]
[SR:Lactococcus lactis (individual_isolate LM0230, sub_specie]”
SPX0787787344884252NO-HIT6
SPX078878834491614831366.00E-14[LN:H70069]116
[AC:H70069:JC7099]
[PN:poly-gamma-glutamic synthesis PgsA protein]
[GN:ywtB:pgsA]
[OR:Bacillus subtilis]
SPX07897893450126378NO-HIT6
SPX079079034512768282428.80E-42[LN:F64819]158
[AC:F64819]
[PN:hypothetical protein b0822]
[CL:Methanobacterium thermoautotrophicum conserved hypothetical protein MTH1071]
[OR:Escherichia coli]
SPX07917913452212636NO-HIT6
SPX0792792345324272611961.80E-160[GI:5001711]109
[LN:AF112358]
[AC:AF112358]
[PN:C3-degrading proteinase]
[GN:cppA]
[OR:Streptococcus pneumoniae]
SPX079379334543129361174.00E-22[GI:6469268]121
[LN:SCC75A]
[AC:AL133220]
[PN:possible secreted esterase]
[GN:SCC75A.29c]
[OR:Streptomyces coelicolor A3(2)]
SPX079479434552998974871.00E-64[LN:YICL_ECOLI]136
[AC:P31437]
[GN:YICL]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 33.1 KD PROTEIN IN SELC-NLPA INTERGENIC REGION]
[SP:P31437]
SPX079579534562336992947.80E-49[LN:D70044]144
[AC:D70044]
[PN:transcription regulator GntR family homolog yvoA]
[GN:yvoA]
[CL:transcription regulator GntR]
[OR:Bacillus subtilis]
SPX07967963457521156317213.40E-294[GI:4321715]92
[LN:AF058326]
[AC:AF058326]
[PN:GMP synthase]
[GN:guaA]
[OR:Lactococcus lactis]
SPX0797797345862186NO-HIT6
SPX07987983459962882042.90E-23“[LN:JC1151]89
[AC:JC1151]
[PN:hypothetical protein, 20.3K]
[OR:Agrobacterium tumefaciens]”
SPX0799799346065195NO-HIT6
SPX08008003461130390910.00062“[GI:5824139]137
[LN:POL245436]
[AC:AJ245436:J04618:J04619:S50571:X52935:X65936]
[PN:hypothetical protein, 57.8 kD]
[OR:Pseudomonas putida]”
SPX08018013462143429849.20E-08“[GI:6009407]140
[LN:AB024946]
[AC:AB024946]
[GN:orf31]
[OR:Escherichia coli]
[SR:Escherichia coli (sub_species:enteropathogenic, strain:B171]”
SPX08028023463150450943.20E-15“[LN:Y4HP_RHISN]128
[AC:P50360]
[GN:Y4HP]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP]
[SP:P50360]”
SPX0803803346478234870.00033“[GI:5824139]137
[LN:POL245436]
[AC:AJ245436:J04618:J04619:S50571:X52935:X65936]
[PN:hypothetical protein, 57.8 kD]
[OR:Pseudomonas putida]”
SPX0804804346545513652532.70E-62“[LN:D69159]217
[AC:D69159]
[PN:methyl coenzyme M reductase system, component A2 homolog]
[GN:MTH454]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Methanobacterium thermoautotrophicum]”
SPX0805805346674222NO-HIT6
SPX08068063467232696881.90E-07[LN:E72202]96
[AC:E72202]
[PN:conserved hypothetical protein]
[GN:TM1868]
[OR:Thermotoga maritima]
SPX08078073468195585NO-HIT6
SPX0808808346958217465543.00E-83[GI:4097162]81
[LN:PMU46488]
[AC:U46488]
[PN:NrpB]
[GN:nrpB]
[OR:Proteus mirabilis]
SPX0809809347058717615262.60E-78[GI:4097161]81
[LN:PMU46488]
[AC:U46488]
[PN:NrpA]
[GN:nrpA]
[OR:Proteus mirabilis]
SPX081081034711594771313.30E-12[LN:SOXS_ECOLI]100
[AC:P22539]
[GN:SOXS]
[OR:Escherichia coli]
[DE:REGULATORY PROTEIN SOXS]
[SP:P22539]
SPX0811811347269207NO-HIT6
SPX0812812347339711918892.70E-126[GI:2995646]177
[LN:AF051092]
[AC:AF051092]
[PN:DNA modification methyltransferase M.XbaI]
[GN:xbaIM]
[FN:recognizes ds DNA sequence TCTAGA; thought to]
[OR:Xanthomonas campestris]
SPX08138133474631891281.30E-17[GI:2995645]169
[LN:AF051092]
[AC:AF051092]
[PN:restriction endonuclease R.XbaI]
[GN:xbaIR]
[FN:recognizes ds DNA sequence TCTAGA; cleaves both]
[OR:Xanthomonas campestris]
SPX08148143475611831994.80E-22[GI:2995645]169
[LN:AF051092]
[AC:AF051092]
[PN:restriction endonuclease R.XbaI]
[GN:xbaIR]
[FN:recognizes ds DNA sequence TCTAGA; cleaves both]
[OR:Xanthomonas campestris]
SPX0815815347671213NO-HIT6
SPX0816816347742912876814.70E-147[LN:H69979]107
[AC:H69979]
[PN:proteinase homolog yrrO]
[GN:yrrO]
[CL:collagenase prtC]
[OR:Bacillus subtilis]
SPX081781734782437292516.20E-58[LN:H69979]107
[AC:H69979]
[PN:proteinase homolog yrrO]
[GN:yrrO]
[CL:collagenase prtC]
[OR:Bacillus subtilis]
SPX081881834792417232254.40E-26[LN:YCBN_BACSU]145
[AC:P42246]
[GN:YCBN]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 31.7 KD PROTEIN IN GLTP-CWLJ INTERGENIC REGION (ORF13)]
[SP:P42246]
SPX08198193480243729NO-HIT6
SPX08208203481802401522.50E-16[GI:1536960]115
[LN:SOORFS]
[AC:Z79691]
[GN:yorfE]
[FN:putative transcription regulator]
[OR:Streptococcus pneumoniae]
SPX08218213482163489NO-HIT6
SPX0822822348348714619811.70E-215[LN:D70008]111
[AC:D70008]
[PN:nicotinate phosphoribosyltransferase homolog yueK]
[GN:yueK]
[OR:Bacillus subtilis]
SPX082382334842758259231.70E-122[LN:NADE_ECOLI]121
[AC:P18843:P78235]
[GN:NADE:EFG:NTRL]
[OR:Escherichia coli]
[EC:6.3.5.1]
[DE:PROTEIN)]
[SP:P18843:P78235]
SPX0824824348566198NO-HIT6
SPX082582534861845521351.80E-13[GI:7635982]117
[LN:SCE6]
[AC:AL353832]
[PN:putative acetyltransferase.]
[GN:SCE6.13]
[OR:Streptomyces coelicolor A3(2)]
SPX08268263487250750660.00023[GI:4185565]101
[LN:AF115379]
[AC:AF115379]
[PN:surface protein Pls]
[GN:pls]
[OR:Staphylococcus aureus]
SPX082782734881303903061.70E-36[LN:A41971]169
[AC:A41971:A60282:A33134]
[PN:surface protein pspA precursor:pneumococcal surface protein A]
[GN:pspA]
[CL:cpl repeat homology]
[OR:Streptococcus pneumoniae]
SPX08288283489347104112295.30E-166[LN:QUEA_BACSU]128
[AC:O32054]
[GN:QUEA]
[OR:Bacillus subtilis]
[EC:5.-.-.-]
[DE:(QUEUOSINE BIOSYNTHESIS PROTEIN QUEA)]
[SP:O32054]
SPX082982934902367083363.00E-66[LN:NAGB_BACSU]139
[AC:O35000]
[GN:NAGB]
[OR:Bacillus subtilis]
[EC:5.3.1.10]
[DE:PHOSPHATE DEAMINASE) (GNPDA) (GLCN6P DEAMINASE)]
[SP:O35000]
SPX08308303491672012481.00E-29[LN:T43742]89
[AC:T43742]
[PN:ribosomal protein S21 [imported]]
[OR:Listeria monocytogenes]
SPX0831831349231393912247.60E-165[GI:4884536]123
[LN:AB027460]
[AC:AB027460]
[PN:Hpr kinase]
[OR:Streptococcus bovis]
[SR:Streptococcus bovis (strain:JB1) DNA]
SPX083283234931925766081.30E-84“[LN:T11569]169
[AC:T11569]
[PN:prolipoprotein diacylglyceryl transferase,]
[GN:lgt]
[CL:prolipoprotein diacylglyceryl transferase]
[OR:Streptococcus mutans]
[EC:2.4.99.-]”
SPX083383334941283843331.50E-41[LN:T11570]77
[AC:T11570]
[PN:hypothetical protein 1]
[OR:Streptococcus mutans]
SPX08348343495110330NO-HIT6
SPX083583534961303901645.70E-17[LN:T11571]77
[AC:T11571]
[PN:hypothetical protein 2]
[OR:Streptococcus mutans]
SPX0836836349737711315964.30E-126“[LN:B69640]184
[AC:B69640]
[PN:coproporphyrinogen oxidase, III, oxygen-independent hemN]
[GN:hemN]
[CL:oxygen-independent coproporphyrinogen oxidase]
[OR:Bacillus subtilis]
[EC:1.3.3.3]”
SPX08378373498166498NO-HIT6
SPX08388383499246738967.20E-11[GI:4704640]92
[LN:AF110462]
[AC:AF110462]
[PN:oleoyl-ACP thioesterase]
[OR:Elaeis guineensis]
SPX083983935002036094663.10E-59[LN:H70023]124
[AC:H70023]
[PN:N-acetyl-glucosamine catabolism homolog yutF]
[GN:yutF]
[CL:nagD protein]
[OR:Bacillus subtilis]
SPX08408403501217651NO-HIT6
SPX08418413502108324NO-HIT6
SPX084284235031344024475.60E-58[LN:D69843]128
[AC:D69843]
[PN:conserved hypothetical protein yjbD]
[GN:yjbD]
[CL:hypothetical protein yjbD]
[OR:Bacillus subtilis]
SPX08438433504932792162.40E-24[LN:C69864]87
[AC:C69864]
[PN:hypothetical protein yktA]
[GN:yktA]
[OR:Bacillus subtilis]
SPX084484435052838492071.30E-46[LN:SUHB_BACSU]120
[AC:Q45499]
[GN:SUHB]
[OR:Bacillus subtilis]
[DE:EXTRAGENIC SUPPRESSOR PROTEIN SUHB HOMOLOG]
[SP:Q45499]
SPX08458453506113339NO-HIT6
SPX084684635073059151438.30E-21[LN:YEBU_ECOLI]149
[AC:P76273:O07980]
[GN:YEBU]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 53.2 KD PROTEIN IN PRC-PRPA INTERGENIC REGION]
[SP:P76273:O07980]
SPX0847847350876228NO-HIT6
SPX0848848350956168NO-HIT6
SPX0849849351078234NO-HIT6
SPX085085035112938794651.40E-80[LN:YQGG_BACSU]103
[AC:P46338]
[GN:YQGG]
[OR:Bacillus subtilis]
[DE:REGION PRECURSOR (ORF108)]
[SP:P46338]
SPX085185135123069184031.00E-99[LN:YQGH_BACSU]92
[AC:P46339]
[GN:YQGH]
[OR:Bacillus subtilis]
[DE:REGION (ORF72)]
[SP:P46339]
SPX085285235132958858422.80E-114[LN:YQGI_BACSU]92
[AC:P46340]
[GN:YQGI]
[OR:Bacillus subtilis]
[DE:REGION (ORF73)]
[SP:P46340]
SPX085385335142688047961.10E-105[LN:PSTB_METJA]145
[AC:Q58418]
[GN:PSTB:MJ1012]
[OR:Methanococcus jannaschii]
[DE:PROBABLE PHOSPHATE TRANSPORT ATP-BINDING PROTEIN PSTB]
[SP:Q58418]
SPX085485435152537597637.10E-100[LN:T43868]193
[AC:T43868]
[PN:phosphate transport system peripheral membrane protein B [imported]]
[GN:pstB]
[CL:inner membrane protein malK:ATP-binding cassette homology]
[OR:Pseudomonas putida]
SPX085585535162186542123.70E-40[GI:4530451]90
[LN:AF118229]
[AC:AF118229]
[PN:PhoU]
[GN:phoU]
[OR:Streptococcus pneumoniae]
SPX085685635172728161902.40E-30“[LN:B72357]181
[AC:B72357]
[PN:amino acid ABC transporter, periplasmic amino acid-binding protein]
[GN:TM0593]
[CL:lysine-arginine-ornithine-binding protein]
[OR:Thermotoga maritima]”
SPX0857857351842412727784.20E-129[GI:4580622]77
[LN:AF118389]
[AC:AF118389]
[PN:unknown]
[OR:Streptococcus suis]
SPX0858858351957171NO-HIT6
SPX085985935201715133403.10E-77[GI:1524117]108
[LN:LLALDB]
[AC:X82620]
[PN:alpha-acetolactate decarboxylase]
[GN:aldB]
[OR:Lactococcus lactis]
SPX08608603521672012652.40E-33[GI:1808671]129
[LN:SGCSHAG]
[AC:X65164:S52427]
[PN:putative alpha-acetolactate decarboxylase]
[GN:aldB]
[OR:Streptococcus gordonii]
SPX086186135222437291061.50E-25[LN:A69830]87
[AC:A69830]
[PN:hypothetical protein yhfC]
[GN:yhfC]
[OR:Bacillus subtilis]
SPX086286235233029062125.60E-55[LN:MURB_BACSU]150
[AC:P18579:P16669:P37581]
[GN:MURB]
[OR:Bacillus subtilis]
[EC:1.1.1.158]
[DE:ACETYLMURAMATE DEHYDROGENASE)]
[SP:P18579:P16669:P37581]
SPX0863863352437911377921.80E-114“[LN:A70180]237
[AC:A70180]
[PN:spermidine/putrescine ABC transporter, ATP-binding protein (potA) homolog]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX08648643525109327NO-HIT6
SPX086586535262116333244.20E-44“[LN:H70179]224
[AC:H70179]
[PN:spermidine/putrescine ABC transporter, permease protein (potB) homolog]
[CL:spermidine/putrescine transport system permease protein potH]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX086686635272587743467.00E-66“[LN:G70179]224
[AC:G70179]
[PN:spermidine/putrescine ABC transporter, permease protein (potC) homolog]
[CL:spermidine/putrescine transport system permease protein potI]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX086786735282266781735.20E-48[LN:POTD_ECOLI]143
[AC:P23861]
[GN:POTD]
[OR:Escherichia coli]
[DE:SPERMIDINE/PUTRESCINE-BINDING PERIPLASMIC PROTEIN PRECURSOR (SPBP)]
[SP:P23861]
SPX086886835291253751971.30E-20[LN:POTD_ECOLI]143
[AC:P23861]
[GN:POTD]
[OR:Escherichia coli]
[DE:SPERMIDINE/PUTRESCINE-BINDING PERIPLASMIC PROTEIN PRECURSOR (SPBP)]
[SP:P23861]
SPX0869869353080240NO-HIT6
SPX0870870353173219NO-HIT6
SPX087187135321634891594.70E-15[LN:G70079]136
[AC:G70079]
[PN:hypothetical protein yxjI]
[GN:yxjI]
[CL:Bacillus subtilis hypothetical protein yxjI]
[OR:Bacillus subtilis]
SPX08728723533892673322.40E-39“[LN:SYA_BACSU]146
[AC:O34526]
[GN:ALAS]
[OR:Bacillus subtilis]
[EC:6.1.1.7]
[DE:ALANYL-TRNA SYNTHETASE, (ALANINE--TRNA LIGASE) (ALARS)]
[SP:O34526]”
SPX0873873353478723615701.20E-202“[LN:SYA_BACSU]146
[AC:O34526]
[GN:ALAS]
[OR:Bacillus subtilis]
[EC:6.1.1.7]
[DE:ALANYL-TRNA SYNTHETASE, (ALANINE--TRNA LIGASE) (ALARS)]
[SP:O34526]”
SPX08748743535485145517262.50E-257[GI:2760119]136
[LN:AB000830]
[AC:AB000830]
[PN:alpha-amylase precursor]
[OR:Streptococcus bovis]
[SR:Streptococcus bovis (strain:148) DNA]
SPX0875875353664192NO-HIT6
SPX087687635372507504891.10E-62“[LN:H75077]187
[AC:H75077]
[PN:abc transporter, ATP-binding protein PAB1696]
[GN:PAB1696]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Pyrococcus abyssi]”
SPX087787735385451635NO-HIT6
SPX0878878353938811644682.20E-96[LN:YWBD_BACSU]144
[AC:P39587]
[GN:YWBD:IPA-19D]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 44.4 KD PROTEIN IN EPR-GALK INTERGENIC REGION]
[SP:P39587]
SPX087987935402266781656.60E-27[GI:5919207]100
[LN:AF184963]
[AC:AF184963]
[PN:3-dehydroquinase]
[GN:aroD]
[OR:Salmonella enteritidis]
SPX088088035412858556805.70E-89[GI:3821433]110
[LN:SPN232281]
[AC:AJ232281]
[PN:shikimate dehydrogenase]
[GN:aroE]
[OR:Streptococcus pneumoniae]
SPX0881881354235610684393.10E-84“[LN:AROB_SYNY3]148
[AC:P73997]
[GN:AROB:SLR2130]
[OR:Synechocystis sp]
[SR:,strain PCC 6803]
[EC:4.6.1.3]
[DE:3-DEHYDROQUINATE SYNTHASE,]
[SP:P73997]”
SPX0882882354338911677901.40E-142[LN:AROC_BACSU]138
[AC:P31104]
[GN:AROF]
[OR:Bacillus subtilis]
[EC:4.6.1.4]
[DE:PHOSPHOLYASE) (VEGETATIVE PROTEIN 216) (VEG216)]
[SP:P31104]
SPX0883883354436811044022.40E-127“[LN:TYRA_LACLA]165
[AC:P43901]
[GN:TYRA]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:1.3.1.12]
[DE:PREPHENATE DEHYDROGENASE, (PDH)]
[SP:P43901]”
SPX088488435451133391527.80E-16[GI:3688819]87
[LN:AF084104]
[AC:AF084104]
[PN:hypothetical protein]
[OR:Bacillus firmus]
SPX08858853546428128420941.40E-284[GI:5616525]129
[LN:AF169483]
[AC:AF169483]
[PN:5-enolpyruvylshikimate-3-phosphate synthase]
[GN:aroA]
[OR:Streptococcus pneumoniae]
SPX088688635471594772623.60E-40“[LN:AROK_LACLA]156
[AC:P43906]
[GN:AROK]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.1.71]
[DE:SHIKIMATE KINASE, (SK)]
[SP:P43906]”
SPX088788735482828467073.20E-98“[LN:PHEA_LACLA]153
[AC:P43909]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.2.1.51]
[DE:PREPHENATE DEHYDRATASE, (PDT)]
[SP:P43909]”
SPX08888883549231693917.60E-09[GI:7160813]107
[LN:EFA276231]
[AC:AJ276231]
[PN:PSR protein]
[GN:psr]
[FN:unknown]
[OR:Enterococcus faecalis]
SPX088988935502006002689.10E-46[GI:7160813]107
[LN:EFA276231]
[AC:AJ276231]
[PN:PSR protein]
[GN:psr]
[FN:unknown]
[OR:Enterococcus faecalis]
SPX089089035512828461721.10E-24[LN:LICD_HAEIN]95
[AC:P14184]
[GN:LICD]
[OR:Haemophilus influenzae]
[DE:LICD PROTEIN]
[SP:P14184]
SPX08918913552134402NO-HIT6
SPX0892892355338611582441.70E-28[LN:F70441]103
[AC:F70441]
[PN:capsular polysaccharide biosynthsis protein]
[GN:cap]
[OR:Aquifex aeolicus]
SPX089389335543299873274.10E-51[GI:3320393]111
[LN:AF030373]
[AC:AF030373]
[PN:galactosyl transferase]
[GN:cps23FU]
[OR:Streptococcus pneumoniae]
SPX089489435554781434960.00022[GI:5931973]100
[LN:AF125164]
[AC:AF125164]
[PN:putative polymerase]
[GN:wzy]
[OR:Bacteroides fragilis]
SPX08958953556151453NO-HIT6
SPX08968963557202606NO-HIT6
SPX0897897355899297NO-HIT6
SPX089889835591855553491.10E-42[GI:5360696]164
[LN:AB022909]
[AC:AB022909]
[PN:negative regulator of genetic competence]
[GN:mecA]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:Xc) DNA]
SPX08998993560128384NO-HIT6
SPX09009003561712131271.70E-11[GI:5360696]164
[LN:AB022909]
[AC:AB022909]
[PN:negative regulator of genetic competence]
[GN:mecA]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:Xc) DNA]
SPX09019013562429128714252.60E-191“[LN:DHOM_LACLA]163
[AC:P52985]
[GN:HOM]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:1.1.1.3]
[DE:HOMOSERINE DEHYDROGENASE, (HDH)]
[SP:P52985]”
SPX0902902356329087014394.70E-194“[LN:KHSE_STRPN]124
[AC:P72535]
[GN:THRB]
[OR:Streptococcus pneumoniae]
[EC:2.7.1.39]
[DE:HOMOSERINE KINASE, (HK)]
[SP:P72535]”
SPX09039033564142426NO-HIT6
SPX09049043565752251928.30E-23[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX09059053566862583666.80E-46[LN:PMSR_STRPN]110
[AC:P35593]
[GN:MSRA:EXP3]
[OR:Streptococcus pneumoniae]
[DE:(EXPORTED PROTEIN 3)]
[SP:P35593]
SPX0906906356725676812369.90E-167[LN:PMSR_STRPN]110
[AC:P35593]
[GN:MSRA:EXP3]
[OR:Streptococcus pneumoniae]
[DE:(EXPORTED PROTEIN 3)]
[SP:P35593]
SPX090790735681033091236.70E-10“[LN:E72396]180
[AC:E72396]
[PN:ABC transporter, ATP-binding protein]
[GN:TM0287]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Thermotoga maritima]”
SPX0908908356948814644723.40E-92“[LN:E72396]180
[AC:E72396]
[PN:ABC transporter, ATP-binding protein]
[GN:TM0287]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Thermotoga maritima]”
SPX0909909357062186NO-HIT6
SPX0910910357158417527227.90E-145[LN:Y08A_MYCTU]148
[AC:Q11047]
[GN:MTCY50.10]
[OR:Mycobacterium tuberculosis]
[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN CY50.10]
[SP:Q11047]
SPX09119113572862583255.10E-41[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX09129123573129387958.00E-06[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX0913913357464192NO-HIT6
SPX0914914357574222NO-HIT6
SPX0915915357669207NO-HIT6
SPX0916916357765195NO-HIT6
SPX0917917357899297NO-HIT6
SPX091891835792958854471.10E-56[LN:A70039]188
[AC:A70039]
[PN:ABC transporter (ATP-binding protein) homolog yvfR]
[GN:yvfR]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX091991935802467382891.00E-39[GI:6759480]90
[LN:BCE243712]
[AC:AJ243712]
[PN:YVFS protein]
[GN:yvfS]
[OR:Bacillus cereus]
SPX09209203581366109817155.40E-238[GI:5830547]102
[LN:SPAJ6400]
[AC:AJ006400]
[PN:histidine kinase]
[GN:hk11]
[OR:Streptococcus pneumoniae]
SPX092192135822006009322.00E-123[GI:5830548]104
[LN:SPAJ6400]
[AC:AJ006400]
[PN:response regulator]
[GN:rr11]
[OR:Streptococcus pneumoniae]
SPX09229223583337101113281.10E-176[GI:7328454]151
[LN:AB028599]
[AC:AB028599]
[PN:catabolite control protein A]
[GN:ccpA]
[OR:Streptococcus bovis]
[SR:Streptococcus bovis (strain:JB1) DNA]
SPX092392335841313932704.60E-32[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX09249243585113339895.70E-05[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX092592535863219632958.70E-56[LN:G75283]102
[AC:G75283]
[PN:L-asparaginase]
[GN:DR2353]
[CL:asparaginase]
[OR:Deinococcus radiodurans]
SPX0926926358746313892139.90E-43[LN:C69862]178
[AC:C69862]
[PN:conserved hypothetical protein ykrA]
[GN:ykrA]
[CL:Methanobacterium thermoautotrophicum conserved hypothetical protein MTH1071]
[OR:Bacillus subtilis]
SPX092792735881514531276.20E-14[LN:A69220]155
[AC:A69220]
[PN:conserved hypothetical protein MTH898]
[GN:MTH898]
[CL:Escherichia coli ybdQ protein]
[OR:Methanobacterium thermoautotrophicum]
SPX0928928358997291NO-HIT6
SPX092992935902397178194.70E-109“[LN:YFBQ_HAEIN]133
[AC:P71348]
[GN:HI0286]
[OR:Haemophilus influenzae]
[EC:2.6.1.-]
[DE:PROBABLE AMINOTRANSFERASE HI0286,]
[SP:P71348]”
SPX09309303591111333NO-HIT6
SPX093193135921253753851.70E-48“[LN:YFBQ_HAEIN]133
[AC:P71348]
[GN:HI0286]
[OR:Haemophilus influenzae]
[EC:2.6.1.-]
[DE:PROBABLE AMINOTRANSFERASE HI0286,]
[SP:P71348]”
SPX09329323593451351707.60E-20[LN:RL34_BACST]113
[AC:P23376]
[GN:RPMH]
[OR:Bacillus stearothermophilus]
[DE:50S RIBOSOMAL PROTEIN L34]
[SP:P23376]
SPX0933933359467201NO-HIT6
SPX093493435952186541169.60E-07[GI:546643]121
[LN:S70345]
[AC:S70345]
[PN:SpaA]
[GN:SpaA]
[OR:Streptococcus sobrinus]
[SR:Streptococcus sobrinus MUCOB 263]
SPX09359353596752251806.20E-19[LN:YABD_BACSU]137
[AC:P37545]
[GN:YABD]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 29.2 KD PROTEIN IN METS-KSGA INTERGENIC REGION]
[SP:P37545]
SPX093693635971815434693.60E-60[LN:YABD_BACSU]137
[AC:P37545]
[GN:YABD]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 29.2 KD PROTEIN IN METS-KSGA INTERGENIC REGION]
[SP:P37545]
SPX093793735981875612352.70E-52[LN:YABF_BACSU]137
[AC:P37547]
[GN:YABF]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 20.7 KD PROTEIN IN METS-KSGA INTERGENIC REGION]
[SP:P37547]
SPX09389383599304912NO-HIT6
SPX09399393600992971493.30E-15[GI:7576923]109
[LN:AF242367]
[AC:AF242367]
[PN:lactococcin 972]
[GN:lclA]
[OR:Lactococcus lactis subsp. lactis]
SPX09409403601269807655.50E-08[GI:3355783]98
[LN:LLJ002203]
[AC:AJ002203]
[PN:putative immunity]
[GN:orf2]
[OR:Lactococcus lactis]
SPX0941941360245013503571.30E-89[GI:4009478]83
[LN:AF068902]
[AC:AF068902]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX094294236032146426672.50E-87[GI:4009479]83
[LN:AF068902]
[AC:AF068902]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX09439433604103309NO-HIT6
SPX09449443605169507NO-HIT6
SPX094594536062918737813.80E-104[LN:KSGA_BACSU]111
[AC:P37468]
[GN:KSGA]
[OR:Bacillus subtilis]
[EC:2.1.1.-]
[DE:DIMETHYLTRANSFERASE)]
[SP:P37468]
SPX094694636072938793945.10E-100[LN:A69879]140
[AC:A69879]
[PN:conserved hypothetical protein yloQ]
[GN:yloQ]
[CL:conserved hypothetical protein HI1714]
[OR:Bacillus subtilis]
SPX094794736083019034601.20E-69“[LN:RPE_RHOCA]154
[AC:P51012]
[GN:CBBE]
[OR:Rhodobacter capsulatus]
[SR:,Rhodopseudomonas capsulata]
[EC:5.1.3.1]
[DE:EPIMERASE) (PPE) (R5P3E)]
[SP:P51012]”
SPX094894836092216631433.50E-18[LN:C69879]87
[AC:C69879]
[PN:hypothetical protein yloS]
[GN:yloS]
[OR:Bacillus subtilis]
SPX094994936104051215915.10E-07[LN:E81528]140
[AC:E81528]
[PN:conserved hypothetical protein CP0874 [imported]]
[GN:CP0874]
[OR:Chlamydophila pneumoniae:Chlamydia pneumoniae]
SPX095095036113149424531.00E-88[LN:G69818]93
[AC:G69818]
[PN:CMP-binding factor homolog yhaM]
[GN:yhaM]
[OR:Bacillus subtilis]
SPX095195136122768284982.80E-98[GI:2706406]117
[LN:LLAJ642]
[AC:AJ222642]
[GN:purR]
[FN:activator of purine biosynthetic genes]
[OR:Lactococcus lactis]
SPX0952952361370210830.00046“[LN:TABA_PSESZ]110
[AC:P31851]
[GN:TABA]
[OR:Pseudomonas syringae]
[SR:,pvtabaci]
[DE:TABA PROTEIN]
[SP:P31851]”
SPX095395336141283841993.60E-21“[LN:TABA_PSESZ]110
[AC:P31851]
[GN:TABA]
[OR:Pseudomonas syringae]
[SR:,pvtabaci]
[DE:TABA PROTEIN]
[SP:P31851]”
SPX09549543615100300NO-HIT6
SPX0955955361633510053718.10E-63“[LN:TABA_PSESZ]110
[AC:P31851]
[GN:TABA]
[OR:Pseudomonas syringae]
[SR:,pvtabaci]
[DE:TABA PROTEIN]
[SP:P31851]”
SPX0956956361726579511218.40E-152[LN:PFLA_STRMU]106
[AC:O68575]
[GN:ACT:PFLC]
[OR:Streptococcus mutans]
[EC:1.97.1.4]
[DE:ENZYME)]
[SP:O68575]
SPX095795736183099271406.90E-32[GI:6117974]98
[LN:AF139908]
[AC:AF139908]
[PN:membrane protein homolog]
[OR:Listeria monocytogenes]
SPX09589583619932791089.80E-09[LN:T35660]96
[AC:T35660]
[PN:probable acylphosphatase]
[GN:SC7A1.20]
[OR:Streptomyces coelicolor]
SPX095995936202537592171.10E-43[LN:G69984]132
[AC:G69984]
[PN:rRNA methylase homolog ysgA]
[GN:ysgA]
[CL:conserved hypothetical protein HI0860]
[OR:Bacillus subtilis]
SPX096096036212286844331.10E-57[GI:3171165]120
[LN:AF064763]
[AC:AF064763]
[PN:putative membrane spanning protein]
[OR:Lactococcus lactis subsp. cremoris]
SPX0961961362272216NO-HIT6
SPX0962962362333199313871.70E-186“[LN:ASNA_HAEIN]157
[AC:P44338]
[GN:ASNA:HI0564]
[OR:Haemophilus influenzae]
[EC:6.3.1.1]
[DE:ASPARTATE--AMMONIA LIGASE, (ASPARAGINE SYNTHETASE A)]
[SP:P44338]”
SPX096396336241805402791.30E-33[LN:E69874]176
[AC:E69874]
[PN:conserved hypothetical protein ylbH]
[GN:ylbH]
[CL:Escherichia coli hypothetical 21.7K protein (ftsY-nikA intergenic region)]
[OR:Bacillus subtilis]
SPX096496436251233691843.00E-25[LN:G81347]136
[AC:G81347]
[PN:3-deoxy-D-manno-octulosonic-acid transferase Cj0767c [imported]]
[GN:kdtB:Cj0767c]
[OR:Campylobacter jejuni]
SPX096596536262397171847.20E-17[LN:A69875]87
[AC:A69875]
[PN:hypothetical protein ylbL]
[GN:ylbL]
[OR:Bacillus subtilis]
SPX09669663627782341011.90E-16[LN:A69875]87
[AC:A69875]
[PN:hypothetical protein ylbL]
[GN:ylbL]
[OR:Bacillus subtilis]
SPX0967967362895285NO-HIT6
SPX0968968362942812846203.20E-133[LN:MURA_ACICA]124
[AC:P33986]
[GN:MURA:MURZ]
[OR:Acinetobacter calcoaceticus]
[EC:2.5.1.7]
[DE:TRANSFERASE) (EPT)]
[SP:P33986]
SPX09699693630752253204.60E-41[LN:EPUA_STRPN]97
[AC:Q03159]
[GN:EPUA]
[OR:Streptococcus pneumoniae]
[DE:EPUA PROTEIN]
[SP:Q03159]
SPX0970970363127582513922.50E-182“[LN:NUCE_STRPN]151
[AC:Q03158]
[GN:ENDA]
[OR:Streptococcus pneumoniae]
[EC:3.1.30.-]
[DE:DNA-ENTRY NUCLEASE (COMPETENCE-SPECIFIC NUCLEASE),]
[SP:Q03158]”
SPX0971971363232898411684.20E-160[GI:2952527]100
[LN:AF051356]
[AC:AF051356]
[PN:putative hemolysin]
[GN:hlyX]
[OR:Streptococcus mutans]
SPX09729723633952852666.50E-33[GI:2952527]100
[LN:AF051356]
[AC:AF051356]
[PN:putative hemolysin]
[GN:hlyX]
[OR:Streptococcus mutans]
SPX097397336341204361219210[LN:T44375]121
[AC:T44375]
[PN:rpoB protein [imported]]
[CL:DNA-directed RNA polymerase beta chain]
[OR:Bacillus halodurans]
SPX09749743635116348NO-HIT6
SPX0975975363657171NO-HIT6
SPX097697636371226367840090[LN:RPOC_STRPY]150
[AC:P95816]
[GN:RPOC]
[OR:Streptococcus pyogenes]
[EC:2.7.7.6]
[DE:BETA′CHAIN) (RNA POLYMERASE BETA′SUBUNIT) (FRAGMENT)]
[SP:P95816]
SPX09779773638131393NO-HIT6
SPX097897836391384141924.30E-48[GI:1655704]121
[LN:XLNM23]
[AC:X97899]
[PN:NM23/nucleoside diphosphate kinase]
[OR:Xenopus laevis]
[SR:African clawed frog]
SPX0979979364093279NO-HIT6
SPX098098036412116334721.50E-87[GI:4009479]83
[LN:AF068902]
[AC:AF068902]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX0981981364267220162774.50E-70[GI:4009478]83
[LN:AF068902]
[AC:AF068902]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX0982982364365195NO-HIT6
SPX098398336442888641102.30E-09[LN:JC6007]152
[AC:JC6007]
[PN:transcription activator plcR]
[GN:plcR]
[CL:Bacillus thuringiensis transcription activator plcR]
[OR:Bacillus thuringiensis]
SPX09849843645137411NO-HIT6
SPX098598536461594771662.20E-36[LN:C69786]130
[AC:C69786]
[PN:conserved hypothetical protein ydiB]
[GN:ydiB]
[CL:hypothetical protein HI0065]
[OR:Bacillus subtilis]
SPX098698636471735191497.60E-28[LN:D72360]96
[AC:D72360]
[PN:conserved hypothetical protein]
[GN:TM0577]
[OR:Thermotoga maritima]
SPX0987987364833910171826.50E-46[LN:LYTR_BACSU]105
[AC:Q02115]
[GN:LYTR]
[OR:Bacillus subtilis]
[DE:MEMBRANE-BOUND PROTEIN LYTR]
[SP:Q02115]
SPX09889883649419125720151.70E-272[LN:CINA_STRPN]161
[AC:P54184:Q54853]
[GN:CINA:EXP10]
[OR:Streptococcus pneumoniae]
[DE:PUTATIVE COMPETENCE-DAMAGE PROTEIN (EXPORTED PROTEIN 10)]
[SP:P54184:Q54853]
SPX09899893650389116719286.10E-256[LN:RECA_STRPN]97
[AC:P30758]
[GN:RECA]
[OR:Streptococcus pneumoniae]
[DE:RECA PROTEIN]
[SP:P30758]
SPX09909903651457137122520[GI:2398825]96
[LN:SPCINREC]
[AC:Z34303]
[PN:DinF protein]
[GN:dinF]
[OR:Streptococcus pneumoniae]
SPX0991991365231995717861.50E-240[LN:ALYS_STRPN]160
[AC:P06653]
[GN:LYTA]
[OR:Streptococcus pneumoniae]
[EC:3.5.1.28]
[DE:HYDROLASE) (MUCOPEPTIDE AMINOHYDROLASE) (CELL WALL HYDROLASE)]
[SP:P06653]
SPX0992992365379237NO-HIT6
SPX0993993365481243NO-HIT6
SPX09949943655120360NO-HIT6
SPX09959953656142426NO-HIT6
SPX0996996365775225NO-HIT6
SPX099799736583329966764.50E-129[GI:2398827]94
[LN:SPCINREC]
[AC:Z34303]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX0998998365982246NO-HIT6
SPX0999999366090270NO-HIT6
SPX10001000366187261NO-HIT6
SPX1001100136621013032967.00E-36[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX100210023663441321085.70E-09[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX100310033664153459NO-HIT6
SPX100410043665203609NO-HIT6
SPX100510053666137411NO-HIT6
SPX100610063667472141624260[LN:A28568]110
[AC:A28568:S12829]
[PN:pneumolysin]
[CL:dipeptide transport protein]
[OR:Streptococcus pneumoniae]
SPX1007100736682397179151.30E-119[LN:A64963]119
[AC:A64963]
[PN:conserved hypothetical protein b1983]
[CL:hypothetical protein MG332]
[OR:Escherichia coli]
SPX1008100836691504501049.20E-07[LN:C72329]93
[AC:C72329]
[PN:hypothetical protein TM0816]
[GN:TM0816]
[OR:Thermotoga maritima]
SPX1009100936702918733091.20E-35[GI:6759558]116
[LN:SC7A8]
[AC:AL137187]
[PN:putative ABC transporter]
[GN:SC7A8.02]
[OR:Streptomyces coelicolor A3(2)]
SPX10101010367134410323357.80E-76[GI:6759559]116
[LN:SC7A8]
[AC:AL137187]
[PN:putative ABC transporter]
[GN:SC7A8.03]
[OR:Streptomyces coelicolor A3(2)]
SPX101110113672121363NO-HIT6
SPX1012101236731685041302.10E-10[LN:Y374_METJA]114
[AC:Q57819]
[GN:MJ0374]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL PROTEIN MJ0374]
[SP:Q57819]
SPX101310133674150450NO-HIT6
SPX101410143675225675NO-HIT6
SPX101510153676742221258.00E-13[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX101610163677100300NO-HIT6
SPX1017101736781063182766.70E-34[LN:G69998]127
[AC:G69998]
[PN:thioredoxin H1 homolog ytpP]
[GN:ytpP]
[CL:thioredoxin:thioredoxin homology]
[OR:Bacillus subtilis]
SPX101810183679126378NO-HIT6
SPX1019101936802096272175.30E-44[LN:A69999]172
[AC:A69999]
[PN:phenylalanyl-tRNA synthetase (beta subunit) homolog ytpR]
[GN:ytpR]
[CL:Mycoplasma genitalium hypothetical protein MG449]
[OR:Bacillus subtilis]
SPX1020102036812547623544.20E-67[GI:2425123]90
[LN:AF019986]
[AC:AF019986]
[PN:PksB]
[GN:pksB]
[OR:Dictyostelium discoideum]
SPX1021102136821323962271.20E-34[GI:6716352]136
[LN:AF145054]
[AC:AF145054:AF001793:AF118440:U89246]
[PN:ORF9]
[GN:orf9]
[OR:Streptococcus thermophilus bacteriophage 7201]
SPX102210223683952854601.90E-58[GI:4566772]105
[LN:AF117741]
[AC:AF117741]
[PN:cochaperonin GroES]
[GN:groES]
[OR:Streptococcus pneumoniae]
SPX1023102336842036093448.20E-43[GI:1196510]143
[LN:MSGTCWPA]
[AC:M15467]
[PN:unknown protein]
[OR:Mycobacterium tuberculosis]
[SR:Mycobacterium tuberculosis (strain Erdman) DNA]
SPX102410243685541162326110[GI:4566773]103
[LN:AF117741]
[AC:AF117741]
[PN:chaperonin GroEL]
[GN:groEL]
[OR:Streptococcus pneumoniae]
SPX10251025368670210703.30E-06[LN:C71647]93
[AC:C71647]
[PN:hypothetical protein RP851]
[GN:RP851]
[OR:Rickettsia prowazekii]
SPX102610263687842521391.80E-13[LN:F72338]96
[AC:F72338]
[PN:conserved hypothetical protein]
[GN:TM0731]
[OR:Thermotoga maritima]
SPX10271027368864192NO-HIT6
SPX1028102836892587741296.70E-09[LN:T33885]149
[AC:T33885]
[PN:hypothetical protein H14E04.1]
[GN:H14E04.1]
[CL:24-sterol C-methyltransferase:bioC homology]
[OR:Caenorhabditis elegans]
SPX1029102936901133391331.50E-11[LN:AB025228]111
[AC:AB025228]
[GN:rgg]
[OR:Streptococcus oralis]
[SR:Streptococcus oralis (strain:ATCC10557) DNA]
SPX103010303691116348908.90E-06[LN:AB025228]111
[AC:AB025228]
[GN:rgg]
[OR:Streptococcus oralis]
[SR:Streptococcus oralis (strain:ATCC10557) DNA]
SPX1031103136921785342944.90E-36[LN:F69815]136
[AC:F69815]
[PN:hypothetical protein ygaC]
[GN:ygaC]
[CL:Bacillus subtilis hypothetical protein ygaC]
[OR:Bacillus subtilis]
SPX10321032369360180NO-HIT6
SPX1033103336942878612263.30E-32[LN:H69800]87
[AC:H69800]
[PN:hypothetical protein yfhG]
[GN:yfhG]
[OR:Bacillus subtilis]
SPX10341034369545213566061.00E-145[LN:F69806]129
[AC:F69806]
[PN:RNA methyltransferase homolog yfjO]
[GN:yfjO]
[CL:hypothetical protein HI0333]
[OR:Bacillus subtilis]
SPX10351035369682246NO-HIT6
SPX10361036369750150827.60E-06[LN:G71244]95
[AC:G71244]
[PN:hypothetical protein PH0217]
[GN:PH0217]
[OR:Pyrococcus horikoshii]
SPX10371037369862186NO-HIT6
SPX103810383699872611363.90E-14[LN:G81516]130
[AC:G81516]
[PN:hypothetical protein CP0988 [imported]]
[GN:CP0988]
[OR:Chlamydophila pneumoniae:Chlamydia pneumoniae]
SPX103910393700762281901.00E-21[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX10401040370179237NO-HIT6
SPX104110413702942823012.00E-35[LN:DHAS_STRMU]108
[AC:P10539]
[GN:ASD]
[OR:Streptococcus mutans]
[EC:1.2.1.11]
[DE:DEHYDROGENASE)]
[SP:P10539]
SPX104210423703922763253.80E-40[LN:DHAS_STRMU]108
[AC:P10539]
[GN:ASD]
[OR:Streptococcus mutans]
[EC:1.2.1.11]
[DE:DEHYDROGENASE)]
[SP:P10539]
SPX1043104337042226665901.20E-108[LN:DHAS_STRMU]108
[AC:P10539]
[GN:ASD]
[OR:Streptococcus mutans]
[EC:1.2.1.11]
[DE:DEHYDROGENASE)]
[SP:P10539]
SPX1044104437053129361922.60E-55“[LN:B72246]187
[AC:B72246]
[PN:dihydrodipicolinate synthase, TM1521 [similarity]]
[GN:TM1521]
[CL:Pseudomonas 5-dehydro-4-deoxyglucarate dehydratase]
[OR:Thermotoga maritima]
[EC:4.2.1.52]”
SPX104510453706458137413121.10E-249[GI:6448626]167
[LN:SAG251564]
[AC:AJ251564]
[PN:thiophene degradation protein F]
[GN:thdF]
[FN:putative thiophene and furan oxidation gene]
[OR:Streptococcus agalactiae]
SPX104610463707752251271.30E-12“[LN:A43397]153
[AC:A43397:S35225]
[PN:4-oxalocrotonate tautomerase, xylH]
[GN:xylH]
[CL:4-oxalocrotonate tautomerase]
[OR:Pseudomonas putida]
[EC:5.3.2.-]”
SPX1047104737081644927247.00E-97“[LN:KITH_STRGC]123
[AC:P47848]
[GN:TDK]
[OR:Streptococcus gordonii challis]
[EC:2.7.1.21]
[DE:THYMIDINE KINASE,]
[SP:P47848]”
SPX1048104837092818436422.20E-103[LN:RF1_BACSU]114
[AC:P45872]
[GN:PRFA]
[OR:Bacillus subtilis]
[DE:PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)]
[SP:P45872]
SPX1049104937101434293502.60E-43[LN:RF1_BACSU]114
[AC:P45872]
[GN:PRFA]
[OR:Bacillus subtilis]
[DE:PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)]
[SP:P45872]
SPX1050105037112808401838.00E-41[LN:HEMK_BACSU]98
[AC:P45873]
[GN:YWKE]
[OR:Bacillus subtilis]
[DE:HEMK PROTEIN HOMOLOG]
[SP:P45873]
SPX1051105137122016032441.80E-32[GI:6015811]110
[LN:SSU18930]
[AC:Y18930]
[PN:hypothetical protein]
[GN:ORF-c09_003]
[OR:Sulfolobus solfataricus]
SPX105210523713144432971.30E-05[LN:PHNO_ECOLI]89
[AC:P16691]
[GN:PHNO]
[OR:Escherichia coli]
[DE:PHNO PROTEIN]
[SP:P16691]
SPX10531053371441912578587.90E-176[LN:GLYA_BACSU]110
[AC:P39148]
[GN:GLYA:GLYC:IPC-34D]
[OR:Bacillus subtilis]
[EC:2.1.2.1]
[DE:(SHMT)]
[SP:P39148]
SPX10541054371533610081303.90E-11[GI:6899993]109
[LN:CST130879]
[AC:AJ130879]
[PN:hypothetical protein]
[FN:unknown]
[OR:Clostridium sticklandii]
SPX1055105537162056152431.60E-27[LN:F69900]101
[AC:F69900]
[PN:transposon-related protein homolog yocA]
[GN:yocA]
[OR:Bacillus subtilis]
SPX1056105637173259751047.60E-08[LN:YPUA_BACSU]160
[AC:P31847:P37951]
[GN:YPUA]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 31.3 KD PROTEIN IN LYSA-PPIB INTERGENIC REGION (ORFX19)]
[SP:P31847:P37951]
SPX10571057371854816447675.90E-131[LN:E69793]129
[AC:E69793]
[PN:RNA methyltransferase homolog yefA]
[GN:yefA]
[CL:hypothetical protein HI0333]
[OR:Bacillus subtilis]
SPX10581058371998294NO-HIT6
SPX10591059372083249NO-HIT6
SPX10601060372165195813.20E-08[LN:C69931]98
[AC:C69931]
[PN:transcription regulator homolog yozG]
[GN:yozG]
[OR:Bacillus subtilis]
SPX10611061372280240NO-HIT6
SPX10621062372334510352763.80E-70[GI:2276374]148
[LN:CDU02617]
[AC:U02617]
[PN:DtxR/iron regulated lipoprotein precursor]
[GN:irp1]
[FN:iron transport]
[OR:Corynebacterium diphtheriae]
SPX106310633724212636NO-HIT6
SPX10641064372533610086431.40E-86[LN:T44797]161
[AC:T44797]
[PN:iron transport membrane protein irp1B [imported]]
[GN:irp1B]
[CL:vitamin B12 transport protein btuC]
[OR:Corynebacterium diphtheriae]
SPX10651065372633610084841.10E-82[LN:T44798]161
[AC:T44798]
[PN:iron transport membrane protein irp1C [imported]]
[GN:irp1C]
[CL:vitamin B12 transport protein btuC]
[OR:Corynebacterium diphtheriae]
SPX10661066372774222NO-HIT6
SPX106710673728138414NO-HIT6
SPX1068106837292657956946.10E-91[LN:G70022]176
[AC:G70022]
[PN:iron(III) dicitrate transport permease homolog yusV]
[GN:yusV]
[CL:inner membrane protein malK:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX106910693730872611511.30E-14[GI:2467226]96
[LN:LLLPK214]
[AC:X92946:Y10522]
[PN:transposase]
[GN:tnpA]
[OR:Lactococcus lactis]
SPX1070107037311524561371.10E-10“[LN:T4BB_BACCO]133
[AC:Q07606]
[GN:BCGIB]
[OR:Bacillus coagulans]
[EC:3.1.21.-]
[DE:RESTRICTION ENZYME BGCI BETA SUBUNIT,]
[SP:Q07606]”
SPX10711071373292276NO-HIT6
SPX10721072373383249NO-HIT6
SPX10731073373470210NO-HIT6
SPX10741074373556016801383.40E-35[GI:6681569]164
[LN:AB014436]
[AC:AB014436]
[PN:cassette chromosome recombinase B]
[GN:ccrB]
[OR:Staphylococcus aureus]
[SR:Staphylococcus aureus (strain:85/2082) DNA]
SPX107510753736204612NO-HIT6
SPX10761076373763189NO-HIT6
SPX107710773738253759NO-HIT6
SPX107810783739285855704.40E-09[GI:7020551]129
[LN:AK000453]
[AC:AK000453]
[OR:Homo sapiens]
[SR:Homo sapiens signet-ring cell carcinoma cell_line:KATO III cDNA t]
SPX1079107937402958851924.90E-36[LN:F69795]97
[AC:F69795]
[PN:conserved hypothetical protein yerQ]
[GN:yerQ]
[OR:Bacillus subtilis]
SPX108010803741932791241.30E-19“[LN:JS0673]127
[AC:JS0673]
[PN:neopullulanase,]
[CL:neopullulanase:alpha-amylase core homology]
[OR:Bacillus sp.]
[EC:3.2.1.135]”
SPX10811081374248514556833.10E-176“[LN:F70033]156
[AC:F70033]
[PN:glucan 1,4-alpha-maltohydrolase homolog yvdF]
[GN:yvdF]
[CL:neopullulanase:alpha-amylase core homology]
[OR:Bacillus subtilis]”
SPX108210823743101303NO-HIT6
SPX1083108337441434292499.00E-30[GI:6102604]127
[LN:AF144880]
[AC:AF144880]
[PN:aminoglycoside 6′-N-acetyltransferase]
[GN:aac(6′)-Iy]
[OR:Salmonella enteritidis]
SPX108410843745190570NO-HIT6
SPX10851085374671213NO-HIT6
SPX10861086374794282NO-HIT6
SPX108710873748651951848.80E-20[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX10881088374941012304191.50E-74[LN:FTSW_ENTHR]114
[AC:Q47866]
[GN:FTSW]
[OR:Enterococcus hirae]
[DE:PROBABLE CELL DIVISION PROTEIN FTSW]
[SP:Q47866]
SPX10891089375089926974181.60E-169[GI:144985]176
[LN:CORPEPC]
[AC:M25819]
[PN:phosphoenolpyruvate carboxylase]
[OR:Corynebacterium glutamicum]
[SR:Corynebacterium glutamicum (clone: pTG1200.) (tissue library: ATC]
SPX109010903751102306NO-HIT6
SPX1091109137522106301052.60E-05[LN:H71693]93
[AC:H71693]
[PN:hypothetical protein RP367]
[GN:RP367]
[OR:Rickettsia prowazekii]
SPX1092109237532236691636.00E-23[LN:A71694]93
[AC:A71694]
[PN:hypothetical protein RP368]
[GN:RP368]
[OR:Rickettsia prowazekii]
SPX1093109337542537593651.80E-45[GI:1661179]119
[LN:SMU75471]
[AC:U75471]
[PN:high affinity branched chain amino acid]
[GN:livG]
[OR:Streptococcus mutans]
SPX10941094375564192822.10E-05[LN:A71007]95
[AC:A71007]
[PN:hypothetical protein PH1351]
[GN:PH1351]
[OR:Pyrococcus horikoshii]
SPX10951095375659217766941.40E-161“[LN:PRIM_LACLA]150
[AC:Q04505]
[GN:DNAG:DNAE]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.7.-]
[DE:DNA PRIMASE,]
[SP:Q04505]”
SPX10961096375730591514522.30E-194[LN:RPOD_STRPN]117
[AC:O08388]
[GN:RPOD]
[OR:Streptococcus pneumoniae]
[DE:RNA POLYMERASE SIGMA FACTOR RPOD]
[SP:O08388]
SPX109710973758661982902.40E-35[LN:RPOD_STRPN]117
[AC:O08388]
[GN:RPOD]
[OR:Streptococcus pneumoniae]
[DE:RNA POLYMERASE SIGMA FACTOR RPOD]
[SP:O08388]
SPX1098109837591103305565.10E-73[GI:2108332]69
[LN:SPDNAGCPO]
[AC:Y11463]
[OR:Streptococcus pneumoniae]
SPX10991099376069207NO-HIT6
SPX11001100376126780113571.40E-186[GI:2108333]79
[LN:SPDNAGCPO]
[AC:Y11463]
[GN:cpoA]
[OR:Streptococcus pneumoniae]
SPX110111013762661983184.00E-38[GI:2108333]79
[LN:SPDNAGCPO]
[AC:Y11463]
[GN:cpoA]
[OR:Streptococcus pneumoniae]
SPX110211023763442132614751.70E-200[GI:2108334]69
[LN:SPDNAGCPO]
[AC:Y11463]
[OR:Streptococcus pneumoniae]
SPX110311033764591771513.70E-16[LN:B72287]96
[AC:B72287]
[PN:conserved hypothetical protein]
[GN:TM1156]
[OR:Thermotoga maritima]
SPX110411043765392117610215.10E-184[LN:OBG_BACSU]112
[AC:P20964]
[GN:OBG]
[OR:Bacillus subtilis]
[DE:SPO0B-ASSOCIATED GTP-BINDING PROTEIN]
[SP:P20964]
SPX11051105376642012604249.00E-142[LN:MURA_BACSU]140
[AC:P19670:Q03225]
[GN:MURA:MURZ]
[OR:Bacillus subtilis]
[EC:2.5.1.7]
[DE:ENOLPYRUVYL TRANSFERASE) (EPT)]
[SP:P19670:Q03225]
SPX1106110637671765281561.00E-17[LN:C69895]170
[AC:C69895]
[PN:conserved hypothetical protein yoaA]
[GN:yoaA]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ]
[OR:Bacillus subtilis]
SPX11071107376842612784254.20E-85[LN:A69998]87
[AC:A69998]
[PN:hypothetical protein ytoI]
[GN:ytoI]
[OR:Bacillus subtilis]
SPX1108110837692878613453.30E-65“[LN:T44405]158
[AC:T44405]
[PN:methionyl aminopeptidase, map [imported]]
[CL:Escherichia coli methionyl aminopeptidase]
[OR:Bacillus halodurans]
[EC:3.4.11.18]”
SPX1109110937701815433072.50E-38[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX111011103771752251045.80E-08[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX1111111137721303903844.80E-49[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX111211123773764229213517.70E-282[LN:E69794]118
[AC:E69794]
[PN:ATP-dependent DNA helicase homolog yerF]
[GN:yerF]
[CL:helicase II]
[OR:Bacillus subtilis]
SPX1113111337742407204882.80E-62[LN:RADC_BACSU]116
[AC:Q02170]
[GN:YSXA]
[OR:Bacillus subtilis]
[DE:DNA REPAIR PROTEIN RADC HOMOLOG (ORFB)]
[SP:Q02170]
SPX1114111437752306902376.50E-27“[LN:YDP3_LACLA]162
[AC:P22347]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:HYPOTHETICAL 18.7 KD PROTEIN IN PEPX 3′REGION (ORF3)]
[SP:P22347]”
SPX1115111537762146423392.60E-68[LN:A69787]87
[AC:A69787]
[PN:hypothetical protein ydiH]
[GN:ydiH]
[OR:Bacillus subtilis]
SPX11161116377784252NO-HIT6
SPX111711173778116348NO-HIT6
SPX1118111837792657952882.40E-63[LN:E69981]141
[AC:E69981]
[PN:iron-sulfur cofactor synthesis protein yrvO]
[GN:yrvO]
[CL:nitrogen fixation protein nifS]
[OR:Bacillus subtilis]
SPX1119111937801454351494.90E-18[GI:2289093]102
[LN:CAU76387]
[AC:U76387]
[PN:PRPP synthetase]
[GN:prs]
[OR:Corynebacterium ammoniagenes]
SPX1120112037811835495476.60E-75[GI:2289093]102
[LN:CAU76387]
[AC:U76387]
[PN:PRPP synthetase]
[GN:prs]
[OR:Corynebacterium ammoniagenes]
SPX1121112137821905701641.20E-26[LN:C69844]136
[AC:C69844]
[PN:hypothetical protein yjbK]
[GN:yjbK]
[CL:Bacillus subtilis hypothetical protein yjbK]
[OR:Bacillus subtilis]
SPX1122112237831685043386.80E-68[LN:E69844]139
[AC:E69844]
[PN:GTP pyrophosphokinase homolog yjbM]
[GN:yjbM]
[CL:GTP pyrophosphokinase related protein]
[OR:Bacillus subtilis]
SPX11231123378471213906.20E-06[LN:E69844]139
[AC:E69844]
[PN:GTP pyrophosphokinase homolog yjbM]
[GN:yjbM]
[CL:GTP pyrophosphokinase related protein]
[OR:Bacillus subtilis]
SPX1124112437852637893094.70E-67[LN:F69844]140
[AC:F69844]
[PN:conserved hypothetical protein yjbN]
[GN:yjbN]
[CL:conserved hypothetical protein HI0072]
[OR:Bacillus subtilis]
SPX1125112537862998972863.40E-66[LN:YJBO_BACSU]137
[AC:O31613]
[GN:YJBO]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 31.5 KD PROTEIN IN MECA-TENA INTERGENIC REGION]
[SP:O31613]
SPX1126112637873259758675.10E-115[LN:PTA_BACSU]152
[AC:P39646]
[GN:PTA:IPA-88D]
[OR:Bacillus subtilis]
[EC:2.3.1.8]
[DE:(PHOSPHOTRANSACETYLASE) (VEGETATIVE PROTEIN 43) (VEG43)]
[SP:P39646]
SPX11271127378879237NO-HIT6
SPX1128112837891995974723.10E-122[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX1129112937901093272802.00E-34[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX1130113037911735198753.10E-119[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX1131113137921083241903.90E-21[LN:YAAK_BACSU]137
[AC:P24281]
[GN:YAAK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 11.8 KD PROTEIN IN DNAZ-RECR INTERGENIC REGION]
[SP:P24281]
SPX113211323793231693891.90E-05[LN:E69896]87
[AC:E69896]
[PN:hypothetical protein yoaK]
[GN:yoaK]
[OR:Bacillus subtilis]
SPX1133113337941053153603.20E-44[LN:RL21_BACSU]110
[AC:P26908]
[GN:RPLU]
[OR:Bacillus subtilis]
[DE:50S RIBOSOMAL PROTEIN L21 (BL20)]
[SP:P26908]
SPX113411343795147441NO-HIT6
SPX1135113537961153451521.30E-22[LN:YSXB_BACSU]159
[AC:P26942:Q45629]
[GN:YSXB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 12.3 KD PROTEIN IN RPLU-RPMA INTERGENIC REGION (ORF X)]
[SP:P26942:Q45629]
SPX113611363797982943721.10E-46[LN:RL27_BACSU]117
[AC:P05657]
[GN:RPMA]
[OR:Bacillus subtilis]
[DE:50S RIBOSOMAL PROTEIN L27 (BL30) (BL24)]
[SP:P05657]
SPX11371137379855165774.70E-09[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX1138113837993069188081.30E-107[GI:2289231]158
[LN:SAU92073]
[AC:U92073]
[PN:macrolide-efflux protein]
[GN:mreA]
[FN:resistance to 14- and 15-membered macrolides]
[OR:Streptococcus agalactiae]
SPX1139113938002838495312.80E-71[LN:YPJC_BACSU]142
[AC:P42978]
[GN:YPJC:JOJC]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 23.6 KD PROTEIN IN QCRC-DAPB INTERGENIC REGION]
[SP:P42978]
SPX1140114038012808402529.50E-36[GI:671632]86
[LN:SADIRED]
[AC:Z16422]
[PN:unknown]
[GN:ORF2]
[OR:Staphylococcus aureus]
SPX114111413802922763979.60E-50[GI:5209334]112
[LN:L40356]
[AC:L40356]
[PN:histone-like DNA-binding protein]
[GN:hlpA]
[OR:Streptococcus gordonii]
SPX11421142380363419029052.00E-202[LN:YDIF_BACSU]131
[AC:O05519]
[GN:YDIF]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YDIF]
[SP:O05519]
SPX1143114338042988942048.40E-33[GI:4102023]134
[LN:AF007761]
[AC:AF007761]
[PN:MutR]
[GN:mutR]
[FN:positive transcriptional regulator of mutA]
[OR:Streptococcus mutans]
SPX11441144380539311791135.30E-22[LN:H72265]93
[AC:H72265]
[PN:hypothetical protein TM1336]
[GN:TM1336]
[OR:Thermotoga maritima]
SPX11451145380665619685211.40E-217“[LN:F69794]140
[AC:F69794]
[PN:DNA ligase (NAD+),]
[GN:yerG]
[CL:polydeoxyribonucleotide synthase (NAD+)]
[OR:Bacillus subtilis]
[EC:6.5.1.2]”
SPX11461146380776022806202.20E-109[GI:3089609]90
[LN:AF060205]
[AC:AF060205]
[PN:pullulanase]
[GN:pul]
[OR:Thermus sp. IM6501]
SPX114711473808475142518182.70E-245[LN:GAPN_STRMU]108
[AC:Q59931]
[GN:GAPN]
[OR:Streptococcus mutans]
[EC:1.2.1.9]
[DE:DEHYDROGENASE)]
[SP:Q59931]
SPX11481148380964319296586.60E-176“[LN:S18599]177
[AC:S18599]
[PN:1,4-alpha-glucan branching enzyme,:glycogen branching enzyme]
[CL:1,4-alpha-glucan branching enzyme]
[OR:Bacillus stearothermophilus]
[EC:2.4.1.18]”
SPX11491149381038111431876.00E-19[LN:CCE277601]105
[AC:AJ277601]
[PN:ADP-glucose pyrophosphorylase]
[GN:glgD]
[OR:Clostridium cellulolyticum]
SPX11501150381138011403244.80E-53[LN:GLGD_BACST]122
[AC:O08327]
[GN:GLGD]
[OR:Bacillus stearothermophilus]
[DE:GLYCOGEN BIOSYNTHESIS PROTEIN GLGD]
[SP:O08327]
SPX11511151381247814348136.80E-159[LN:GLGA_BACSU]101
[AC:P39125]
[GN:GLGA]
[OR:Bacillus subtilis]
[EC:2.4.1.21]
[DE:SYNTHASE)]
[SP:P39125]
SPX1152115238131243722147.80E-24[LN:B69517]97
[AC:B69517]
[PN:phosphoserine phosphatase (serB) homolog]
[OR:Archaeoglobus fulgidus]
SPX1153115338141103302136.30E-24“[LN:A64499]131
[AC:A64499]
[PN:phosphoserine phosphatase,]
[CL:phosphoserine phosphatase]
[OR:Methanococcus jannaschii]
[EC:3.1.3.3]”
SPX115411543815372111616701.30E-226[GI:7380122]125
[LN:NMA5Z2491]
[AC:AL162756:AL157959]
[PN:hypothetical protein NMA1473]
[GN:NMA1473]
[OR:Neisseria meningitidis]
SPX115511553816149447NO-HIT6
SPX115611563817435130521196.30E-286[GI:5263171]148
[LN:AB029313]
[AC:AB029313]
[PN:enolase]
[GN:eno]
[OR:Streptococcus intermedius]
[SR:Streptococcus intermedius (strain:ATCC 27335) DNA]
SPX115711573818156468746.80E-09“[LN:T45116]113
[AC:T45116]
[PN:phosphopyruvate hydratase, [imported]]
[OR:Schizosaccharomyces pombe]
[EC:4.2.1.11]”
SPX11581158381944132752.00E-06[LN:B72477]92
[AC:B72477]
[PN:hypothetical protein APE2459]
[GN:APE2459]
[OR:Aeropyrum pernix]
SPX1159115938201695071743.60E-16[GI:6782411]97
[LN:STH243106]
[AC:AJ243106]
[PN:integrase]
[GN:int]
[OR:Streptococcus thermophilus]
SPX1160116038211133395566.20E-74[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX1161116138221163485731.80E-75[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX116211623823109232763152.90E-101[LN:T30307]75
[AC:T30307]
[PN:rexB protein]
[GN:rexB]
[OR:Lactococcus lactis]
SPX116311633824121736515171.80E-246[LN:T30308]65
[AC:T30308]
[PN:rexA protein]
[OR:Lactococcus lactis]
SPX11641164382579237NO-HIT6
SPX116511653826641922052.00E-24[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX1166116638273931179NO-HIT6
SPX116711673828111333NO-HIT6
SPX1168116838291966589874850[GI:1213494]149
[LN:SPU47687]
[AC:U47687]
[PN:immunoglobulin A1 protease]
[GN:iga]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae strain=R6]
SPX116911693830762281388.00E-12[GI:6911257]115
[LN:AF221126]
[AC:AF221126]
[PN:putative zinc metalloprotease]
[GN:zmpB]
[OR:Streptococcus pneumoniae]
SPX1170117038312848527072.50E-96[LN:F69880]139
[AC:F69880]
[PN:conserved hypothetical protein ylqF]
[GN:ylqF]
[CL:conserved hypothetical protein MG442]
[OR:Bacillus subtilis]
SPX1171117138322607806153.40E-79[LN:C69693]101
[AC:C69693]
[PN:ribonuclease H rnh]
[GN:rnh]
[CL:ribonuclease HII]
[OR:Bacillus subtilis]
SPX11721172383351715512611.40E-51[LN:YADQ_ECOLI]149
[AC:P37019:P77394]
[GN:YADQ]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 46.0 KD PROTEIN IN HEML-PFS INTERGENIC REGION]
[SP:P37019:P77394]
SPX117311733834357107115299.60E-206[GI:3152920]79
[LN:AF065141]
[AC:AF065141]
[PN:unknown]
[OR:Streptococcus mutans]
SPX1174117438353309905776.60E-108[LN:G69830]125
[AC:G69830]
[PN:lipoate-protein ligase homolog yhfJ]
[GN:yhfJ]
[CL:lipoate-protein ligase]
[OR:Bacillus subtilis]
SPX11751175383656817043346.80E-104[LN:I40794]96
[AC:I40794]
[PN:dihydrolipoamide dehydrogenase]
[OR:Clostridium magnum]
[EC:1.8.1.4]
SPX11761176383737611283668.20E-70“[LN:I40793]177
[AC:I40793]
[PN:dihydrolipoamide S-acetyltransferase,]
[CL:dihydrolipoamide acetyltransferase:lipoyl/biotin-binding homology]
[OR:Clostridium magnum]
[EC:2.3.1.12]”
SPX1177117738383319935505.00E-108“[LN:I40791]168
[AC:I40791]
[PN:acetoin dehydrogenase (TPP-dependent), beta chain]
[CL:pyruvate dehydrogenase (lipoamide) beta chain]
[OR:Clostridium magnum]
[EC:1.-.-.-]”
SPX117811783839146438NO-HIT6
SPX1179117938401043121366.90E-13[LN:G72548]92
[AC:G72548]
[PN:hypothetical protein APE1675]
[GN:APE1675]
[OR:Aeropyrum pernix]
SPX1180118038413239695546.20E-107“[LN:I40790]216
[AC:I40790]
[PN:acetoin dehydrogenase (TPP-dependent), alpha chain]
[CL:pyruvate dehydrogenase (lipoamide) alpha chain:thiamin pyrophosphate-binding domain homology]
[OR:Clostridium magnum]
[EC:1.-.-.-]”
SPX11811181384245413624822.40E-117[LN:F69906]140
[AC:F69906]
[PN:conserved hypothetical protein yojI]
[GN:yojI]
[CL:conserved hypothetical protein HI1612]
[OR:Bacillus subtilis]
SPX11821182384387261NO-HIT6
SPX11831183384442312693511.70E-86“[LN:PYRC_LACLE]125
[AC:P48795]
[GN:PYRC]
[OR:Lactobacillus leichmannii]
[EC:3.5.2.3]
[DE:DIHYDROOROTASE, (DHOASE)]
[SP:P48795]”
SPX1184118438451554658457.70E-113“[LN:MUTX_STRPN]144
[AC:P41354]
[GN:MUTX]
[OR:Streptococcus pneumoniae]
[EC:3.6.1.-]
[DE:(8-OXO-DGTPASE), (DGTP PYROPHOSPHOHYDROLASE)]
[SP:P41354]”
SPX11851185384622266611238.50E-151“[LN:UNG_STRPN]127
[AC:P23379]
[GN:UNG]
[OR:Streptococcus pneumoniae]
[EC:3.2.2.-]
[DE:URACIL-DNA GLYCOSYLASE, (UDG)]
[SP:P23379]”
SPX118611863847201603NO-HIT6
SPX1187118738482387142605.40E-57[LN:E69814]153
[AC:E69814]
[PN:conserved hypothetical protein yfnB]
[GN:yfnB]
[CL:Alcaligenes eutrophus phosphoglycolate phosphatase]
[OR:Bacillus subtilis]
SPX11881188384976228661.60E-05[LN:H75623]101
[AC:H75623]
[PN:conserved hypothetical protein]
[GN:DRB0052]
[OR:Deinococcus radiodurans]
SPX11891189385085225564123.10E-104[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX11901190385183024903973.60E-100[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX119111913852411123317634.80E-237[GI:4958916]169
[LN:AB027569]
[AC:AB027569]
[PN:phosphoenolpyruvate-protein phosphotransferase]
[GN:ptsI]
[OR:Streptococcus bovis]
[SR:Streptococcus bovis (strain:JB1) DNA]
SPX119211923853461381441.50E-15[LN:YKXH_BACSU]132
[AC:P08876]
[GN:YKXH]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 7.4 KD PROTEIN IN PTSX OPERON (PROTEIN K)]
[SP:P08876]
SPX119311933854882644022.30E-50[LN:PTHP_STRMU]138
[AC:P45596]
[GN:PTSH]
[OR:Streptococcus mutans]
[DE:PHOSPHOCARRIER PROTEIN HPR (HISTIDINE-CONTAINING PROTEIN)]
[SP:P45596]
SPX119411943855732192331.50E-27“[LN:NRDH_LACLC]154
[AC:Q48708]
[GN:NRDH]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[DE:GLUTAREDOXIN-LIKE PROTEIN NRDH]
[SP:Q48708]”
SPX119511953856720216010422.20E-255[GI:3077613]125
[LN:CANRDFGEN]
[AC:Y09572]
[PN:ribonucleotide reductase subunit R1E]
[GN:nrdE]
[OR:Corynebacterium ammoniagenes]
SPX11961196385763189NO-HIT6
SPX1197119738583219638182.90E-116[GI:3068719]132
[LN:AF050168]
[AC:AF050168]
[PN:ribonucleoside diphosphate reductase small]
[GN:nrdF]
[OR:Corynebacterium ammoniagenes]
SPX1198119838592547623712.50E-80“[LN:LACR_LACLA]163
[AC:P18816]
[GN:LACR]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:LACTOSE PHOSPHOTRANSFERASE SYSTEM REPRESSOR]
[SP:P18816]”
SPX11991199386084252NO-HIT6
SPX120012003861472141624520“[LN:LACG_LACLA]180
[AC:P11546]
[GN:LACG]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:3.2.1.85]
[DE:GALACTOHYDROLASE) (PGALASE) (P-BETA-GAL) (PBG)]
[SP:P11546]”
SPX120112013862565169516284.50E-299“[LN:PTLB_LACLA]157
[AC:P23531]
[GN:LACE]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EII-LAC)]
[SP:P23531]”
SPX1202120238631063184542.90E-58“[LN:PTLA_LACLA]158
[AC:P23532]
[GN:LACF]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EIII-LAC)]
[SP:P23532]”
SPX1203120338642798374871.40E-75[LN:LACT_LACCA]113
[AC:P24401]
[GN:LACT]
[OR:Lactobacillus casei]
[DE:TRANSCRIPTION ANTITERMINATOR LACT]
[SP:P24401]
SPX12041204386527081012321.10E-164“[LN:LACD_LACLA]182
[AC:P26593]
[GN:LACD]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.2.40]
[DE:ALDOLASE) (D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE)]
[SP:P26593]”
SPX1205120538662738198109.10E-118“[LN:LACC_LACLA]185
[AC:P23391]
[GN:LACC]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.1.144]
[DE:TAGATOSE-6-PHOSPHATE KINASE, (PHOSPHOTAGATOKINASE)]
[SP:P23391]”
SPX120612063867163489NO-HIT6
SPX1207120738681725168105.00E-108“[LN:LACB_LACLA]179
[AC:P23495]
[GN:LACB]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:5.3.1.26]
[DE:GALACTOSE-6-PHOSPHATE ISOMERASE LACB SUBUNIT,]
[SP:P23495]”
SPX1208120838691424266122.90E-80“[LN:LACA_LACLA]179
[AC:P23494]
[GN:LACA]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:5.3.1.26]
[DE:GALACTOSE-6-PHOSPHATE ISOMERASE LACA SUBUNIT,]
[SP:P23494]”
SPX12091209387097291570.00024[GI:712785]72
[LN:S74218]
[AC:S74218]
[GN:E9]
[OR:reindeer papillomavirus]
SPX1210121038711594775071.70E-65“[LN:LAXP_LACLA]141
[AC:P23496]
[GN:LACX]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:LACX PROTEIN, PLASMID]
[SP:P23496]”””
SPX1211121138722076213741.20E-65[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX1212121238731073211934.90E-21[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX121312133874101303NO-HIT6
SPX121412143875148444881.30E-10“[GI:4512375]181
[LN:AB011837]
[AC:AB011837]
[PN:phosphotransferase system (PTS)]
[GN:fruA]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”
SPX121512153876431129321592.90E-302[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX121612163877631891202.10E-12[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX121712173878417125113952.00E-200“[LN:THD1_LACLA]144
[AC:Q02145]
[GN:ILVA]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.2.1.16]
[DE:DEAMINASE)]
[SP:Q02145]”
SPX121812183879119357NO-HIT6
SPX12191219388078234NO-HIT6
SPX12201220388189267NO-HIT6
SPX122112213882341102313299.50E-179“[LN:ILVC_LACLA]199
[AC:Q02138]
[GN:ILVC]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:1.1.1.86]
[DE:ISOMEROREDUCTASE) (ALPHA-KETO-BETA-HYDROXYLACIL REDUCTOISOMERASE)]
[SP:Q02138]”
SPX1222122238831675014774.10E-62“[LN:ILVN_LACLA]182
[AC:Q02140]
[GN:ILVN]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.3.18]
[DE:(ACETOHYDROXY-ACID SYNTHASE SMALL SUBUNIT) (ALS)]
[SP:Q02140]”
SPX122312233884567170112072.30E-266“““[LN:ILVB_LACLA]182
[AC:Q02137]
[GN:ILVB]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.3.18]
[DE:(ACETOHYDROXY-ACID SYNTHASE LARGE SUBUNIT) (ALS)]
[SP:Q02137]”
SPX12241224388567920375657.80E-167[LN:E69879]151
[AC:E69879]
[PN:conserved hypothetical protein yloV]
[GN:yloV]
[CL:Mycoplasma genitalium hypothetical protein MG369]
[OR:Bacillus subtilis]
SPX122512253886631892224.40E-26[LN:RL28_BACSU]103
[AC:P37807]
[GN:RPMB]
[OR:Bacillus subtilis]
[DE:50S RIBOSOMAL PROTEIN L28]
[SP:P37807]
SPX122612263887822461235.10E-19[GI:6760462]100
[LN:AF224467]
[AC:AF224467]
[PN:putative glycosyl transferase]
[OR:Haemophilus ducreyi]
SPX122712273888661981578.80E-16[GI:6760462]100
[LN:AF224467]
[AC:AF224467]
[PN:putative glycosyl transferase]
[OR:Haemophilus ducreyi]
SPX12281228388951515457712.70E-216[GI:3256222]110
[LN:SAY14370]
[AC:Y14370]
[PN:peptide chain release factor 3]
[GN:RF3]
[OR:Staphylococcus aureus]
SPX1229122938901013031904.90E-21[LN:A69795]145
[AC:A69795]
[PN:conserved hypothetical protein yerL]
[GN:yerL]
[CL:probable glu-tRNA amidotransferase C chain]
[OR:Bacillus subtilis]
SPX123012303891489146713331.60E-186[LN:B69795]113
[AC:B69795]
[PN:amidase homolog yerM]
[GN:yerM]
[CL:indoleacetamide hydrolase]
[OR:Bacillus subtilis]
SPX1231123138922136394144.30E-94[LN:T44293]110
[AC:T44293]
[PN:hypothetical protein yerN [imported]]
[CL:PET112 protein]
[OR:Bacillus halodurans]
SPX1232123238932698077444.60E-97[LN:C69795]114
[AC:C69795]
[PN:pet112-like protein homolog yerN]
[GN:yerN]
[CL:PET112 protein]
[OR:Bacillus subtilis]
SPX12331233389434810447191.70E-145“[LN:H69789]216
[AC:H69789]
[PN:L-iditol 2-dehydrogenase, homolog ydjL:sorbitol dehydrogenase homolog]
[GN:ydjL]
[CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology]
[OR:Bacillus subtilis]
[EC:1.1.1.14]”
SPX123412343895672011384.80E-14[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX1235123538961875614307.10E-54[LN:EFP_BACSU]102
[AC:P49778]
[GN:EFP]
[OR:Bacillus subtilis]
[DE:ELONGATION FACTOR P (EF-P)]
[SP:P49778]
SPX1236123638971303901398.30E-19[LN:YQHY_BACSU]137
[AC:P54519]
[GN:YQHY]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 14.7 KD PROTEIN IN ACCC-FOLD INTERGENIC REGION]
[SP:P54519]
SPX1237123738981414231051.00E-12[GI:6580774]137
[LN:AF088897]
[AC:AF088897:AF034613:AF086792:U63733]
[PN:N-utilization substance protein B]
[GN:nusB]
[OR:Zymomonas mobilis]
SPX1238123838991905709487.40E-131[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX12391239390026178310751.10E-148[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX124012403901278834809.90E-07[LN:E69787]87
[AC:E69787]
[PN:hypothetical protein ydiL]
[GN:ydiL]
[OR:Bacillus subtilis]
SPX12411241390284252NO-HIT6
SPX1242124239032567686534.10E-90[GI:285621]155
[LN:BACPK]
[AC:D13095]
[PN:undefined open reading frame]
[OR:Bacillus stearothermophilus]
[SR:Bacillus stearothermophilus (strain:NCA1503) DNA]
SPX1243124339042888646022.20E-92“[LN:ACCD_SYNP7]168
[AC:Q54776]
[GN:ACCD]
[OR:Synechococcus sp]
[SR:,strain PCC 7942:Anacystis nidulans R2]
[EC:6.4.1.2]
[DE:(EC 6.4.1.2) (ACCASE BETA CHAIN)]
[SP:Q54776]”
SPX124412443905456136811011.50E-181[LN:A69581]170
[AC:A69581]
[PN:acetyl-CoA carboxylase (biotin carboxylase subunit) accC]
[GN:accC]
[CL:biotin carboxylase:biotin carboxylase homology]
[OR:Bacillus subtilis]
SPX1245124539061414232991.60E-49“[LN:D70065]201
[AC:D70065]
[PN:(3R)-hydroxymyristoyl-[acyl carrier protein]
dehydratase, ywpB]
[GN:ywpB]
[CL:(3R)-hydroxymyristoyl-[acyl carrier protein]
dehydratase]
[OR:Bacillus subtilis]
[EC:4.2.1.-]”
SPX1246124639071624862481.10E-34“[LN:C75558]195
[AC:C75558]
[PN:acetyl-CoA carboxylase, bitoin carboxyl carrier protein]
[GN:DR0118]
[CL:biotin carboxyl carrier protein:lipoyl/biotin-binding homology]
[OR:Deinococcus radiodurans]”
SPX124712473908932791341.30E-13[LN:FAB2_MYCTU]152
[AC:Q10525]
[GN:RV2246:MTCY427.27]
[OR:Mycobacterium tuberculosis]
[EC:2.3.1.41]
[DE:(BETA-KETOACYL-ACP SYNTHASE 2) (KAS 2)]
[SP:Q10525]
SPX12481248390936010804772.60E-113“[LN:S77464]237
[AC:S77464]
[PN:3-oxoacyl-[acyl-carrier-protein]
synthase, beta chain:beta ketoacyl-acyl carrier protein synthase:protein sll1069:beta ketoacyl-acyl carrier protein synthase:protein sll1069]
[GN:fabF]
[OR:Synechocystis sp.]”
SPX1249124939102447324822.10E-76[LN:FABG_CUPLA]138
[AC:P28643]
[GN:CLKR27]
[OR:Cuphea lanceolata]
[EC:1.1.1.100]
[DE:(3-KETOACYL-ACYL CARRIER PROTEIN REDUCTASE)]
[SP:P28643]
SPX12501250391174222819.50E-05[LN:H72482]92
[AC:H72482]
[PN:hypothetical protein APE2504]
[GN:APE2504]
[OR:Aeropyrum pernix]
SPX1251125139123079213741.00E-85“[LN:B41856]249
[AC:B41856:A42147:S20443:A64853]
[PN:[acyl-carrier-protein]
S-malonyltransferase,]
[GN:fabD:tfpA]
[CL:[acyl-carrier-protein]
S-malonyltransferase:[acyl-carrier-protein]
S-malonyltransferase homology]
[OR:Escherichia coli]
[EC:2.3.1.39]”
SPX1252125239133259756815.90E-101[LN:A72335]96
[AC:A72335]
[PN:conserved hypothetical protein]
[GN:TM0800]
[OR:Thermotoga maritima]
SPX12531253391475225801.80E-12[LN:ACP_BACSU]122
[AC:P80643:P51832]
[GN:ACPA:ACPP]
[OR:Bacillus subtilis]
[DE:ACYL CARRIER PROTEIN (ACP)]
[SP:P80643:P51832]
SPX1254125439151895672026.90E-38“[LN:S75457]236
[AC:S75457]
[PN:beta-ketoacyl-acyl carrier protein synthase III:protein slr1511:protein slr1511]
[GN:fabH]
[CL:3-oxoacyl-[acyl-carrier-protein]
synthase III]
[OR:Synechocystis sp.]
[SR:PCC 6803, , PCC 6803]
[SR:PCC 6803, ]”
SPX1255125539161404202691.30E-46[GI:7416010]177
[LN:AB025973]
[AC:AB025973]
[PN:3-oxoacyl-[acyl-carrier-protein]
synthase III]
[GN:accS]
[OR:Lactobacillus plantarum]
[SR:Lactobacillus plantarum (strain:L137) DNA]
SPX12561256391766198NO-HIT6
SPX1257125739181454351395.00E-12[GI:4139249]84
[LN:AF110185]
[AC:AF110185]
[PN:unknown]
[OR:Burkholderia pseudomallei]
SPX12581258391966198NO-HIT6
SPX125912593920982941387.10E-13[GI:3253198]91
[LN:AF029714]
[AC:AF029714:Z71175]
[PN:PhaB]
[GN:phaB]
[OR:Pseudomonas putida]
SPX126012603921762281569.00E-18[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX126112613922455136512406.10E-166[LN:A69763]147
[AC:A69763]
[PN:homoserine dehydrogenase homolog yclM]
[GN:yclM]
[CL:aspartate kinase:aspartate kinase homology]
[OR:Bacillus subtilis]
SPX1262126239231243724932.80E-64[GI:5669858]93
[LN:AF130465]
[AC:AF130465]
[PN:unknown]
[GN:manO]
[OR:Streptococcus salivarius]
SPX12631263392437511255648.90E-141“[LN:SYS_BACSU]145
[AC:P37464]
[GN:SERS]
[OR:Bacillus subtilis]
[EC:6.1.1.11]
[DE:SERYL-TRNA SYNTHETASE, (SERINE--TRNA LIGASE) (SERRS)]
[SP:P37464]”
SPX126412643925912731016.30E-08“[LN:SYS_MYCGE]155
[AC:P47251]
[GN:SERS:MG005]
[OR:Mycoplasma genitalium]
[EC:6.1.1.11]
[DE:SERYL-TRNA SYNTHETASE, (SERINE--TRNA LIGASE) (SERRS)]
[SP:P47251]”
SPX126512653926304912NO-HIT6
SPX12661266392769207NO-HIT6
SPX1267126739281835492172.40E-57[GI:7379894]125
[LN:NMA4Z2491]
[AC:AL162755:AL157959]
[PN:hypothetical protein NMA1203]
[GN:NMA1203]
[OR:Neisseria meningitidis]
SPX12681268392944113236116.80E-118“[LN:D71327]210
[AC:D71327]
[PN:probable D-alanine glycine permease (dagA)]
[GN:TP0414]
[CL:sodium-dependent D-alanine/glycine transport protein]
[OR:Treponema pallidum subsp. pallidum]
[SR:, syphilis spirochete]”
SPX12691269393077923376715.70E-155[LN:MUS2_BACSU]92
[AC:P94545]
[GN:MUTS2]
[OR:Bacillus subtilis]
[DE:MUTS2 PROTEIN]
[SP:P94545]
SPX1270127039312517531757.10E-43[GI:6746427]90
[LN:AF179847]
[AC:AF179847]
[PN:putative transposase]
[OR:Lactococcus lactis]
SPX12711271393265195NO-HIT6
SPX1272127239331825461071.20E-15[GI:3849798]118
[LN:U91581]
[AC:U91581:U04057]
[PN:putative transposase]
[GN:tpase]
[OR:Lactococcus lactis subsp. lactis]
SPX127312733934183549954.30E-13[LN:B69985]87
[AC:B69985]
[PN:hypothetical protein yshB]
[GN:yshB]
[OR:Bacillus subtilis]
SPX127412743935104312NO-HIT6
SPX12751275393629488214448.00E-194“[LN:RNH2_STRPN]130
[AC:O07874]
[GN:RNHB]
[OR:Streptococcus pneumoniae]
[EC:3.1.26.4]
[DE:RIBONUCLEASE HII, (RNASE HII)]
[SP:O07874]”
SPX12761276393720561510656.70E-145“[LN:LEP_STRPN]155
[AC:O07344]
[GN:LEPB:SPI]
[OR:Streptococcus pneumoniae]
[EC:3.4.21.89]
[DE:SIGNAL PEPTIDASE I, (SPASE I) (LEADER PEPTIDASE I)]
[SP:O07344]”
SPX12771277393893279NO-HIT6
SPX12781278393978923677385.80E-165[LN:A69979]103
[AC:A69979]
[PN:conjugation transfer protein homolog yrrC]
[GN:yrrC]
[OR:Bacillus subtilis]
SPX127912793940428128416911.40E-223[GI:3549287]88
[LN:AF073922]
[AC:AF073922]
[PN:RopA]
[GN:ropA]
[OR:Streptococcus pyogenes]
SPX128012803941379113713502.20E-182“[LN:MTLD_STRMU]134
[AC:Q02418]
[GN:MTLD]
[OR:Streptococcus mutans]
[EC:1.1.1.17]
[DE:MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE,]
[SP:Q02418]”
SPX1281128139421464385445.30E-71[LN:PTMA_STRMU]119
[AC:Q02420]
[GN:MTLF]
[OR:Streptococcus mutans]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EIII-MTL)]
[SP:Q02420]
SPX12821282394365219563921.00E-47[LN:YMTF_STRMU]126
[AC:Q02425]
[OR:Streptococcus mutans]
[DE:HYPOTHETICAL PROTEIN IN MTLF 5′REGION (ORFX) (FRAGMENT)]
[SP:Q02425]
SPX128312833944596178810994.90E-194[LN:PTMB_BACST]125
[AC:P50852]
[GN:MTLA]
[OR:Bacillus stearothermophilus]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EII-MTL)]
[SP:P50852]
SPX12841284394567201NO-HIT6
SPX1285128539461915734222.30E-53[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX1286128639472788345821.50E-140[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX128712873948341102311425.00E-219[GI:1914875]101
[LN:SPZ82002]
[AC:Z82002]
[PN:PCPC]
[GN:pcpC]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX128812883949982941943.40E-25[GI:4586910]161
[LN:AB017447]
[AC:AB017447]
[PN:protective antigen SpaA.1]
[OR:Erysipelothrix rhusiopathiae]
[SR:Erysipelothrix rhusiopathiae (strain:Fujisawa) DNA]
SPX1289128939502196571041.50E-08[LN:S25140]119
[AC:S25140]
[PN:serine proteinase homolog]
[CL:staphylococcal serine proteinase]
[OR:Enterococcus faecalis]
SPX129012903951802402968.20E-35[GI:1914874]81
[LN:SPZ82002]
[AC:Z82002]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX129112913952912731463.20E-14[GI:4584089]155
[LN:BAJ10128]
[AC:AJ010128]
[PN:DNA alkylation repair enzyme]
[GN:alkD]
[FN:complements DNA alkylation repair deficiency]
[OR:Bacillus cereus]
SPX129212923953852551022.90E-08[GI:4584089]155
[LN:BAJ10128]
[AC:AJ010128]
[PN:DNA alkylation repair enzyme]
[GN:alkD]
[FN:complements DNA alkylation repair deficiency]
[OR:Bacillus cereus]
SPX12931293395421163310401.50E-139[GI:5830527]104
[LN:SPAJ6393]
[AC:AJ006393]
[PN:response regulator]
[GN:rr03]
[OR:Streptococcus pneumoniae]
SPX12941294395533299616033.60E-220[GI:5830526]102
[LN:SPAJ6393]
[AC:AJ006393]
[PN:histidine kinase]
[GN:hk03]
[OR:Streptococcus pneumoniae]
SPX1295129539562336991041.50E-11[LN:G70045]87
[AC:G70045]
[PN:hypothetical protein yvqF]
[GN:yvqF]
[OR:Bacillus subtilis]
SPX12961296395733710111516.20E-42[LN:D75084]162
[AC:D75084]
[PN:carotenoid biosynthetic gene erwcrts related PAB1662]
[GN:PAB1662]
[CL:carotenoid biosynthesis protein homolog]
[OR:Pyrococcus abyssi]
SPX1297129739583361008670.00053“[LN:KIME_METJA]126
[AC:Q58487]
[GN:MJ1087]
[OR:Methanococcus jannaschii]
[EC:2.7.1.36]
[DE:MEVALONATE KINASE, (MK)]
[SP:Q58487]”
SPX12981298395934510351415.90E-28[GI:6625790]116
[LN:AF203779]
[AC:AF203779]
[PN:diphosphomevalonate decarboxylase MVD1]
[GN:MVD1]
[OR:Candida albicans]
SPX1299129939602938791341.60E-20[LN:F72474]98
[AC:F72474]
[PN:probable mevalonate kinase APE2439]
[GN:APE2439]
[OR:Aeropyrum pernix]
SPX1300130039611103301938.50E-21[GI:1914875]101
[LN:SPZ82002]
[AC:Z82002]
[PN:PCPC]
[GN:pcpC]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX130113013962292876NO-HIT6
SPX1302130239634111233974.90E-10[GI:3582221]114
[LN:AE001272]
[AC:AE001272]
[PN:conserved hypothetical protein]
[GN:ORF00049]
[OR:Lactococcus lactis]
SPX1303130339643339994021.50E-124[GI:1914875]101
[LN:SPZ82002]
[AC:Z82002]
[PN:PCPC]
[GN:pcpC]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX13041304396537111132891.70E-89[GI:1914875]101
[LN:SPZ82002]
[AC:Z82002]
[PN:PCPC]
[GN:pcpC]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX1305130539662306902127.30E-56[GI:3599371]139
[LN:AF082668]
[AC:AF082668]
[PN:CsrR]
[GN:csrR]
[FN:negative regulator of hyaluronic acid capsule]
[OR:Streptococcus pyogenes]
SPX13061306396745813748015.10E-226[GI:3033358]100
[LN:LLU74322]
[AC:U74322]
[PN:6-phosphogluconate dehydrogenase]
[OR:Lactococcus lactis]
SPX13071307396846513951091.10E-06[GI:1684847]78
[LN:HSU77718]
[AC:U77718]
[PN:pinin]
[OR:Homo sapiens]
[SR:human]
SPX13081308396938611586781.20E-133[LN:YPSC_BACSU]147
[AC:P50840]
[GN:YPSC]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 43.5 KD PROTEIN IN COTD-KDUD INTERGENIC REGION PRECURSOR]
[SP:P50840]
SPX1309130939701103301666.70E-18[LN:YPSB_BACSU]137
[AC:P50839]
[GN:YPSB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 11.6 KD PROTEIN IN COTD-KDUD INTERGENIC REGION]
[SP:P50839]
SPX1310131039711765281478.20E-19[LN:YPSA_BACSU]137
[AC:P50838]
[GN:YPSA]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 21.1 KD PROTEIN IN COTD-KDUD INTERGENIC REGION]
[SP:P50838]
SPX13111311397219959710433.40E-141[LN:YPOA_STRPN]120
[AC:P38034]
[OR:Streptococcus pneumoniae]
[DE:HYPOTHETICAL 23.1 KD PROTEIN IN PONA 5′REGION]
[SP:P38034]
SPX131213123973720216037340[GI:6563337]116
[LN:AF210745]
[AC:AF210745]
[PN:penicillin-binding protein 1A]
[GN:pbp1a]
[OR:Streptococcus pneumoniae]
SPX13131313397468204NO-HIT6
SPX1314131439751768530417629.10E-232[GI:1658320]77
[LN:SPDEXCAP]
[AC:Z47210]
[GN:orf]
[OR:Streptococcus pneumoniae]
SPX131513153976661198333780LN:ALIA_STRPN]201
[AC:P35592:Q54782:O54620:O52228]
[GN:ALIA:EXP1:PLPA]
[OR:Streptococcus pneumoniae]
[DE:OLIGOPEPTIDE-BINDING PROTEIN ALIA PRECURSOR (EXPORTED PROTEIN 1)]
[SP:P35592:Q54782:O54620:O52228]
SPX13161316397778234870.00034“[GI:5824139]137
[LN:POL245436]
[AC:AJ245436:J04618:J04619:S50571:X52935:X65936]
[PN:hypothetical protein, 57.8 kD]
[OR:Pseudomonas putida]”
SPX131713173978150450943.20E-15“[LN:Y4HP_RHISN]128
[AC:P50360]
[GN:Y4HP]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP]
[SP:P50360]”
SPX13181318397958174NO-HIT6
SPX13191319398086258808.90E-06“[LN:Y4HP_RHISN]128
[AC:P50360]
[GN:Y4HP]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:HYPOTHETICAL 61.7 KD PROTEIN Y4HP]
[SP:P50360]”
SPX132013203981143429849.20E-08“[GI:6009407]140
[LN:AB024946]
[AC:AB024946]
[GN:orf31]
[OR:Escherichia coli]
[SR:Escherichia coli (sub_species:enteropathogenic, strain:B171]”
SPX13211321398228485214801.00E-198[GI:2804705]110
[LN:AF030362]
[AC:AF030362]
[PN:dTDP-L-rhamnose synthase]
[GN:cpsO]
[OR:Streptococcus pneumoniae]
SPX132213223983350105018532.90E-249[GI:4200435]92
[LN:AF026471]
[AC:AF026471]
[PN:Cps2N]
[GN:cps2N]
[OR:Streptococcus pneumoniae]
SPX13231323398419959710274.50E-137“[GI:3907611]131
[LN:AF094575]
[AC:AF094575]
[PN:dTDP-4-keto-6-deoxyglucose-3,5-epimerase]
[GN:cps19aM]
[OR:Streptococcus pneumoniae]”
SPX13241324398529087014307.20E-193[GI:4406249]131
[LN:AF105113]
[AC:AF105113]
[PN:glucose-1-phosphate thymidylyl transferase]
[GN:cps19AL]
[OR:Streptococcus pneumoniae]
SPX132513253986476142820173.10E-287[GI:3907608]129
[LN:AF094575]
[AC:AF094575]
[PN:putative repeat unit transporter Cps19aJ]
[GN:cps19aJ]
[OR:Streptococcus pneumoniae]
SPX13261326398795285NO-HIT6
SPX13271327398844813441486.90E-31[GI:3907607]122
[LN:AF094575]
[AC:AF094575]
[PN:polysaccharide polymerase Cps19aI]
[GN:cps19aI]
[OR:Streptococcus pneumoniae]
SPX1328132839893299871782.00E-31[LN:T00087]86
[AC:T00087]
[PN:rhamnosyltransferase]
[GN:rgpBc]
[OR:Streptococcus mutans]
SPX132913293990242726931.90E-06[LN:T35395]92
[AC:T35395]
[PN:probable transferase]
[GN:SC6A5.04]
[OR:Streptomyces coelicolor]
SPX1330133039911865581543.00E-14[GI:2209209]96
[LN:AF004325]
[AC:AF004325]
[PN:unknown]
[GN:cps19bG]
[OR:Streptococcus pneumoniae]
SPX133113313992315945966.50E-16[GI:3132871]104
[LN:AF019375]
[AC:AF019375]
[PN:UDP-glucose:(glucosyl) LPS]
[GN:waaR]
[OR:Escherichia coli]
SPX133213323993456136811410[GI:3907603]129
[LN:AF094575]
[AC:AF094575]
[PN:glucosyl-1-phosphate transferase Cps19aE]
[GN:cps19aE]
[OR:Streptococcus pneumoniae]
SPX13331333399422768110554.60E-145[GI:3907602]136
[LN:AF094575]
[AC:AF094575]
[PN:Cps19aD]
[GN:cps19aD]
[FN:chain length regulation and export]
[OR:Streptococcus pneumoniae]
SPX13341334399523269610612.00E-141[GI:3907601]136
[LN:AF094575]
[AC:AF094575]
[PN:Cps19aC]
[GN:cps19aC]
[FN:chain length regulation and export]
[OR:Streptococcus pneumoniae]
SPX13351335399626078011952.90E-162[GI:3907600]96
[LN:AF094575]
[AC:AF094575]
[PN:Cps19aB]
[GN:cps19aB]
[OR:Streptococcus pneumoniae]
SPX133613363997485145522380[GI:3550627]83
[LN:SPAJ6986]
[AC:AJ006986]
[GN:cap33fA]
[OR:Streptococcus pneumoniae]
SPX133713373998358107416909.20E-228[LN:TRA2_STRPN]116
[AC:Q54513]
[OR:Streptococcus pneumoniae]
[DE:TRANSPOSASE FOR INSERTION SEQUENCE IS1202]
[SP:Q54513]
SPX1338133839991203605816.60E-75[LN:TRA2_STRPN]116
[AC:Q54513]
[OR:Streptococcus pneumoniae]
[DE:TRANSPOSASE FOR INSERTION SEQUENCE IS1202]
[SP:Q54513]
SPX1339133940003179512673.80E-61“““[GI:6332767]194
[LN:AB033763]
[AC:AB033763:AB014419:AB014429:AB014439]
[PN:hypothetical protein]
[OR:Staphylococcus aureus]
[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”””
SPX1340134040011795375511.10E-70[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX1341134140021614835502.00E-80[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX1342134240032788345871.60E-140[LN:A33595]107
[AC:A33595:A30868]
[PN:probable transposase]
[CL:transposase IS3]
[OR:Streptococcus agalactiae]
SPX134313434004537161124990“[GI:3320387]110
[LN:AF030373]
[AC:AF030373]
[PN:alpha, 1-6-glucosidase]
[GN:dexB]
[OR:Streptococcus pneumoniae]”
SPX1344134440054951485NO-HIT6
SPX1345134540061614832889.40E-46[LN:D75280]143
[AC:D75280]
[PN:conserved hypothetical protein]
[GN:DR2387]
[CL:conserved hypothetical protein HI0491]
[OR:Deinococcus radiodurans]
SPX134613464007702210620490[GI:871784]147
[LN:BOVCLPAB]
[AC:L34677]
[PN:Clp-like ATP-dependent protease binding subunit]
[OR:Bos taurus]
[SR:Bos taurus calf thymus cDNA to mRNA]
SPX13471347400880240NO-HIT6
SPX13481348400932798116198.40E-229[GI:4009489]132
[LN:AF068903]
[AC:AF068903]
[PN:undecaprenyl-phosphate-UDP-MurNAc-pentapeptide]
[GN:mraY]
[OR:Streptococcus pneumoniae]
SPX134913494010751225338120[LN:PBPX_STRPN]131
[AC:P14677]
[GN:PBPX]
[OR:Streptococcus pneumoniae]
[DE:PENICILLIN-BINDING PROTEIN 2X (PBP-2X) (PBP2X)]
[SP:P14677]
SPX1350135040111063185051.40E-65[GI:4009487]90
[LN:AF068903]
[AC:AF068903]
[PN:YllD]
[GN:yllD]
[OR:Streptococcus pneumoniae]
SPX13511351401231795116042.70E-217[GI:4009486]90
[LN:AF068903]
[AC:AF068903]
[PN:YllC]
[GN:yllC]
[OR:Streptococcus pneumoniae]
SPX135213524013651953231.20E-40[GI:1536960]115
[LN:SOORFS]
[AC:Z79691]
[GN:yorfE]
[FN:putative transcription regulator]
[OR:Streptococcus pneumoniae]
SPX1353135340141424262911.40E-36[GI:1524349]87
[LN:SOORFS]
[AC:Z79691]
[PN:OrfC]
[GN:yorfC]
[OR:Streptococcus pneumoniae]
SPX13541354401594282NO-HIT6
SPX135513554016852551785.70E-20[GI:1536959]87
[LN:SOORFS]
[AC:Z79691]
[PN:OrfB]
[GN:yorfb]
[OR:Streptococcus pneumoniae]
SPX135613564017812433912.00E-51[GI:1536959]87
[LN:SOORFS]
[AC:Z79691]
[PN:OrfB]
[GN:yorfb]
[OR:Streptococcus pneumoniae]
SPX1357135740181123362194.90E-27[GI:1536959]87
[LN:SOORFS]
[AC:Z79691]
[PN:OrfB]
[GN:yorfb]
[OR:Streptococcus pneumoniae]
SPX135813584019641921114.30E-10[GI:1536959]87
[LN:SOORFS]
[AC:Z79691]
[PN:OrfB]
[GN:yorfb]
[OR:Streptococcus pneumoniae]
SPX135913594020334100217032.00E-229“[GI:1536958]139
[LN:SOORFS]
[AC:Z79691]
[PN:RegR]
[GN:regR]
[FN:putative transcription regulator, member GalR]
[OR:Streptococcus pneumoniae]”
SPX136013604021634190210943.90E-148[GI:1524347]87
[LN:SOORFS]
[AC:Z79691]
[PN:OrfA]
[GN:yorfA]
[OR:Streptococcus pneumoniae]
SPX13611361402298294967.80E-07[LN:D70408]120
[AC:D70408]
[PN:conserved hypothetical protein aq_1254]
[GN:aq_1254]
[CL:yajC protein]
[OR:Aquifex aeolicus]
SPX1362136240232738192683.50E-51“[LN:PTPD_ECOLI]102
[AC:P42911]
[GN:AGAD]
[OR:Escherichia coli]
[DE:ENZYME II, D COMPONENT)]
[SP:P42911]”
SPX1363136340242607801704.30E-27[GI:1732200]115
[LN:VFU65015]
[AC:U65015]
[PN:PTS permease for mannose subunit IIPMan]
[GN:manY]
[OR:Vibrio furnissii]
SPX1364136440251644922863.40E-44“[LN:PTPV_ECOLI]133
[AC:P42904:P76669]
[GN:AGAV]
[OR:Escherichia coli]
[EC:2.7.1.69]
[DE:ENZYME II, B COMPONENT 2),]
[SP:P42904:P76669]”
SPX13651365402633610084752.70E-95[GI:5869507]148
[LN:AB019619]
[AC:AB019619]
[PN:unsaturated glucuronyl hydrolase]
[GN:ugl]
[OR:Bacillus sp. GL1]
[SR:Bacillus sp. GL1 (strain:GL1) DNA]
SPX136613664027146438NO-HIT6
SPX1367136740281454351293.30E-17[GI:5669855]128
[LN:AF130465]
[AC:AF130465]
[PN:mannose-specific phosphotransferase system]
[GN:manL]
[OR:Streptococcus salivarius]
SPX1368136840292186544361.40E-55[LN:YJGU_ECOLI]102
[AC:P39345]
[GN:YJGU]
[OR:Escherichia coli]
[EC:1.-.-.-]
[DE:(EC 1.-.-.-)]
[SP:P39345]
SPX136913694030125375NO-HIT6
SPX137013704031982941692.50E-19[LN:YJGU_ECOLI]102
[AC:P39345]
[GN:YJGU]
[OR:Escherichia coli]
[EC:1.-.-.-]
[DE:(EC 1.-.-.-)]
[SP:P39345]
SPX137113714032214642NO-HIT6
SPX13721372403333410023171.00E-46[LN:G72422]112
[AC:G72422]
[PN:2-keto-3-deoxygluconate kinase]
[GN:TM0067]
[CL:ribokinase]
[OR:Thermotoga maritima]
SPX1373137340342106302716.10E-46[LN:F72422]190
[AC:F72422]
[PN:2-dehydro-3-deoxyphosphogluconate aldolase/4-hydroxy-2-oxoglutarate aldolase]
[GN:TM0066]
[CL:2-dehydro-3-deoxyphosphogluconate aldolase]
[OR:Thermotoga maritima]
SPX1374137440351183542641.50E-50[GI:1841332]178
[LN:D64071]
[AC:D64071]
[PN:putative protein of unknown function]
[OR:Actinobacillus actinomycetemcomitans]
[SR:Actinobacillus actinomycetemcomitans (strain:Y4) DNA]
SPX1375137540361079323748630“[LN:HYSA_STRPN]156
[AC:Q54873:Q54874]
[OR:Streptococcus pneumoniae]
[EC:4.2.2.1]
[DE:HYALURONATE LYASE PRECURSOR, (HYALURONIDASE) (HYASE)]
[SP:Q54873:Q54874]”
SPX1376137640371594774821.90E-62[GI:2598550]100
[LN:LLAJ109]
[AC:AJ000109]
[PN:gluthatione peroxidase]
[GN:gpo]
[OR:Lactococcus lactis]
SPX13771377403873822141814.50E-33[GI:6686567]120
[LN:AAC252161]
[AC:AJ252161]
[PN:putative alpha-glucosidase]
[GN:glcA]
[OR:Alicyclobacillus acidocaldarius]
SPX13781378403961183NO-HIT6
SPX13791379404044913472313.40E-63“[LN:PTCC_BACST]157
[AC:Q45400]
[GN:CELB]
[OR:Bacillus stearothermophilus]
[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]
[SP:Q45400]”
SPX138013804041169507NO-HIT6
SPX1381138140421053152342.00E-27[LN:PTCA_BACSU]121
[AC:P46319]
[GN:CELC:LICA]
[OR:Bacillus subtilis]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EIII-CEL)]
[SP:P46319]
SPX13821382404366019801389.20E-51[LN:CELR_BACSU]112
[AC:P46321]
[GN:CELR:LICR]
[OR:Bacillus subtilis]
[DE:PUTATIVE CEL OPERON REGULATOR]
[SP:P46321]
SPX138313834044114342842.40E-08[LN:PTCB_BACST]115
[AC:Q45399]
[GN:CELA]
[OR:Bacillus stearothermophilus]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69)]
[SP:Q45399]
SPX138413844045802401421.20E-15[LN:Y110_METJA]114
[AC:Q57574]
[GN:MJ0110]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL PROTEIN MJ0110]
[SP:Q57574]
SPX13851385404649314797972.50E-225[LN:JE0395]120
[AC:JE0395]
[PN:phospho-beta-galactosidase I]
[CL:Agrobacterium beta-glucosidase]
[OR:Lactobacillus gasseri]
SPX138613864047122366NO-HIT6
SPX138713874048692073592.90E-46[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX1388138840491313934561.30E-58[LN:RS9_BACST]118
[AC:P07842]
[GN:RPSI]
[OR:Bacillus stearothermophilus]
[DE:30S RIBOSOMAL PROTEIN S9 (BS10)]
[SP:P07842]
SPX1389138940501494474872.30E-62[LN:RL13_STACA]109
[AC:Q00990]
[GN:RPLM]
[OR:Staphylococcus carnosus]
[DE:50S RIBOSOMAL PROTEIN L13]
[SP:Q00990]
SPX139013904051122366NO-HIT6
SPX139113914052106318NO-HIT6
SPX1392139240531313936308.40E-84“[LN:SULD_STRPN]181
[AC:P22291:O33697]
[GN:SULD]
[OR:Streptococcus pneumoniae]
[EC:4.1.2.25:2.7.6.3]
[DE:HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE) (PPPK)]]
[SP:P22291:O33697]”
SPX1393139340541705108341.40E-111“[LN:A36704]220
[AC:A36704]
[PN:bifunctional folate biosynthesis enzyme sulD:6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase:7, 8-dihydro-6-hydroxymethylpterin pyrophosphokinase]
[GN:sulD]
[OR:Streptococcus pneumoniae]”
SPX1394139440551855559384.90E-127“[LN:GCH1_STRPN]133
[AC:P51595]
[GN:SULC]
[OR:Streptococcus pneumoniae]
[EC:3.5.4.16]
[DE:GTP CYCLOHYDROLASE I, (GTP-CH-I)]
[SP:P51595]”
SPX139513954056441132322190146
SPX13961396405732798114857.00E-201[LN:DHPS_STRPN]117
[AC:P05382]
[GN:SULA]
[OR:Streptococcus pneumoniae]
[EC:2.5.1.15]
[DE:PYROPHOSPHORYLASE)]
[SP:P05382]
SPX1397139740582367081433.00E-13[GI:1402529]128
[LN:D78257]
[AC:D78257]
[PN:ORF8]
[GN:orf8]
[OR:Enterococcus faecalis]
[SR:Enterococcus faecalis plasmid:pYI17 DNA]
SPX13981398405962186NO-HIT6
SPX13991399406049414824471.70E-116[GI:6624219]127
[LN:AB023289]
[AC:AB023289]
[GN:ORFX]
[OR:Pseudomonas fluorescens]
[SR:Pseudomonas fluorescens (strain:No.33) DNA]
SPX1400140040612718131998.70E-36[LN:F69841]178
[AC:F69841]
[PN:conserved hypothetical protein yitU]
[GN:yitU]
[CL:Methanobacterium thermoautotrophicum conserved hypothetical protein MTH1071]
[OR:Bacillus subtilis]
SPX1401140140623119338612.70E-156[GI:7379448]124
[LN:NMA3Z2491]
[AC:AL162754:AL157959]
[PN:putative alcohol dehydrogenase]
[GN:adhA]
[OR:Neisseria meningitidis]
SPX1402140240633339997952.40E-188[GI:5669855]128
[LN:AF130465]
[AC:AF130465]
[PN:mannose-specific phosphotransferase system]
[GN:manL]
[OR:Streptococcus salivarius]
SPX1403140340642688049741.10E-144[GI:5669856]128
[LN:AF130465]
[AC:AF130465]
[PN:mannose-specific phosphotransferase system]
[GN:manM]
[OR:Streptococcus salivarius]
SPX14041404406530491211573.60E-158[GI:5669857]128
[LN:AF130465]
[AC:AF130465]
[PN:mannose-specific phosphotransferase system]
[GN:manN]
[OR:Streptococcus salivarius]
SPX140514054066445133519004.00E-256“[LN:PEPC_STRTR]120
[AC:Q56115]
[GN:PEPC]
[OR:Streptococcus thermophilus]
[EC:3.4.22.-]
[DE:AMINOPEPTIDASE C,]
[SP:Q56115]”
SPX1406140640672417232231.50E-59[GI:7328274]103
[LN:SAY14816]
[AC:Y14816]
[PN:hypothetical protein]
[GN:ORF231]
[OR:Staphylococcus aureus]
SPX1407140740681374113282.80E-41[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX14081408406977231NO-HIT6
SPX140914094070772311541.90E-17[LN:B69770]97
[AC:B69770]
[PN:conserved hypothetical protein ydaS]
[GN:ydaS]
[OR:Bacillus subtilis]
SPX141014104071414124217926.20E-241[GI:4731022]107
[LN:AF102860]
[AC:AF102860]
[PN:aminopeptidase PepS]
[GN:pepS]
[OR:Streptococcus thermophilus]
SPX14111411407260180NO-HIT6
SPX14121412407377231NO-HIT6
SPX141314134074932791101.90E-19“[LN:B71883]188
[AC:B71883]
[PN:hypothetical protein jhp0831]
[GN:jhp0831]
[CL:conserved hypothetical protein HI0711]
[OR:Helicobacter pylori]
[SR:strain J99, , strain J99]
[SR:strain J99, ]”
SPX14141414407588264800.00012[LN:DINJ_ECOLI]107
[AC:Q47150]
[GN:DINJ]
[OR:Escherichia coli]
[DE:DNA-DAMAGE-INDUCIBLE PROTEIN J]
[SP:Q47150]
SPX1415141540761464439216890“[GI:143342]109
[LN:BACPOLC]
[AC:M22996]
[GN:polC]
[OR:Bacillus subtilis]
[SR:B.subtilis SB19 DNA, clone PRO10]”
SPX141614164077694208228330[LN:T44380]191
[AC:T44380]
[PN:translation elongation factor EF-G fus [imported]]
[GN:fus]
[CL:translation elongation factor G:translation elongation factor Tu homology]
[OR:Bacillus halodurans]
SPX141714174078119357865.20E-10[LN:YHA2_EIKCO]115
[AC:P35649]
[OR:Eikenella corrodens]
[DE:HYPOTHETICAL 66.3 KD PROTEIN IN HAG2 5′REGION]
[SP:P35649]
SPX141814184079150450881.30E-08[LN:YHA2_EIKCO]115
[AC:P35649]
[OR:Eikenella corrodens]
[DE:HYPOTHETICAL 66.3 KD PROTEIN IN HAG2 5′REGION]
[SP:P35649]
SPX1419141940801444321731.90E-17[GI:7576785]112
[LN:AF214675]
[AC:AF214675]
[PN:unknown in vivo-induced protein 131-19]
[OR:Pseudomonas aeruginosa]
SPX1420142040811574716331.10E-83[LN:F69699]161
[AC:F69699:S11357]
[PN:ribosomal protein S7 (rpsG):ribosomal protein BS7]
[GN:rpsG]
[CL:Escherichia coli ribosomal protein S7]
[OR:Bacillus subtilis]
SPX1421142140821384146991.70E-91[LN:RS12_STRPN]114
[AC:P30891]
[GN:RPSL:STR]
[OR:Streptococcus pneumoniae]
[DE:30S RIBOSOMAL PROTEIN S12]
[SP:P30891]
SPX1422142240831205361514780[GI:1665738]125
[LN:D78258]
[AC:D78258]
[PN:alkaline amylopullulanase]
[OR:Bacillus sp.]
[SR:Bacillus sp. (strain:KSM-1378) DNA]
SPX1423142340843089246551.70E-115“[GI:2735505]114
[LN:SCU96107]
[AC:U96107]
[PN:N5,N10-methylenetetrahydromethanopterin]
[OR:Staphylococcus carnosus]”
SPX14241424408560318099633.70E-194“[LN:B69633]210
[AC:B69633]
[PN:glutamine--fructose-6-phosphate transaminase (isomerizing), glmS]
[GN:glmS]
[CL:glutamine--fructose-6-phosphate aminotransferase (isomerizing)]
[OR:Bacillus subtilis]
[EC:2.6.1.16]”
SPX14251425408646013808512.00E-207[LN:D69785]127
[AC:D69785]
[PN:beta-glucosidase homolog ydhP]
[GN:ydhP]
[CL:Agrobacterium beta-glucosidase]
[OR:Bacillus subtilis]
SPX14261426408734710412981.30E-82“[LN:G69682]153
[AC:G69682]
[PN:proline--tRNA ligase, proS:prolyl-tRNA synthetase]
[GN:proS]
[CL:proline--tRNA ligase]
[OR:Bacillus subtilis]
[EC:6.1.1.15]”
SPX14271427408833610086915.20E-109“[LN:G69682]153
[AC:G69682]
[PN:proline--tRNA ligase, proS:prolyl-tRNA synthetase]
[GN:proS]
[CL:proline--tRNA ligase]
[OR:Bacillus subtilis]
[EC:6.1.1.15]”
SPX14281428408942012604368.50E-136[GI:5714510]129
[LN:AF152237]
[AC:AF152237]
[PN:Eep]
[GN:eep]
[FN:determinant for enhanced expression of]
[OR:Enterococcus faecalis]
SPX1429142940902688042021.20E-51[LN:CDSA_BACSU]101
[AC:O31752]
[GN:CDSA]
[OR:Bacillus subtilis]
[EC:2.7.7.41]
[DE:SYNTHASE)]
[SP:O31752]
SPX1430143040912597774902.80E-90[LN:UPPS_BACSU]136
[AC:O31751]
[GN:UPPS]
[OR:Bacillus subtilis]
[EC:2.5.1.31]
[DE:(DI-TRANS-POLY-CIS-DECAPRENYLCISTRANSFERASE)]
[SP:O31751]
SPX1431143140921915731271.50E-11[LN:S70841]192
[AC:S70841]
[PN:hypothetical transmembrane protein (sipS 3′region)]
[CL:Bradyrhizobium japonicum hypothetical transmembrane protein (sipS 3′region)]
[OR:Bradyrhizobium japonicum]
SPX14321432409333399910451.50E-140[LN:H81105]124
[AC:H81105]
[PN:Holliday junction DNA helicase RuvB NMB1243 [imported]]
[GN:NMB1243]
[OR:Neisseria meningitidis]
SPX14331433409435105760.00015[LN:H72613]92
[AC:H72613]
[PN:hypothetical protein APE1371]
[GN:APE1371]
[OR:Aeropyrum pernix]
SPX1434143440951394171031.50E-06[GI:5616248]95
[LN:AF158628]
[AC:AF158628]
[PN:hypothetical protein]
[OR:Prochlorococcus PCC9511]
SPX1435143540962326964821.50E-73“[LN:YIW2_YEAST]155
[AC:P40586]
[GN:YIR042C]
[OR:Saccharomyces cerevisiae]
[SR:,Baker′s yeast]
[DE:HYPOTHETICAL 27.4 KD PROTEIN IN HYR1 3′REGION]
[SP:P40586]”
SPX14361436409764192NO-HIT6
SPX14371437409883425029440“LN:C70131]199
[AC:C70131]
[PN:leucine--tRNA ligase, leuS:leucyl-tRNA synthetase:leucyl-tRNA synthetase]
[CL:leucine--tRNA ligase]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]
[EC:6.1.1.4]”
SPX14381438409936310899981.00E-137“[LN:GLDA_BACST]137
[AC:P32816]
[GN:GLDA:GLD]
[OR:Bacillus stearothermophilus]
[EC:1.1.1.6]
[DE:GLYCEROL DEHYDROGENASE, (GLDH)]
[SP:P32816]”
SPX1439143941002236693568.20E-53[GI:2582658]142
[LN:CBAJ2527]
[AC:AJ002527]
[PN:OrfX]
[GN:orfX]
[FN:putative transaldolase (37.4% identity to talC]
[OR:Clostridium beijerinckii]
SPX14401440410181624489921.80E-275[LN:PFLF_ECOLI]99
[AC:P75793]
[GN:YBIW]
[OR:Escherichia coli]
[EC:2.3.1.54]
[DE:LYASE 3)]
[SP:P75793]
SPX14411441410242712813374.90E-89“[LN:PTCC_BACST]157
[AC:Q45400]
[GN:CELB]
[OR:Bacillus stearothermophilus]
[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]
[SP:Q45400]”
SPX1442144241031033091943.50E-22[LN:A69785]189
[AC:A69785]
[PN:cellobiose phosphotransferase system enzym homolog ydhM]
[GN:ydhM]
[CL:phosphotransferase system enzyme II cellobiose-specific factor IIB]
[OR:Bacillus subtilis]
SPX1443144341041073211865.70E-21[LN:PTCA_BACSU]121
[AC:P46319]
[GN:CELC:LICA]
[OR:Bacillus subtilis]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EIII-CEL)]
[SP:P46319]
SPX1444144441053279812652.80E-49[LN:SORC_KLEPN]130
[AC:P37078]
[GN:SORC]
[OR:Klebsiella pneumoniae]
[DE:SORBITOL OPERON REGULATOR (SOR OPERON ACTIVATOR)]
[SP:P37078]
SPX1445144541062497472526.10E-57[LN:YCIT_ECOLI]145
[AC:P76034]
[GN:YCIT]
[OR:Escherichia coli]
[DE:HYPOTHETICAL TRANSCRIPTIONAL REGULATOR IN OSMB-RNB INTERGENIC REGION]
[SP:P76034]
SPX1446144641072597772664.40E-55“[LN:PFLE_ECOLI]145
[AC:P75794]
[GN:YBIY]
[OR:Escherichia coli]
[EC:1.97.1.4]
[DE:PUTATIVE PYRUVATE FORMATE-LYASE 3 ACTIVATING ENZYME,]
[SP:P75794]”
SPX144714474108832491053.60E-08[GI:7331182]88
[LN:AF235048]
[AC:AF235048]
[PN:AgpT]
[GN:agpT]
[OR:Sinorhizobium meliloti]
SPX144814484109651951774.60E-18[GI:6127225]129
[LN:SHU75349]
[AC:U75349]
[PN:periplasmic-iron-binding protein BitA]
[GN:bit operon]
[OR:Brachyspira hyodysenteriae]
SPX1449144941101233692421.10E-26[GI:6127225]129
[LN:SHU75349]
[AC:U75349]
[PN:periplasmic-iron-binding protein BitA]
[GN:bit operon]
[OR:Brachyspira hyodysenteriae]
SPX1450145041113189547991.70E-113[GI:2766194]121
[LN:SHU75349]
[AC:U75349]
[PN:putative ABC transporter BitD]
[GN:bit operon]
[OR:Brachyspira hyodysenteriae]
SPX1451145141122096272832.70E-40[GI:2766195]114
[LN:SHU75349]
[AC:U75349]
[PN:putative permease BitE]
[GN:bit operon]
[OR:Brachyspira hyodysenteriae]
SPX1452145241132577712951.50E-68[GI:2766196]114
[LN:SHU75349]
[AC:U75349]
[PN:putative permease BitF]
[GN:bit operon]
[OR:Brachyspira hyodysenteriae]
SPX145314534114661981643.20E-17[GI:2766196]114
[LN:SHU75349]
[AC:U75349]
[PN:putative permease BitF]
[GN:bit operon]
[OR:Brachyspira hyodysenteriae]
SPX1454145441152507501373.20E-10[LN:PMGY_TREPA]122
[AC:P96121]
[GN:GPM:PGM:TP0168]
[OR:Treponema pallidum]
[EC:5.4.2.1]
[DE:(BPG-DEPENDENT PGAM)]
[SP:P96121]
SPX14551455411644613388556.60E-196[GI:7380543]127
[LN:NMA6Z2491]
[AC:AL162757:AL157959]
[PN:conserved hypothetical protein]
[GN:NMA1908]
[OR:Neisseria meningitidis]
SPX1456145641171203601239.30E-21[LN:E64494]86
[AC:E64494]
[PN:hypothetical protein MJ1558]
[OR:Methanococcus jannaschii]
SPX1457145741181293872822.20E-58[LN:T44411]140
[AC:T44411]
[PN:ribosomal protein L17 [imported]]
[GN:rplQ]
[CL:Escherichia coli ribosomal protein L17]
[OR:Bacillus halodurans]
SPX1458145841193129369636.70E-130[LN:RPOA_BACSU]134
[AC:P20429]
[GN:RPOA]
[OR:Bacillus subtilis]
[EC:2.7.7.6]
[DE:ALPHA CHAIN) (RNA POLYMERASE ALPHA SUBUNIT)]
[SP:P20429]
SPX145914594120134402NO-HIT6
SPX1460146041211414234941.80E-63[LN:RS11_BACSU]110
[AC:P04969]
[GN:RPSK]
[OR:Bacillus subtilis]
[DE:30S RIBOSOMAL PROTEIN S11 (BS11)]
[SP:P04969]
SPX1461146141221223664331.70E-55[GI:1044989]97
[LN:BACRPLP]
[AC:L47971]
[PN:ribosomal protein S13]
[GN:rpsM]
[OR:Bacillus subtilis]
SPX146214624123561682371.10E-28[LN:S17988]151
[AC:S17988]
[PN:translation initiation factor IF-1]
[GN:infA]
[CL:translation initiation factor IF-1]
[OR:Lactococcus lactis subsp. lactis]
SPX1463146341242136395608.10E-95“[LN:KAD_LACLA]177
[AC:P27143]
[GN:ADK]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.4.3]
[DE:ADENYLATE KINASE, (ATP-AMP TRANSPHOSPHORYLASE)]
[SP:P27143]”
SPX14641464412543713119274.30E-126“[LN:SECY_LACLA]155
[AC:P27148]
[GN:SECY]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:PREPROTEIN TRANSLOCASE SECY SUBUNIT]
[SP:P27148]”
SPX1465146541261474416147.90E-79[LN:RL15_STAAU]107
[AC:O06445]
[GN:RPLO]
[OR:Staphylococcus aureus]
[DE:50S RIBOSOMAL PROTEIN L15]
[SP:O06445]
SPX146614664127611831856.90E-21[LN:RL30_STAAU]107
[AC:O06444]
[GN:RPMD]
[OR:Staphylococcus aureus]
[DE:50S RIBOSOMAL PROTEIN L30]
[SP:O06444]
SPX1467146741281654956218.70E-81[LN:RS5_BACST]117
[AC:P02357]
[GN:RPSE]
[OR:Bacillus stearothermophilus]
[DE:30S RIBOSOMAL PROTEIN S5 (BS5)]
[SP:P02357]
SPX1468146841291193572322.60E-53[LN:RL18_BACSU]117
[AC:P46899:P70969]
[GN:RPLR]
[OR:Bacillus subtilis]
[DE:50S RIBOSOMAL PROTEIN L18]
[SP:P46899:P70969]
SPX1469146941301755254782.00E-66[LN:B69695]136
[AC:B69695]
[PN:ribosomal protein L6 (BL8) rplF]
[GN:rplF]
[CL:Escherichia coli ribosomal protein L6]
[OR:Bacillus subtilis]
SPX1470147041311333995212.60E-67[GI:1044978]96
[LN:BACRPLP]
[AC:L47971]
[PN:ribosomal protein S8]
[GN:rpsH]
[OR:Bacillus subtilis]
SPX14711471413279237NO-HIT6
SPX147214724133902703258.80E-41[LN:F69835]140
[AC:F69835]
[PN:ribosomal protein S14 homolog yhzA]
[GN:yhzA]
[CL:Escherichia coli ribosomal protein S14]
[OR:Bacillus subtilis]
SPX1473147341341815437286.40E-96[LN:T44395]138
[AC:T44395]
[PN:ribosomal protein L5 [imported]]
[GN:rplE]
[CL:Escherichia coli ribosomal protein L5]
[OR:Bacillus halodurans]
SPX1474147441351023065082.80E-65[GI:4927751]91
[LN:AF126059]
[AC:AF126059]
[PN:RpL24]
[GN:rplX]
[OR:Streptococcus pneumoniae]
SPX1475147541361233695972.20E-78[GI:4927750]91
[LN:AF126059]
[AC:AF126059]
[PN:RpL14]
[GN:rplN]
[OR:Streptococcus pneumoniae]
SPX1476147641371103301004.40E-07[LN:E71186]150
[AC:E71186]
[PN:hypothetical protein PH1769]
[GN:PH1769]
[CL:Pyrococcus horikoshii hypothetical protein PH1769]
[OR:Pyrococcus horikoshii]
SPX147714774138872614303.10E-55[GI:4927749]91
[LN:AF126059]
[AC:AF126059]
[PN:RpS17]
[GN:rpsQ]
[OR:Streptococcus pneumoniae]
SPX147814784139133399NO-HIT6
SPX147914794140692073248.90E-40[GI:4927748]91
[LN:AF126059]
[AC:AF126059]
[PN:RpL29]
[GN:rpmC]
[OR:Streptococcus pneumoniae]
SPX1480148041411384147081.30E-94[GI:4927747]91
[LN:AF126059]
[AC:AF126059]
[PN:RpL16]
[GN:rplP]
[OR:Streptococcus pneumoniae]
SPX14811481414220962710632.10E-142[GI:4927746]90
[LN:AF126059]
[AC:AF126059]
[PN:RpS3]
[GN:rpsC]
[OR:Streptococcus pneumoniae]
SPX148214824143752253561.60E-44[GI:4927745]91
[LN:AF126059]
[AC:AF126059]
[PN:RpL22]
[GN:rplV]
[OR:Streptococcus pneumoniae]
SPX14831483414482246NO-HIT6
SPX148414844145942824925.20E-64[GI:4927744]91
[LN:AF126059]
[AC:AF126059]
[PN:RpS19]
[GN:rpsS]
[OR:Streptococcus pneumoniae]
SPX14851485414627883411442.80E-152[LN:RL2_BACST]111
[AC:P04257]
[GN:RPLB]
[OR:Bacillus stearothermophilus]
[DE:50S RIBOSOMAL PROTEIN L2]
[SP:P04257]
SPX148614864147992971621.30E-30[GI:3273331]138
[LN:AB015722]
[AC:AB015722]
[PN:ribosomal protrein L23]
[OR:Bacillus stearothermophilus]
[SR:Bacillus stearothermophilus DNA]
SPX1487148741482086246966.80E-91[LN:RL4_BACST]111
[AC:P28601]
[GN:RPLD]
[OR:Bacillus stearothermophilus]
[DE:50S RIBOSOMAL PROTEIN L4]
[SP:P28601]
SPX1488148841492096274966.60E-110[LN:RL3_BACSU]107
[AC:P42920]
[GN:RPLC]
[OR:Bacillus subtilis]
[DE:50S RIBOSOMAL PROTEIN L3 (BL3)]
[SP:P42920]
SPX1489148941501033094943.40E-64[LN:RS10_STRMU]106
[AC:P48853]
[GN:RPSJ]
[OR:Streptococcus mutans]
[DE:30S RIBOSOMAL PROTEIN S10]
[SP:P48853]
SPX149014904151206618710.00018[GI:7302797]105
[LN:AE003803]
[AC:AE003803:AE002787]
[GN:CG4798]
[OR:Drosophila melanogaster]
[SR:fruit fly]
SPX1491149141521975918433.60E-112[GI:4098082]167
[LN:LLU73336]
[AC:U73336]
[PN:anaerobic ribonucleotide reductase activator]
[GN:nrdG]
[FN:activation of anaerobic]
[OR:Lactococcus lactis subsp. cremoris]
SPX14921492415369207NO-HIT6
SPX1493149341541695071874.50E-19[LN:G75479]90
[AC:G75479]
[PN:hypothetical protein]
[GN:DR0763]
[OR:Deinococcus radiodurans]
SPX149414944155155465NO-HIT6
SPX149514954156738221411231.10E-231[GI:4098081]128
[LN:LLU73336]
[AC:U73336]
[PN:anaerobic ribonucleotide reductase]
[GN:nrdD]
[OR:Lactococcus lactis subsp. cremoris]
SPX1496149641575191557NO-HIT6
SPX14971497415849214765193.70E-97[LN:YWAP_STRMU]119
[AC:P34001]
[OR:Streptococcus mutans]
[DE:HYPOTHETICAL PROTEIN IN WAPA 3′REGION (FRAGMENT)]
[SP:P34001]
SPX149814984159186558930.00012[LN:A26892]84
[AC:A26892]
[PN:Mopa box protein]
[OR:Mus musculus]
[SR:, house mouse]”
SPX14991499416070210NO-HIT6
SPX150015004161130390667.30E-09[GI:1119198]122
[LN:BACCOMC]
[AC:M30805]
[PN:unknown protein]
[OR:Bacillus subtilis]
[SR:Bacillus subtilis (strain IS75) DNA]
SPX1501150141621614831195.10E-16[LN:FOLC_LACCA]111
[AC:P15925]
[GN:FGS]
[OR:Lactobacillus casei]
[EC:6.3.2.17]
[DE:SYNTHETASE) (FPGS)]
[SP:P15925]
SPX1502150241631644922512.00E-38[LN:FOLC_BACSU]110
[AC:Q05865]
[GN:FOLC]
[OR:Bacillus subtilis]
[EC:6.3.2.17]
[DE:SYNTHETASE) (FPGS)]
[SP:Q05865]
SPX150315034164102306875.90E-11[LN:A69982]87
[AC:A69982]
[PN:hypothetical protein yrzB]
[GN:yrzB]
[OR:Bacillus subtilis]
SPX1504150441651404203272.00E-40[LN:D69979]163
[AC:D69979]
[PN:conserved hypothetical protein yrrK]
[GN:yrrK]
[CL:Haemophilus influenzae conserved hypothetical protein HI0305]
[OR:Bacillus subtilis]
SPX15051505416689267NO-HIT6
SPX150615064167190570NO-HIT6
SPX1507150741681333993151.80E-38[GI:6650536]81
[LN:AF103794]
[AC:AF103794]
[PN:unknown]
[OR:Listeria monocytogenes]
SPX1508150841691263783331.60E-40[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX1509150941701313933403.70E-41[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX15101510417129688810358.50E-139[GI:6318592]185
[LN:AF146529]
[AC:AF146529]
[PN:aromatic amino acid aminotransferase]
[GN:araT]
[FN:catalyzes the last reaction in the biosynthesis]
[OR:Lactococcus lactis subsp. cremoris]
SPX15111511417262186NO-HIT6
SPX1512151241732577712972.20E-40[LN:YQXN_BACSU]89
[AC:P42095]
[GN:YQXN:YQFI]
[OR:Bacillus subtilis]
[DE:(ORF3)]
[SP:P42095]
SPX1513151341743319936236.80E-120[LN:H69679]148
[AC:H69679]
[PN:involved in fatty acid/phospholipid synthesis plsX]
[GN:plsX]
[CL:phospholipid synthesis protein]
[OR:Bacillus subtilis]
SPX151415144175112336NO-HIT6
SPX151515154176782341291.40E-17[LN:C72349]142
[AC:C72349]
[PN:acyl carrier protein]
[GN:TM0662]
[CL:acyl carrier protein:acyl carrier protein homology]
[OR:Thermotoga maritima]
SPX151615164177982943204.80E-40[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX15171517417877231643.00E-06[GI:2695624]128
[LN:STU93029]
[AC:U93029]
[PN:amphipathic pore-forming peptide precursor]
[GN:thmA]
[OR:Streptococcus thermophilus]
SPX15181518417969207NO-HIT6
SPX151915194180720216035710[LN:COMA_STRPN]119
[AC:Q03727]
[GN:COMA]
[OR:Streptococcus pneumoniae]
[DE:TRANSPORT ATP-BINDING PROTEIN COMA]
[SP:Q03727]
SPX152015204181450135021848.20E-289[LN:COMB_STRPN]107
[AC:P36498]
[GN:COMB]
[OR:Streptococcus pneumoniae]
[DE:TRANSPORT PROTEIN COMB]
[SP:P36498]
SPX15211521418225075011891.40E-160[LN:PUR7_STRPN]117
[AC:Q07296]
[GN:PURC]
[OR:Streptococcus pneumoniae]
[EC:6.3.2.6]
[DE:(SAICAR SYNTHETASE)]
[SP:Q07296]
SPX1522152241832547621272.80E-08“““[LN:C69492]217
[AC:C69492]
[PN:phosphoribosylformylglycinamidine synthase, component II:formylglycinamide ribotide amidotransferase:phosphoribosylformylglycinamidine synthetase]
[OR:Archaeoglobus fulgidus]
[EC:6.3.5.3]”””
SPX152315234184952851553.80E-15[GI:4928281]110
[LN:AF132127]
[AC:AF132127]
[PN:glucose-6-phosphate isomerase]
[GN:gpi]
[OR:Streptococcus mutans]
SPX152415244185457137117641.20E-238[GI:4928281]110
[LN:AF132127]
[AC:AF132127]
[PN:glucose-6-phosphate isomerase]
[GN:gpi]
[OR:Streptococcus mutans]
SPX1525152541862467382463.10E-28“[LN:YDP3_LACLA]162
[AC:P22347]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:HYPOTHETICAL 18.7 KD PROTEIN IN PEPX 3′REGION (ORF3)]
[SP:P22347]”
SPX152615264187604181210012.10E-222[GI:4104142]99
[LN:AF033015]
[AC:AF033015]
[PN:ABC transporter homolog Z]
[OR:Listeria monocytogenes]
SPX15271527418872216NO-HIT6
SPX1528152841891083241051.60E-07[GI:6015958]110
[LN:SSU18930]
[AC:Y18930]
[PN:hypothetical protein]
[GN:ORF-c22_037]
[OR:Sulfolobus solfataricus]
SPX1529152941901965884557.30E-58[GI:4104141]99
[LN:AF033015]
[AC:AF033015]
[PN:ABC transporter homolog Y]
[OR:Listeria monocytogenes]
SPX15301530419136110834222.80E-66[GI:4104140]99
[LN:AF033015]
[AC:AF033015]
[PN:ABC transporter homolog X]
[OR:Listeria monocytogenes]
SPX153115314192655196532900[LN:HEXA_STRPN]117
[AC:P10564]
[GN:HEXA]
[OR:Streptococcus pneumoniae]
[DE:DNA MISMATCH REPAIR PROTEIN HEXA]
[SP:P10564]
SPX1532153241931825468596.40E-114[LN:HEXA_STRPN]117
[AC:P10564]
[GN:HEXA]
[OR:Streptococcus pneumoniae]
[DE:DNA MISMATCH REPAIR PROTEIN HEXA]
[SP:P10564]
SPX1533153341941494477407.50E-99[LN:ARGR_STRPN]112
[AC:Q54870]
[GN:ARGR]
[OR:Streptococcus pneumoniae]
[DE:PROBABLE ARGININE REPRESSOR]
[SP:Q54870]
SPX15341534419556416923653.20E-102“[LN:SYRC_YEAST]154
[AC:Q05506]
[GN:YDR341C:D9651.10]
[OR:Saccharomyces cerevisiae]
[SR:,Baker′s yeast]
[EC:6.1.1.19]
[DE:-TRNA LIGASE) (ARGRS)]
[SP:Q05506]”
SPX1535153541961504503986.20E-51[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX15361536419768204NO-HIT6
SPX153715374198952851026.20E-17“[LN:S74709]124
[AC:S74709]
[PN:hypothetical protein sll1188]
[OR:Synechocystis sp.]
[SR:PCC 6803, , PCC 6803]
[SR:PCC 6803, ]”
SPX15381538419923670812094.90E-164[GI:5830529]104
[LN:SPAJ6394]
[AC:AJ006394]
[PN:response regulator]
[GN:phoP]
[OR:Streptococcus pneumoniae]
SPX153915394200444133221964.10E-300[GI:5830530]102
[LN:SPAJ6394]
[AC:AJ006394]
[PN:histidine kinase]
[GN:phoR]
[OR:Streptococcus pneumoniae]
SPX15401540420129287614351.70E-188[GI:4530447]116
[LN:AF118229]
[AC:AF118229]
[PN:phosphate binding protein PstS]
[GN:pstS]
[OR:Streptococcus pneumoniae]
SPX15411541420227281613332.80E-185[GI:4530448]112
[LN:AF118229]
[AC:AF118229]
[PN:transmembrane protein PstC]
[GN:pstC]
[OR:Streptococcus pneumoniae]
SPX15421542420327281613121.10E-182[GI:4530449]112
[LN:AF118229]
[AC:AF118229]
[PN:transmembrane protein PstA]
[GN:PstA]
[OR:Streptococcus pneumoniae]
SPX15431543420425175312842.00E-174[GI:4530450]119
[LN:AF118229]
[AC:AF118229]
[PN:ATP-binding cassette protein PstB]
[GN:pstB]
[OR:Streptococcus pneumoniae]
SPX15441544420521765110678.20E-144[GI:4530451]90
[LN:AF118229]
[AC:AF118229]
[PN:PhoU]
[GN:phoU]
[OR:Streptococcus pneumoniae]
SPX1545154542061424261312.90E-10[GI:5822769]109
[LN:AB024553]
[AC:AB024553]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA]
SPX15461546420773219NO-HIT6
SPX154715474208153459NO-HIT6
SPX15481548420933910179216.40E-122[LN:GPDA_BACSU]144
[AC:P46919]
[GN:GPSA:GLYC]
[OR:Bacillus subtilis]
[EC:1.1.1.94]
[DE:DEPENDENT DIHYDROXYACETONE-PHOSPHATE REDUCTASE)]
[SP:P46919]
SPX15491549421030090014811.60E-199[GI:3550619]159
[LN:SPAJ4869]
[AC:AJ004869]
[PN:UTP-glucose-1-phosphate uridylyltransferase]
[GN:galU]
[FN:synthesis of UDP-glucose]
[OR:Streptococcus pneumoniae]
SPX155015504211225675NO-HIT6
SPX1551155142122276815201.90E-70[LN:SUB400707]80
[AC:AJ400707]
[PN:hypothetical protein]
[OR:Streptococcus uberis]
SPX1552155242131825462361.30E-55[GI:3192049]108
[LN:AB001562]
[AC:AB001562]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:Xc) DNA]
SPX15531553421437711316224.50E-119[LN:G69866]119
[AC:G69866]
[PN:hippurate hydrolase homolog ykuR]
[GN:ykuR]
[CL:hippurate hydrolase]
[OR:Bacillus subtilis]
SPX1554155442152336995781.10E-86“[LN:H72245]146
[AC:H72245]
[PN:2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase-related protein]
[GN:TM1519]
[OR:Thermotoga maritima]”
SPX155515554216153459755.50E-08[GI:6103625]71
[LN:AF172095]
[AC:AF172095]
[PN:unknown]
[OR:Picea rubens]
SPX15561556421772216NO-HIT6
SPX1557155742182788342142.60E-30[LN:YDED_BACSU]136
[AC:P96661]
[GN:YDED]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 35.3 KD PROTEIN IN CSPC-NAP INTERGENIC REGION]
[SP:P96661]
SPX155815584219821246341470[GI:6165962]116
[LN:AF101781]
[AC:AF101781]
[PN:penicillin-binding protein 1b]
[GN:pbp1b]
[OR:Streptococcus pneumoniae]
SPX15591559422041912576971.90E-174[LN:SYY1_BACSU]100
[AC:P22326]
[GN:TYRS]
[OR:Bacillus subtilis]
[EC:6.1.1.1]
[DE:(TYRRS 1)]
[SP:P22326]
SPX15601560422169120732181.60E-63“[LN:COPA_ENTHR]148
[AC:P32113:Q47841]
[GN:COPA]
[OR:Enterococcus hirae]
[EC:3.6.1.36]
[DE:COPPER/POTASSIUM-TRANSPORTING ATPASE A,]
[SP:P32113:Q47841]”
SPX15611561422265195NO-HIT6
SPX156215624223882641092.90E-08[LN:RRMA_ECOLI]109
[AC:P36999]
[GN:RRMA]
[OR:Escherichia coli]
[EC:2.1.1.51]
[DE:METHYLTRANSFERASE)]
[SP:P36999]
SPX1563156342241975911921.90E-25[LN:YXJB_BACSU]128
[AC:P42313]
[GN:YXJB:N15I]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 31.5 KD PROTEIN IN KATB 3′REGION]
[SP:P42313]
SPX15641564422557171NO-HIT6
SPX156515654226191573NO-HIT6
SPX15661566422775322594735.80E-165“[LN:PHSG_BACSU]116
[AC:P39123]
[GN:GLGP]
[OR:Bacillus subtilis]
[EC:2.4.1.1]
[DE:GLYCOGEN PHOSPHORYLASE,]
[SP:P39123]”
SPX156715674228506151826870[LN:MALQ_STRPN]137
[AC:P29851]
[GN:MALM]
[OR:Streptococcus pneumoniae]
[EC:2.4.1.25]
[DE:(DISPROPORTIONATING ENZYME) (D-ENZYME)]
[SP:P29851]
SPX156815684229424127221673.30E-288[LN:MALX_STRPN]131
[AC:P29850]
[GN:MALX]
[OR:Streptococcus pneumoniae]
[DE:MALTOSE/MALTODEXTRIN-BINDING PROTEIN PRECURSOR]
[SP:P29850]
SPX156915694230431129321760[LN:MALC_STRPN]136
[AC:Q04698]
[GN:MALC]
[OR:Streptococcus pneumoniae]
[DE:MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALC]
[SP:Q04698]
SPX15701570423128184312652.40E-177[LN:MALD_STRPN]136
[AC:Q04699]
[GN:MALD]
[OR:Streptococcus pneumoniae]
[DE:MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALD]
[SP:Q04699]
SPX1571157142322678015401.70E-145[LN:MALA_STRPN]97
[AC:Q08510]
[GN:MALA]
[OR:Streptococcus pneumoniae]
[DE:MALA PROTEIN]
[SP:Q08510]
SPX15721572423332998716687.30E-227[GI:2656094]146
[LN:STRMALR]
[AC:L21856]
[PN:repressor protein]
[GN:malR]
[FN:maltose operon transcriptional repressor]
[OR:Streptococcus pneumoniae]
SPX157315734234114342NO-HIT6
SPX1574157442351273813788.30E-48[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX1575157542363149424636.90E-73[GI:1620924]62
[LN:BS168NPRB]
[AC:Z79580]
[OR:Bacillus subtilis]
SPX15761576423758817647011.30E-229[LN:SYD_BACSU]98
[AC:O32038]
[GN:ASPS]
[OR:Bacillus subtilis]
[EC:6.1.1.12]
[DE:(ASPRS)]
[SP:O32038]
SPX157715774238144432NO-HIT6
SPX15781578423964192NO-HIT6
SPX15791579424077231NO-HIT6
SPX1580158042412146421209.80E-14[GI:1402529]128
[LN:D78257]
[AC:D78257]
[PN:ORF8]
[GN:orf8]
[OR:Enterococcus faecalis]
[SR:Enterococcus faecalis plasmid:pYI17 DNA]
SPX158115814242247741NO-HIT6
SPX15821582424367201NO-HIT6
SPX158315834244155465780.00011[LN:T07291]89
[AC:T07291]
[PN:hypothetical protein 42c]
[OR:chloroplast Chlorella vulgaris]
SPX15841584424562186NO-HIT6
SPX15851585424664192NO-HIT6
SPX158615864247631892007.00E-24[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX158715874248430129017407.50E-236[LN:SYH_STREQ]106
[AC:P30053]
[GN:HISS]
[OR:Streptococcus equisimilis]
[EC:6.1.1.21]
[DE:(HISRS)]
[SP:P30053]
SPX158815884249307921NO-HIT6
SPX15891589425041612483342.10E-57[GI:3582221]114
[LN:AE001272]
[AC:AE001272]
[PN:conserved hypothetical protein]
[GN:ORF00049]
[OR:Lactococcus lactis]
SPX159015904251133399NO-HIT6
SPX1591159142522848523011.70E-34[LN:RGG_STRGC]100
[AC:P49330]
[GN:RGG]
[OR:Streptococcus gordonii challis]
[DE:RGG PROTEIN]
[SP:P49330]
SPX1592159242531143422276.60E-27[GI:2258088]96
[LN:AB000631]
[AC:AB000631]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans DNA]
SPX15931593425456817049941.30E-207“[LN:S76895]148
[AC:S76895]
[PN:hypothetical protein]
[CL:dihydroxy-acid dehydratase]
[OR:Synechocystis sp.]
[SR:PCC 6803, , PCC 6803]
[SR:PCC 6803, ]”
SPX1594159442553119332722.40E-45“[LN:TKTC_METJA]149
[AC:Q58092]
[GN:MJ0679]
[OR:Methanococcus jannaschii]
[EC:2.2.1.1]
[DE:PUTATIVE TRANSKETOLASE C-TERMINAL SECTION, (TK)]
[SP:Q58092]”
SPX1595159542562868583477.70E-66“[LN:TKTN_METJA]149
[AC:Q58094]
[GN:MJ0681]
[OR:Methanococcus jannaschii]
[EC:2.2.1.1]
[DE:PUTATIVE TRANSKETOLASE N-TERMINAL SECTION, (TK)]
[SP:Q58094]”
SPX15961596425744913475359.90E-132[LN:T37066]107
[AC:T37066]
[PN:probable integral membrane protein]
[GN:SCJ21.17c]
[OR:Streptomyces coelicolor]
SPX15971597425895285NO-HIT6
SPX15981598425967720311978.80E-31“[GI:4512373]144
[LN:AB011837]
[AC:AB011837]
[GN:yjdC]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”
SPX15991599426033610081331.30E-18[GI:6689167]118
[LN:SCE20]
[AC:AL136058]
[PN:putative membrane protein]
[GN:SCE20.08c]
[OR:Streptomyces coelicolor A3(2)]
SPX16001600426167201NO-HIT6
SPX160116014262611832403.00E-28“[LN:RL32_LACLC]149
[AC:O34101]
[GN:RPMF]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[DE:50S RIBOSOMAL PROTEIN L32]
[SP:O34101]”
SPX160216024263642192613200[GI:1914872]88
[LN:SPZ82001]
[AC:Z82001]
[PN:PCPA]
[GN:pcpA]
[OR:Streptococcus pneumoniae]
SPX16031603426476228NO-HIT6
SPX1604160442651925764294.10E-54[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX1605160542661263783034.10E-37[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX1606160642671093274957.70E-65[GI:1914871]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX1607160742686271881950.00073[LN:T27355]100
[AC:T27355]
[PN:hypothetical protein Y70D2A.2]
[GN:Y70D2A.2]
[OR:Caenorhabditis elegans]
SPX1608160842692908701082.70E-22“[LN:F70203]181
[AC:F70203]
[PN:xylose operon regulatory protein (xylR-2) homolog]
[CL:glucose kinase:glucose kinase homology]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX16091609427088726613456.30E-65[LN:YBGG_ECOLI]151
[AC:P54746:P75753]
[GN:YBGG]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 100.0 KD PROTEIN IN HRSA-CYDA INTERGENIC REGION]
[SP:P54746:P75753]
SPX16101610427143513054096.20E-106[LN:T37125]101
[AC:T37125]
[PN:hypothetical protein SCJ4.42c]
[GN:SCJ4.42c]
[OR:Streptomyces coelicolor]
SPX16111611427269520854089.50E-105[GI:5759293]108
[LN:AF175722]
[AC:AF175722]
[PN:immunoreactive 89kD antigen PG87]
[OR:Porphyromonas gingivalis]
SPX16121612427356016802492.20E-63“[GI:4096756]170
[LN:SSU39394]
[AC:U39394]
[PN:alpha-1,3/4-fucosidase precursor]
[FN:alpha-fucosidase specific for alpha-1,3 and]
[OR:Streptomyces sp.]
[SR:Streptomyces sp]”
SPX16131613427441012309421.30E-244[LN:SAGP_STRPY]114
[AC:P16962]
[GN:SAGP]
[OR:Streptococcus pyogenes]
[DE:STREPTOCOCCAL ACID GLYCOPROTEIN]
[SP:P16962]
SPX16141614427533910178973.80E-184[GI:2764612]108
[LN:LSAJ1330]
[AC:AJ001330]
[PN:ornithine transcarbamoylase]
[GN:arcB]
[OR:Lactobacillus sakei]
SPX1615161542763169484653.40E-129[GI:2894540]143
[LN:EFAJ3331]
[AC:AJ223331]
[PN:carbamate kinase]
[GN:arcC]
[FN:synthesis of ATP from carbamylphosphate]
[OR:Enterococcus faecium]
SPX16161616427750415124264.50E-106[GI:2697115]75
[LN:AF008219]
[AC:AF008219]
[PN:unknown]
[OR:Borrelia afzelii]
SPX16171617427844413322778.20E-67[LN:S43914]101
[AC:S43914]
[PN:hypothetical protein 1]
[CL:peptidase V]
[OR:Bacillus stearothermophilus]
SPX16181618427964192NO-HIT6
SPX16191619428079237NO-HIT6
SPX16201620428189267NO-HIT6
SPX16211621428251153NO-HIT6
SPX162216224283722161764.20E-20[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX16231623428455165NO-HIT6
SPX1624162442853009005602.70E-78[GI:6714460]98
[LN:ATAC008261]
[AC:AC008261]
[GN:T4P13.3]
[OR:Arabidopsis thaliana]
[SR:thale cress]
SPX16251625428664192NO-HIT6
SPX16261626428738411528401.50E-119“[LN:ADH2_ECOLI]123
[AC:P37686]
[GN:YIAY]
[OR:Escherichia coli]
[EC:1.1.1.1]
[DE:PROBABLE ALCOHOL DEHYDROGENASE,]
[SP:P37686]”
SPX16271627428858917678747.80E-287[GI:6015981]108
[LN:AF137263]
[AC:AF137263]
[PN:L-fucose isomerase]
[GN:fucI]
[OR:Bacteroides thetaiotaomicron]
SPX1628162842892437292018.40E-20“[LN:B70645]155
[AC:B70645]
[PN:L-fuculose-phosphate aldolase,]
[GN:fucA]
[CL:L-ribulose-phosphate 4-epimerase]
[OR:Mycobacterium tuberculosis]
[EC:4.1.2.17]”
SPX16291629429010293087NO-HIT6
SPX163016304291738221417093.00E-243[GI:4567098]113
[LN:AF130985]
[AC:AF130985]
[PN:alpha-galactosidase AgaN]
[GN:agaN]
[OR:Bacillus stearothermophilus]
SPX16311631429262418721125.60E-07[LN:T36462]101
[AC:T36462]
[PN:hypothetical protein SCF85.02]
[GN:SCF85.02]
[OR:Streptomyces coelicolor]
SPX16321632429344013201741.10E-50[LN:T36467]123
[AC:T36467]
[PN:probable glycosyl hydrolase]
[GN:SCF85.07]
[CL:alpha-L-fucosidase]
[OR:Streptomyces coelicolor]
SPX16331633429462186NO-HIT6
SPX1634163442952958853723.60E-50[LN:YURM_BACSU]128
[AC:O32154]
[GN:YURM]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL ABC TRANSPORTER PERMEASE PROTEIN YURM]
[SP:O32154]
SPX1635163542963109301637.70E-27“[LN:E72357]140
[AC:E72357]
[PN:sugar ABC transporter, permease protein]
[GN:TM0596]
[CL:inner membrane protein malF]
[OR:Thermotoga maritima]”
SPX1636163642974311293845.60E-07[GI:1524333]116
[LN:SCMALREFG]
[AC:Y07706]
[PN:putative maltose-binding pootein]
[GN:malE]
[OR:Streptomyces coelicolor]
SPX16371637429846814042102.00E-81“[LN:E70014]117
[AC:E70014]
[PN:rhamnulokinase, yulC]
[GN:yulC]
[CL:rhamnulokinase]
[OR:Bacillus subtilis]
[EC:2.7.1.5]”
SPX16381638429959177NO-HIT6
SPX1639163943002587741237.20E-21[LN:SRLR_ECOLI]121
[AC:P15082:P77030]
[GN:SRLR:GUTR]
[OR:Escherichia coli]
[DE:GLUCITOL OPERON REPRESSOR]
[SP:P15082:P77030]
SPX16401640430173219NO-HIT6
SPX16411641430269207NO-HIT6
SPX164216424303502150621588.80E-289[LN:T46756]107
[AC:T46756]
[PN:Zn-binding lipoprotein adcA [imported]]
[GN:adcA]
[OR:Streptococcus pneumoniae]
SPX16431643430426980712614.10E-177[LN:T46755]101
[AC:T46755]
[PN:membrane protein adcB [imported]]
[GN:adcB]
[OR:Streptococcus pneumoniae]
SPX16441644430523570512471.40E-168[LN:T46754]92
[AC:T46754]
[PN:AdcC protein [imported]]
[GN:adcC]
[OR:Streptococcus pneumoniae]
SPX16451645430664192891.20E-06[LN:G72536]92
[AC:G72536]
[PN:hypothetical protein APE1580]
[GN:APE1580]
[OR:Aeropyrum pernix]
SPX1646164643071675017281.10E-95[LN:T46753]102
[AC:T46753]
[PN:repressor protein adcR [imported]]
[GN:adcR]
[OR:Streptococcus pneumoniae]
SPX16471647430842812846121.10E-162[GI:3403204]96
[LN:AF050517]
[AC:AF050517:S78492]
[PN:unknown]
[GN:dlt4]
[OR:Streptococcus mutans]
SPX164816484309802403608.20E-46[GI:2981430]93
[LN:AF049357]
[AC:AF049357:S78492]
[PN:Glg3]
[GN:glg3]
[OR:Streptococcus mutans]
SPX164916494310415124512362.30E-227[GI:2952530]107
[LN:AF051356]
[AC:AF051356]
[PN:integral membrane protein]
[GN:dltB]
[OR:Streptococcus mutans]
SPX165016504311517155121541.90E-292[LN:DLTA_STRMU]144
[AC:Q53526:O68576]
[GN:DLTA]
[OR:Streptococcus mutans]
[EC:6.3.2.-]
[DE:ALANYL CARRIER PROTEIN LIGASE) (DCL)]
[SP:Q53526:O68576]
SPX16511651431266198NO-HIT6
SPX1652165243131745222153.50E-24[LN:H69812]97
[AC:H69812]
[PN:conserved hypothetical protein yfmI]
[GN:yfmI]
[OR:Bacillus subtilis]
SPX165316534314237711972.60E-14[LN:H69812]97
[AC:H69812]
[PN:conserved hypothetical protein yfmI]
[GN:yfmI]
[OR:Bacillus subtilis]
SPX16541654431562186NO-HIT6
SPX16551655431663189NO-HIT6
SPX16561656431733199317122.40E-235[GI:2804734]100
[LN:AF030367]
[AC:AF030367]
[PN:maturase-related protein]
[OR:Streptococcus pneumoniae]
SPX165716574318942824706.40E-60[GI:2804734]100
[LN:AF030367]
[AC:AF030367]
[PN:maturase-related protein]
[OR:Streptococcus pneumoniae]
SPX16581658431982246NO-HIT6
SPX16591659432066198NO-HIT6
SPX166016604321196588NO-HIT6
SPX166116614322682043444.40E-42[GI:1217989]78
[LN:SPU12567]
[AC:U12567]
[PN:ORF3]
[OR:Streptococcus pneumoniae]
SPX1662166243232537599682.20E-159[LN:GLPF_STRPN]120
[AC:P52281]
[GN:GLPF]
[OR:Streptococcus pneumoniae]
[DE:GLYCEROL UPTAKE FACILITATOR PROTEIN]
[SP:P52281]
SPX166316634324609182730580[GI:3551774]154
[LN:SPU94770]
[AC:U94770]
[PN:alpha-glycerophosphate oxidase]
[GN:glpO]
[FN:oxidizes alpha-glycerophosphate to]
[OR:Streptococcus pneumoniae]
SPX1664166443251003003021.90E-38“[LN:S67936]166
[AC:S67936]
[PN:glycerol-3-phosphate dehydrogenase homolog GlpD]
[GN:glpD]
[OR:Streptococcus pneumoniae]
[SR:strain P13, , strain P13]
[SR:strain P13, ]”
SPX166516654326503150912512.90E-274“[LN:GLPK_ENTFA]147
[AC:O34154]
[GN:GLPK]
[OR:Enterococcus faecalis]
[SR:,Streptococcus faecalis]
[EC:2.7.1.30]
[DE:(GLYCEROKINASE) (GK)]
[SP:O34154]”
SPX1666166643274761428NO-HIT6
SPX16671667432866198NO-HIT6
SPX16681668432929187310632.60E-140[GI:4033717]79
[LN:SPU49397]
[AC:U49397]
[PN:unknown]
[OR:Streptococcus pyogenes]
SPX16691669433032798113034.70E-175[GI:4033718]79
[LN:SPU49397]
[AC:U49397]
[PN:unknown]
[OR:Streptococcus pyogenes]
SPX16701670433163189NO-HIT6
SPX1671167143322226662354.10E-25[GI:558538]179
[LN:SUHSAPI]
[AC:D38490]
[PN:sperm-activating peptide I precursor]
[OR:Hemicentrotus pulcherrimus]
[SR:Hemicentrotus pulcherrimus female ovary accessory cell (library]
SPX16721672433345113535006.50E-65[GI:4838563]98
[LN:AF145055]
[AC:AF145055]
[PN:surface protein C PspC]
[OR:Streptococcus pneumoniae]
SPX1673167343341835492131.70E-21[GI:7293488]106
[LN:AE003509]
[AC:AE003509:AE002593]
[GN:CG15040]
[OR:Drosophila melanogaster]
[SR:fruit fly]
SPX1674167443351765281121.00E-08[GI:406446]64
[LN:MGU02192]
[AC:U02192]
[OR:Mycoplasma genitalium]
SPX1675167543361825461071.20E-15[GI:3849798]118
[LN:U91581]
[AC:U91581:U04057]
[PN:putative transposase]
[GN:tpase]
[OR:Lactococcus lactis subsp. lactis]
SPX1676167643372517531757.10E-43[GI:6746427]90
[LN:AF179847]
[AC:AF179847]
[PN:putative transposase]
[OR:Lactococcus lactis]
SPX16771677433865195NO-HIT6
SPX167816784339551651831.50E-19[GI:2576331]112
[LN:SPSPSA2]
[AC:AJ002054]
[PN:SpsA protein]
[FN:IgA binding protein]
[OR:Streptococcus pneumoniae]
SPX167916794340419125720391.30E-284[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX16801680434123269612961.20E-171[GI:4097980]101
[LN:SPU72655]
[AC:U72655]
[PN:surface protein C]
[GN:pspC]
[OR:Streptococcus pneumoniae]
SPX168116814342110330NO-HIT6
SPX168216824343105315987.50E-05[LN:T14867]79
[AC:T14867]
[PN:interaptin]
[GN:abpD]
[OR:Dictyostelium discoideum]
SPX1683168343442176515991.00E-117[GI:6469845]93
[LN:AF068645]
[AC:AF068645]
[PN:unknown]
[GN:pspC]
[OR:Streptococcus pneumoniae]
SPX16841684434573219660.001“[GI:340613]163
[LN:LEIKPMURF2]
[AC:L07545]
[GN:MURF2]
[OR:Kinetoplast Leishmania tarentolae]
[SR:Kinetoplast Leishmania tarentolae (strain UC, organelle Kinetoplas]”
SPX168516854346105315941.40E-05“[LN:YHU3_YEAST]119
[AC:P38844]
[GN:YHR143W]
[OR:Saccharomyces cerevisiae]
[SR:,Baker′s yeast]
[DE:PRECURSOR]
[SP:P38844]”
SPX1686168643472768286977.60E-123[GI:2576333]113
[LN:SPSPSA47]
[AC:AJ002055]
[PN:SpsA protein]
[FN:IgA binding protein]
[OR:Streptococcus pneumoniae]
SPX1687168743481765283821.80E-50[LN:F81147]119
[AC:F81147]
[PN:conserved hypothetical protein NMB0883 [imported]]
[GN:NMB0883]
[OR:Neisseria meningitidis]
SPX168816884349447134112450[GI:5830533]102
[LN:SPAJ6395]
[AC:AJ006395]
[PN:histidine kinase]
[GN:hk06]
[OR:Streptococcus pneumoniae]
SPX16891689435021865411003.60E-150[GI:5830532]104
[LN:SPAJ6395]
[AC:AJ006395]
[PN:response regulator]
[GN:rr06]
[OR:Streptococcus pneumoniae]
SPX16901690435175225NO-HIT6
SPX169116914352811243311023.30E-266[GI:4103472]84
[LN:AF023422]
[AC:AF023422]
[PN:ClpC]
[GN:clpC]
[OR:Lactococcus lactis]
SPX1692169243531745223234.90E-44[LN:LLA249133]111
[AC:AJ249133]
[PN:CtsR protein]
[GN:ctsR]
[FN:transcriptional regulator]
[OR:Lactococcus lactis]
SPX1693169343542437292551.80E-47“[LN:B72369]180
[AC:B72369]
[PN:ABC transporter, ATP-binding protein]
[GN:TM0483]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Thermotoga maritima]”
SPX16941694435533610085619.10E-87[LN:C72369]93
[AC:C72369]
[PN:hypothetical protein TM0484]
[GN:TM0484]
[OR:Thermotoga maritima]
SPX169516954356136408NO-HIT6
SPX1696169643572507504401.10E-58“[LN:D72369]165
[AC:D72369]
[PN:ABC transporter, permease protein, cysTW family]
[GN:TM0485]
[CL:Synechococcus nitrate transport protein nrtB]
[OR:Thermotoga maritima]”
SPX169716974358972911184.00E-14[LN:YVI2_CLOPE]126
[AC:Q46213]
[OR:Clostridium perfringens]
[DE:HYPOTHETICAL 10.7 KD PROTEIN IN VIRR 5′REGION (ORF2)]
[SP:Q46213]
SPX1698169843592848523198.30E-35[LN:S57721]98
[AC:S57721]
[PN:cspB protein]
[CL:cpl repeat homology]
[OR:Clostridium acetobutylicum]
SPX1699169943601384141027.10E-06[GI:1340128]63
[LN:SA1234]
[AC:X97985]
[OR:Staphylococcus aureus]
SPX17001700436189267723.10E-05[LN:VEG_BACSU]87
[AC:P37466]
[GN:VEG]
[OR:Bacillus subtilis]
[DE:VEG PROTEIN]
[SP:P37466]
SPX17011701436245113538271.60E-171“[LN:DNAC_BACSU]118
[AC:P37469]
[GN:DNAC]
[OR:Bacillus subtilis]
[EC:3.6.1.-]
[DE:REPLICATIVE DNA HELICASE,]
[SP:P37469]”
SPX1702170243631514531931.20E-44[LN:RL9_BACST]118
[AC:P02417]
[GN:RPLI]
[OR:Bacillus stearothermophilus]
[DE:50S RIBOSOMAL PROTEIN L9 (BL17)]
[SP:P02417]
SPX17031703436465819743016.60E-68[LN:YYBT_BACSU]137
[AC:P37484]
[GN:YYBT]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 74.3 KD PROTEIN IN RPLI-COTF INTERGENIC REGION]
[SP:P37484]
SPX1704170443651835493585.10E-68[LN:LLA249134]78
[AC:AJ249134]
[PN:hypothetical protein]
[OR:Lactococcus lactis]
SPX1705170543662216631432.90E-23[LN:CMF3_BACSU]106
[AC:P39147]
[GN:COMFC:COMF3]
[OR:Bacillus subtilis]
[DE:COMF OPERON PROTEIN 3]
[SP:P39147]
SPX17061706436743312992692.00E-31[LN:CMF1_BACSU]106
[AC:P39145]
[GN:COMFA:COMF1]
[OR:Bacillus subtilis]
[DE:COMF OPERON PROTEIN 1]
[SP:P39145]
SPX1707170743682126364751.00E-60[LN:YVYE_BACSU]156
[AC:P32437:P96500]
[GN:YVYE:YVHK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 24.8 KD PROTEIN IN DEGS-TAGO INTERGENIC REGION]
[SP:P32437:P96500]
SPX17081708436930992712897.30E-171[GI:6567187]141
[LN:AB028865]
[AC:AB028865]
[PN:O-acetylserine lyase]
[GN:cysM]
[OR:Streptococcus suis]
[SR:Streptococcus suis (strain:SMR) DNA]
SPX17091709437034710414981.10E-82[LN:EFTS_BACSU]119
[AC:P80700:O31748]
[GN:TSF]
[OR:Bacillus subtilis]
[DE:ELONGATION FACTOR TS (EF-TS)]
[SP:P80700:O31748]
SPX171017104371129387NO-HIT6
SPX17111711437228886410131.60E-135[LN:RS2_PEDAC]108
[AC:P49668]
[GN:RPSB]
[OR:Pediococcus acidilactici]
[DE:30S RIBOSOMAL PROTEIN S2]
[SP:P49668]
SPX17121712437375225NO-HIT6
SPX17131713437439311794593.30E-76[LN:JN0097]83
[AC:JN0097]
[PN:secreted 45K protein precursor]
[OR:Lactococcus lactis]
SPX17141714437580240NO-HIT6
SPX1715171543761654951087.90E-08[LN:MRED_BACSU]117
[AC:Q01467]
[GN:MRED:RODB]
[OR:Bacillus subtilis]
[DE:ROD SHAPE-DETERMINING PROTEIN MRED]
[SP:Q01467]
SPX1716171643772738191411.60E-17[LN:MREC_BACSU]112
[AC:Q01466]
[GN:MREC]
[OR:Bacillus subtilis]
[DE:ROD SHAPE-DETERMINING PROTEIN MREC]
[SP:Q01466]
SPX1717171743782657956941.30E-95[LN:F69742]87
[AC:F69742]
[PN:hypothetical protein ybaF]
[GN:ybaF]
[OR:Bacillus subtilis]
SPX17181718437957171NO-HIT6
SPX1719171943802808406234.20E-94[LN:E69742]188
[AC:E69742]
[PN:ABC transporter (ATP-binding protein) homolog ybaE]
[GN:ybaE]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX1720172043811163481277.40E-11[LN:C71234]95
[AC:C71234]
[PN:hypothetical protein PH0133]
[GN:PH0133]
[OR:Pyrococcus horikoshii]
SPX1721172143822627868531.50E-116[GI:3426368]119
[LN:AF082738]
[AC:AF082738]
[PN:ABC transporter ATP-binding protein]
[GN:stpA]
[OR:Streptococcus pyogenes]
SPX172217224383752251061.30E-09[LN:A71007]95
[AC:A71007]
[PN:hypothetical protein PH1351]
[GN:PH1351]
[OR:Pyrococcus horikoshii]
SPX1723172343841825465316.40E-72[GI:3426367]121
[LN:AF082738]
[AC:AF082738]
[PN:phosphotidylglycerophosphate synthase]
[GN:pgsA]
[OR:Streptococcus pyogenes]
SPX1724172443852778311001.50E-21[GI:3426366]81
[LN:AF082738]
[AC:AF082738]
[PN:unknown]
[OR:Streptococcus pyogenes]
SPX17251725438642812844031.10E-102[GI:3426365]81
[LN:AF082738]
[AC:AF082738]
[PN:unknown]
[OR:Streptococcus pyogenes]
SPX17261726438741712516942.70E-103[GI:3426364]81
[LN:AF082738]
[AC:AF082738]
[PN:unknown]
[OR:Streptococcus pyogenes]
SPX1727172743881233691481.20E-26[LN:JC4754]89
[AC:JC4754]
[PN:hypothetical 13.6k protein]
[GN:recF]
[OR:Lactococcus lactis]
SPX172817284389366109811271.20E-163[LN:RECF_STRPY]95
[AC:P49999]
[GN:RECF]
[OR:Streptococcus pyogenes]
[DE:RECF PROTEIN]
[SP:P49999]
SPX172917294390493147922830[LN:IMDH_STRPY]127
[AC:P50099]
[GN:GUAB]
[OR:Streptococcus pyogenes]
[EC:1.1.1.205]
[DE:DEHYDROGENASE) (IMPDH) (IMPD)]
[SP:P50099]
SPX17301730439149147991.30E-07[LN:F71456]95
[AC:F71456]
[PN:hypothetical protein PH0308]
[GN:PH0308]
[OR:Pyrococcus horikoshii]
SPX17311731439234210266722.00E-153[LN:SYW_CLOLO]108
[AC:Q46127]
[GN:TRPS:TRSA]
[OR:Clostridium longisporum]
[EC:6.1.1.2]
[DE:(TRPRS)]
[SP:Q46127]
SPX173217324393541162313649.40E-252[LN:E69861]188
[AC:E69861]
[PN:ABC transporter (ATP-binding protein) homolog ykpA]
[GN:ykpA]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX17331733439485125535031.40E-88[GI:3043878]94
[LN:LLU95840]
[AC:U95840]
[PN:transmembrane protein Tmp5]
[OR:Lactococcus lactis]
SPX1734173443951053151815.50E-19[LN:YHGE_BACSU]144
[AC:P32399]
[GN:YHGE]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 84.1 KD PROTEIN IN HEMY-GLTT INTERGENIC REGION (ORFB)]
[SP:P32399]
SPX1735173543961133391381.10E-11[LN:YHGE_BACSU]144
[AC:P32399]
[GN:YHGE]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 84.1 KD PROTEIN IN HEMY-GLTT INTERGENIC REGION (ORFB)]
[SP:P32399]
SPX1736173643972567683072.50E-46[GI:3043882]94
[LN:LLU95842]
[AC:U95842]
[PN:transmembrane protein Tmp7]
[OR:Lactococcus lactis]
SPX173717374398181543985.30E-09[GI:6899263]113
[LN:AE002125]
[AC:AE002125:AF222894]
[PN:unique hypothetical]
[GN:UU290]
[OR:Ureaplasma urealyticum]
SPX17381738439925175312942.50E-176[GI:1613769]102
[LN:SPU33315]
[AC:U33315]
[PN:response regulator]
[GN:comE]
[OR:Streptococcus pneumoniae]
SPX173917394400442132622460[GI:1613768]108
[LN:SPU33315]
[AC:U33315]
[PN:histidine protein kinase]
[GN:comD]
[OR:Streptococcus pneumoniae]
SPX1740174044011604807814.50E-104[GI:2109449]83
[LN:SPDNAARG]
[AC:AF000658]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX174117414402398119419638.90E-259[GI:2109443]112
[LN:SPDNAARG]
[AC:AF000658]
[PN:putative serine protease]
[GN:sphtra]
[OR:Streptococcus pneumoniae]
SPX17421742440325375912255.80E-163[GI:2109444]107
[LN:SPDNAARG]
[AC:AF000658]
[PN:SPSpoJ]
[GN:spspoJ]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX174317434404454136222870[LN:DNAA_STRPN]131
[AC:O08397]
[GN:DNAA]
[OR:Streptococcus pneumoniae]
[DE:CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA]
[SP:O08397]
SPX174417444405379113718572.90E-250“[LN:DP3B_STRPN]131
[AC:O06672]
[GN:DNAN]
[OR:Streptococcus pneumoniae]
[EC:2.7.7.7]
[DE:DNA POLYMERASE III, BETA CHAIN,]
[SP:O06672]”
SPX174517454406651953391.60E-43[GI:2109447]83
[LN:SPDNAARG]
[AC:AF000658]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX17461746440737511257109.10E-176[LN:YYAF_BACSU]84
[AC:P37518]
[GN:YYAF]
[OR:Bacillus subtilis]
[DE:REGION]
[SP:P37518]
SPX1747174744081905703683.70E-62[LN:SP5C_BACSU]119
[AC:P37470]
[GN:SPOVC:PTH]
[OR:Bacillus subtilis]
[EC:3.1.1.29]
[DE:SPORULATION PROTEIN C)]
[SP:P37470]
SPX1748174844091170351020880[GI:3511015]116
[LN:AF054624]
[AC:AF054624]
[PN:transcription-repair coupling factor]
[GN:mfd]
[OR:Lactobacillus sakei]
SPX17491749441099297NO-HIT6
SPX175017504411892672753.50E-33[LN:YABO_BACSU]136
[AC:P37557]
[GN:YABO]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 9.7 KD PROTEIN IN MFD-DIVIC INTERGENIC REGION]
[SP:P37557]
SPX1751175144121233691121.50E-08[GI:4090866]97
[LN:AF023181]
[AC:AF023181]
[PN:DivIC homolog]
[GN:divL]
[OR:Listeria monocytogenes]
SPX17521752441374222NO-HIT6
SPX1753175344144461338NO-HIT6
SPX17541754441542612781286.70E-28[LN:D72358]129
[AC:D72358]
[PN:conserved hypothetical protein]
[GN:TM0579]
[CL:hypothetical protein HI0404]
[OR:Thermotoga maritima]
SPX1755175544161815433741.10E-80“[LN:HPRT_LACLA]142
[AC:Q02522]
[GN:HPT]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.4.2.8]
[DE:(HGPRTASE)]
[SP:Q02522]”
SPX175617564417653195932770[GI:5030426]112
[LN:AF061748]
[AC:AF061748]
[PN:cell division protein FtsH]
[GN:ftsH]
[OR:Streptococcus pneumoniae]
SPX1757175744182086241819.80E-25[LN:A71115]95
[AC:A71115]
[PN:hypothetical protein PH0688]
[GN:PH0688]
[OR:Pyrococcus horikoshii]
SPX17581758441936108NO-HIT6
SPX1759175944201604808449.40E-114[GI:5739312]126
[LN:AF161700]
[AC:AF161700]
[PN:ComX1]
[GN:comX1]
[FN:transcriptional regulator of]
[OR:Streptococcus pneumoniae]
SPX17601760442182246NO-HIT6
SPX17611761442250150827.60E-06[LN:G71244]95
[AC:G71244]
[PN:hypothetical protein PH0217]
[GN:PH0217]
[OR:Pyrococcus horikoshii]
SPX17621762442362186NO-HIT6
SPX176317634424872611363.90E-14[LN:G81516]130
[AC:G81516]
[PN:hypothetical protein CP0988 [imported]]
[GN:CP0988]
[OR:Chlamydophila pneumoniae:Chlamydia pneumoniae]
SPX176417644425136408NO-HIT6
SPX17651765442652156NO-HIT6
SPX17661766442752156873.30E-06[LN:D75542]90
[AC:D75542]
[PN:hypothetical protein]
[GN:DR0254]
[OR:Deinococcus radiodurans]
SPX176717674428822462471.10E-29[LN:F81737]131
[AC:F81737]
[PN:hypothetical protein TC0129 [imported]]
[GN:TC0129]
[OR:Chlamydia muridarum:Chlamydia trachomatis MoPn]
SPX176817684429782341434.90E-15[LN:F71245]95
[AC:F71245]
[PN:hypothetical protein PHS004]
[GN:PHS004]
[OR:Pyrococcus horikoshii]
SPX176917694430692073407.40E-44[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX177017704431822462561.40E-36[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX177117714432471411191.30E-09[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX177217724433912733873.30E-50[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX17731773443481243NO-HIT6
SPX177417744435443132917392.60E-235“[LN:A42280]175
[AC:S65968:A42280:H69683]
[PN:adenylosuccinate synthase, purA:IMP--aspartate ligase]
[GN:purA]
[CL:adenylosuccinate synthase]
[OR:Bacillus subtilis]
[EC:6.3.4.4]”
SPX1775177544361414233651.90E-46[LN:YAAJ_BACSU]137
[AC:P21335]
[GN:YAAJ]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 17.8 KD PROTEIN IN SERS-DNAH INTERGENIC REGION]
[SP:P21335]
SPX1776177644371484442052.80E-38[GI:2765131]76
[LN:LLABIKORF]
[AC:Y11901]
[PN:dUTPase]
[OR:Lactococcus lactis]
SPX177717774438186558NO-HIT6
SPX17781778443968204NO-HIT6
SPX177917794440455136511671.60E-201[LN:RADA_BACSU]146
[AC:P37572]
[GN:RADA:SMS]
[OR:Bacillus subtilis]
[DE:DNA REPAIR PROTEIN RADA HOMOLOG (DNA REPAIR PROTEIN SMS HOMOLOG)]
[SP:P37572]
SPX178017804441207621NO-HIT6
SPX1781178144421664982682.80E-38[LN:Y023_MYCTU]130
[AC:Q10612]
[GN:MTCY373.03]
[OR:Mycobacterium tuberculosis]
[DE:HYPOTHETICAL 18.2 KD PROTEIN CY373.03]
[SP:Q10612]
SPX178217824443264792NO-HIT6
SPX1783178344443239696079.40E-148[GI:532204]118
[LN:LISTMS]
[AC:M92842]
[GN:prs]
[OR:Listeria monocytogenes]
[SR:Listeria monocytogenes (strain L028) DNA]
SPX1784178444451604804933.90E-65[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX178517854446113339NO-HIT6
SPX178617864447122366NO-HIT6
SPX178717874448131393NO-HIT6
SPX178817884449118354NO-HIT6
SPX178917894450890267044120“[LN:DPO1_STRPN]125
[AC:P13252]
[GN:POLA]
[OR:Streptococcus pneumoniae]
[EC:2.7.7.7]
[DE:DNA POLYMERASE I, (POL I)]
[SP:P13252]”
SPX1790179044511243721813.30E-32[LN:B69892]128
[AC:B69892]
[PN:conserved hypothetical protein yneT]
[GN:yneT]
[CL:hypothetical protein yneT]
[OR:Bacillus subtilis]
SPX1791179144521374113282.80E-41[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX179217924453105315830.00036[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX1793179344542397173983.00E-50[LN:YOR3_BACCE]104
[AC:O31352]
[OR:Bacillus cereus]
[DE:HYPOTHETICAL PROTEIN (ORF3) (FRAGMENT)]
[SP:O31352]
SPX1794179444551715132125.40E-30[LN:YF05_METTH]128
[AC:O27549]
[GN:MTH1505]
[OR:Methanobacterium thermoautotrophicum]
[DE:HYPOTHETICAL PROTEIN MTH1505]
[SP:O27549]
SPX179517954456126378NO-HIT6
SPX1796179644571675014562.50E-57[LN:RL10_BACSU]111
[AC:P42923]
[GN:RPLJ]
[OR:Bacillus subtilis]
[DE:(VEGETATIVE PROTEIN 300) (VEG300)]
[SP:P42923]
SPX1797179744581233692551.30E-46“[LN:RL7_MICLU]150
[AC:P02395]
[GN:RPLL]
[OR:Micrococcus luteus]
[SR:,Micrococcus lysodeikticus]
[DE:50S RIBOSOMAL PROTEIN L7/L12 (MA1/MA2)]
[SP:P02395]”
SPX179817984459115345981.30E-05[LN:T40374]92
[AC:T40374]
[PN:hypothetical protein SPBC3D6.14c]
[OR:Schizosaccharomyces pombe]
SPX179917994460196588NO-HIT6
SPX18001800446150515152141.60E-47[LN:T35180]160
[AC:T35180]
[PN:hypothetical protein SC5A7.31]
[GN:SC5A7.31]
[CL:Streptomyces coelicolor hypothetical protein SC5A7.31]
[OR:Streptomyces coelicolor]
SPX1801180144621985941366.60E-20[GI:290801]133
[LN:FRNVALAB]
[AC:L17003]
[GN:valA]
[OR:Francisella tularensis var. novicida]
[SR:Francisella novicida (strain U112) DNA]
SPX18021802446397291NO-HIT6
SPX1803180344642477413571.50E-55[GI:7288062]139
[LN:SCD40A]
[AC:AL161691]
[PN:putative ABC-transporter ATP-binding protein]
[GN:SCD40A.12c]
[OR:Streptomyces coelicolor A3(2)]
SPX18041804446560180NO-HIT6
SPX180518054466129387906.90E-06[LN:F72598]92
[AC:F72598]
[PN:hypothetical protein APE1254]
[GN:APE1254]
[OR:Aeropyrum pernix]
SPX1806180644674401320NO-HIT6
SPX18071807446860180NO-HIT6
SPX18081808446974222NO-HIT6
SPX180918094470451351093.10E-09“[LN:Y4PE_RHISN]138
[AC:P55614]
[GN:Y4PE,Y4SA]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:HYPOTHETICAL 15.5 KD PROTEIN Y4PE/Y4SA]
[SP:P55614]”
SPX181018104471882643014.50E-37[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX1811181144722336993312.60E-64“[LN:C70180]125
[AC:C70180]
[PN:conserved hypothetical protein BB0644]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX181218124473308924984.30E-21[LN:I40867]80
[AC:I40867]
[PN:hypothetical protein 2]
[OR:Clostridium perfringens]
SPX18131813447454316291023.10E-21[LN:B71130]143
[AC:B71130]
[PN:probable oligopeptide binding protein APPA]
[GN:PH0807]
[CL:dipeptide transport protein]
[OR:Pyrococcus horikoshii]
SPX1814181444753179513352.30E-78“[LN:D75202]166
[AC:D75202]
[PN:dipeptide abc transporter, dipeptide-binding protein PAB0092]
[GN:dppB-1:PAB0092]
[CL:transmembrane protein dppB]
[OR:Pyrococcus abyssi]”
SPX1815181544762968886425.70E-87[LN:APPC_BACSU]122
[AC:P42063]
[GN:APPC]
[OR:Bacillus subtilis]
[DE:OLIGOPEPTIDE TRANSPORT PERMEASE PROTEIN APPC]
[SP:P42063]
SPX181618164477204612NO-HIT6
SPX18171817447866119836441.60E-146[LN:YLIA_ECOLI]130
[AC:P75796]
[GN:YLIA]
[OR:Escherichia coli]
[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YLIA]
[SP:P75796]
SPX18181818447966198NO-HIT6
SPX1819181944804701410NO-HIT6
SPX1820182044811634894508.60E-58[LN:YUTG_BACSU]136
[AC:O32124]
[GN:YUTG]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 18.7 KD PROTEIN IN HOM-MRGA INTERGENIC REGION]
[SP:O32124]
SPX1821182144821364081901.30E-38“[LN:CDD_BACSU]142
[AC:P19079]
[GN:CDD]
[OR:Bacillus subtilis]
[EC:3.5.4.5]
[DE:CYTIDINE DEAMINASE, (CYTIDINE AMINOHYDROLASE) (CDA)]
[SP:P19079]”
SPX18221822448395285NO-HIT6
SPX1823182344842748227711.10E-101[GI:2385360]100
[LN:CTSIALIDA]
[AC:Y08695]
[PN:putative acylneuraminate lyase]
[OR:Clostridium tertium]
SPX182418244485682041731.10E-18[LN:S43901]87
[AC:S43901:S27537]
[PN:hypothetical protein A]
[OR:Clostridium perfringens]
SPX1825182544861735191453.80E-20[GI:2668605]82
[LN:AF015453]
[AC:AF015453]
[PN:unknown]
[OR:Lactobacillus rhamnosus]
SPX1826182644872146425097.20E-64[GI:6318176]131
[LN:BSP250862]
[AC:AJ250862]
[PN:MrsT protein]
[GN:mrsT]
[FN:putative ABC-transporter]
[OR:Bacillus sp. HIL-Y85/54728]
SPX18271827448863189NO-HIT6
SPX18281828448944913477315.00E-191[GI:3702805]121
[LN:AF056335]
[AC:AF056335]
[PN:NADP-specific glutamate dehydrogenase]
[GN:gdhA]
[OR:Bacillus licheniformis]
SPX182918294490138414996.40E-06[LN:S31840]82
[AC:S31840]
[PN:probable transposase]
[OR:Bacillus stearothermophilus]
SPX18301830449157171943.30E-07“[LN:Y4PE_RHISN]138
[AC:P55614]
[GN:Y4PE,Y4SA]
[OR:Rhizobium sp]
[SR:,strain NGR234]
[DE:HYPOTHETICAL 15.5 KD PROTEIN Y4PE/Y4SA]
[SP:P55614]”
SPX1831183144922186541541.00E-20[GI:722339]100
[LN:AXU22323]
[AC:U22323]
[PN:unknown]
[OR:Acetobacter xylinus]
[SR:Acetobacter xylinum]
SPX18321832449373219NO-HIT6
SPX183318334494952851468.10E-34[GI:4193373]105
[LN:AF072894]
[AC:AF072894]
[PN:ribosomal protein L31]
[GN:rpmE]
[OR:Listeria monocytogenes]
SPX1834183444953129363977.80E-97[LN:F69999]150
[AC:F69999]
[PN:conserved hypothetical protein ytqI]
[GN:ytqI]
[CL:Mycoplasma conserved hypothetical protein MG190]
[OR:Bacillus subtilis]
SPX1835183544961454352712.00E-32[LN:FLAV_BACSU]99
[AC:O34737]
[GN:YKUN]
[OR:Bacillus subtilis]
[DE:PROBABLE FLAVODOXIN 1]
[SP:O34737]
SPX183618364497892671172.80E-11[LN:Y246_METJA]114
[AC:Q57696]
[GN:MJ0246]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL PROTEIN MJ0246]
[SP:Q57696]
SPX1837183744981253751695.60E-18[LN:C75108]118
[AC:C75108]
[PN:crcb protein PAB1925]
[GN:PAB1925]
[CL:hypothetical protein MJ1523]
[OR:Pyrococcus abyssi]
SPX183818384499110330931.20E-10[LN:B71026]128
[AC:B71026]
[PN:hypothetical protein PH1502]
[GN:PH1502]
[CL:hypothetical protein MJ1523]
[OR:Pyrococcus horikoshii]
SPX1839183945001163485374.70E-71[LN:RL19_STRTR]112
[AC:O34031]
[GN:RPLS]
[OR:Streptococcus thermophilus]
[DE:50S RIBOSOMAL PROTEIN L19]
[SP:O34031]
SPX1840184045012698073542.70E-85[LN:YIDA_ECOLI]150
[AC:P09997:P76737]
[GN:YIDA]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 29.7 KD PROTEIN IN IBPA-GYRB INTERGENIC REGION]
[SP:P09997:P76737]
SPX18411841450244813445612.90E-126[LN:YWFO_BACSU]130
[AC:P39651]
[GN:YWFO:IPA-93D]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 51.0 KD PROTEIN IN PTA 3′REGION]
[SP:P39651]
SPX184218424503126378NO-HIT6
SPX1843184345041113334993.70E-65[GI:1850606]97
[LN:SMU88582]
[AC:U88582]
[PN:YlxM]
[GN:ylxM]
[FN:unknown]
[OR:Streptococcus mutans]
SPX184418444505185555NO-HIT6
SPX184518454506524157219935.90E-290[LN:SR54_STRMU]150
[AC:Q54431:P96469]
[GN:FFH]
[OR:Streptococcus mutans]
[DE:SIGNAL RECOGNITION PARTICLE PROTEIN (FIFTY-FOUR HOMOLOG)]
[SP:Q54431:P96469]
SPX184618464507163489NO-HIT6
SPX1847184745082577715001.10E-87[LN:PYRP_BACCL]118
[AC:P41006]
[GN:PYRP]
[OR:Bacillus caldolyticus]
[DE:URACIL PERMEASE (URACIL TRANSPORTER)]
[SP:P41006]
SPX1848184845091474412315.00E-42[LN:LLA132624]86
[AC:AJ132624]
[PN:uracil transporter]
[GN:pyrP]
[OR:Lactococcus lactis]
SPX1849184945102387143533.70E-81[LN:GIDB_BACSU]114
[AC:P25813]
[GN:GIDB]
[OR:Bacillus subtilis]
[DE:GLUCOSE INHIBITED DIVISION PROTEIN B]
[SP:P25813]
SPX1850185045111875612611.60E-57[GI:1519287]86
[LN:LMU66186]
[AC:U66186]
[PN:LemA]
[GN:lemA]
[OR:Listeria monocytogenes]
SPX1851185145123039097571.70E-165[LN:HTPX_STRGC]123
[AC:O30795]
[GN:HTPX]
[OR:Streptococcus gordonii challis]
[DE:PUTATIVE HEAT SHOCK PROTEIN HTPX]
[SP:O30795]
SPX18521852451352015601971.40E-47[LN:YHES_ECOLI]130
[AC:P45535]
[GN:YHES]
[OR:Escherichia coli]
[DE:HYPOTHETICAL ABC TRANSPORTER ATP-BINDING PROTEIN YHES]
[SP:P45535]
SPX18531853451492276NO-HIT6
SPX185418544515122366NO-HIT6
SPX185518554516181543646.40E-07[LN:C69875]87
[AC:C69875]
[PN:hypothetical protein ylbN]
[GN:ylbN]
[OR:Bacillus subtilis]
SPX18561856451762186NO-HIT6
SPX1857185745182106304462.10E-57[LN:END3_BACSU]122
[AC:P39788]
[GN:NTH:JOOB]
[OR:Bacillus subtilis]
[EC:4.2.99.18]
[DE:APYRIMIDINIC SITE) LYASE)]
[SP:P39788]
SPX1858185845191745226264.30E-82[LN:LLA132624]141
[AC:AJ132624]
[PN:pyrimidine regulatory protein]
[GN:pyrR]
[FN:Regulates expression of the pyrimidine]
[OR:Lactococcus lactis]
SPX1859185945203089249426.40E-134[LN:LLA132624]95
[AC:AJ132624]
[PN:aspartate transcarbamoylase]
[GN:pyrB]
[OR:Lactococcus lactis]
SPX186018604521360108014922.60E-202[LN:LLA132624]112
[AC:AJ132624]
[PN:carbamoyl phosphate synthetase small subunit]
[GN:carA]
[OR:Lactococcus lactis]
SPX1861186145221059317740000[GI:2598551]108
[LN:LLAJ109]
[AC:AJ000109]
[PN:carbamoylphosphate synthetase]
[GN:carB]
[OR:Lactococcus lactis]
SPX18621862452370210NO-HIT6
SPX18631863452428184314251.90E-195[GI:5001693]92
[LN:AF106539]
[AC:AF106539]
[PN:LicD2]
[GN:licD2]
[OR:Streptococcus pneumoniae]
SPX18641864452526880414196.40E-194[GI:5001692]92
[LN:AF106539]
[AC:AF106539]
[PN:LicD1]
[GN:licD1]
[OR:Streptococcus pneumoniae]
SPX186518654526496148824830[GI:5001691]83
[LN:AF106539]
[AC:AF106539]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX186618664527236708967.30E-17[LN:S60902]100
[AC:S60902:S49238:S44071]
[PN:CDP-ribitol pyrophosphorylase]
[OR:Haemophilus influenzae]
SPX1867186745283471041666.20E-05[LN:YJJN_ECOLI]94
[AC:P39400]
[GN:YJJN]
[OR:Escherichia coli]
[DE:INTERGENIC REGION]
[SP:P39400]
SPX18681868452929087013612.10E-181[GI:2708632]99
[LN:AF036951]
[AC:AF036951]
[PN:choline kinase]
[GN:pck]
[OR:Streptococcus pneumoniae]
SPX1869186945302938791561.70E-15[LN:LICB_HAEIN]130
[AC:P14182:Q57357:O05075]
[GN:LICB:HI1538]
[OR:Haemophilus influenzae]
[DE:LICB PROTEIN]
[SP:P14182:Q57357:O05075]
SPX1870187045312306903454.10E-54[LN:D64128]82
[AC:D64128]
[PN:lic-1 protein C]
[GN:licC]
[OR:Haemophilus influenzae]
SPX1871187145322838494588.00E-59[LN:C72399]88
[AC:C72399]
[PN:DNA processing chain A]
[GN:TM0250]
[OR:Thermotoga maritima]
SPX1872187245331715133095.10E-41[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX1873187345341524561071.30E-07[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX18741874453569207NO-HIT6
SPX18751875453634810441792.10E-23[LN:Y678_METJA]114
[AC:Q58091]
[GN:MJ0678]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL PROTEIN MJ0678]
[SP:Q58091]
SPX187618764537702210610650[LN:TOP1_BACSU]128
[AC:P39814]
[GN:TOPA:TOPI]
[OR:Bacillus subtilis]
[EC:5.99.1.2]
[DE:(UNTWISTING ENZYME) (SWIVELASE)]
[SP:P39814]
SPX1877187745381203602084.20E-25[LN:YBAN_ECOLI]149
[AC:P45808:P77478]
[GN:YBAN]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 14.8 KD PROTEIN IN PRIC-APT INTERGENIC REGION]
[SP:P45808:P77478]
SPX1878187845392116331812.30E-34[GI:4680703]89
[LN:AF132966]
[AC:AF132966]
[PN:CGI-32 protein]
[OR:Homo sapiens]
[SR:human]
SPX1879187945402196571423.40E-22[LN:YYAQ_BACSU]137
[AC:P37507]
[GN:YYAQ]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 13.9 KD PROTEIN IN COTF-TETB INTERGENIC REGION]
[SP:P37507]
SPX1880188045412116335961.30E-93[GI:2565151]96
[LN:LLU92974]
[AC:U92974:M90760:M90761]
[PN:LeuA]
[GN:leuA]
[OR:Lactococcus lactis]
SPX18811881454270210NO-HIT6
SPX1882188245431454353086.00E-39“[LN:LEU1_LACLA]166
[AC:Q02141]
[GN:LEUA]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.1.3.12]
[DE:SYNTHASE) (ALPHA-IPM SYNTHETASE)]
[SP:Q02141]”
SPX18831883454434610386084.50E-153“[LN:LEU3_LACLA]151
[AC:Q02143]
[GN:LEUB]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:1.1.1.85]
[DE:(IMDH) (3-IPM-DH)]
[SP:Q02143]”
SPX188418844545902701298.30E-13[LN:G69983]87
[AC:G69983]
[PN:hypothetical protein ysdA]
[GN:ysdA]
[OR:Bacillus subtilis]
SPX1885188545461203603739.40E-47“[LN:LEUD_LACLA]183
[AC:Q02144]
[GN:LEUD]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:4.2.1.33]
[DE:(ISOPROPYLMALATE ISOMERASE) (ALPHA-IPM ISOMERASE)]
[SP:Q02144]”
SPX18861886454779237NO-HIT6
SPX18871887454889267NO-HIT6
SPX18881888454964519351381.60E-33“[LN:MCRB_ECOLI]145
[AC:P15005]
[GN:MCRB:RGLB]
[OR:Escherichia coli]
[EC:3.1.21.-]
[DE:5-METHYLCYTOSINE-SPECIFIC RESTRICTION ENZYME B,]
[SP:P15005]”
SPX1889188945504481344964.40E-09[LN:D81431]105
[AC:D81431]
[PN:hypothetical protein Cj0140 [imported]]
[GN:Cj0140]
[OR:Campylobacter jejuni]
SPX1890189045513299879131.40E-171“[LN:C70015]237
[AC:C70015]
[PN:probable GMP reductase, yumD:guanosine monophosphate reductase]
[GN:yumD]
[CL:GMP reductase:IMP dehydrogenase amino-terminal homology:IMP dehydrogenase catalytic homology]
[OR:Bacillus subtilis]
[EC:1.6.6.8]”
SPX18911891455278234NO-HIT6
SPX18921892455367201NO-HIT6
SPX1893189345542336995381.70E-69“[LN:B69693]188
[AC:B69693:JC4821]
[PN:ribonuclease III,:RNase D:RNase O]
[GN:rncS:srb]
[CL:ribonuclease III:double-stranded RNA-binding repeat homology]
[OR:Bacillus subtilis]
[EC:3.1.26.3]”
SPX189418944555737221112587.10E-169[LN:G69708]189
[AC:G69708:JC4819:PC4029]
[PN:chromosome segregation SMC protein:minichromosome stabilizing protein SMC]
[GN:smc]
[CL:conserved hypothetical P115 protein]
[OR:Bacillus subtilis]
SPX1895189545562176511392.70E-09[GI:2246532]148
[LN:U93872]
[AC:U93872]
[OR:Kaposi′s sarcoma-associated herpesvirus]
[SR:Kaposi′s sarcoma-associated herpesvirus - Human herpesvirus 8]
SPX189618964557102306950.00014[LN:P115_MYCHR]83
[AC:P41508]
[OR:Mycoplasma hyorhinis]
[DE:P115 PROTEIN]
[SP:P41508]
SPX1897189745581965884282.90E-69[LN:G69708]189
[AC:G69708:JC4819:PC4029]
[PN:chromosome segregation SMC protein:minichromosome stabilizing protein SMC]
[GN:smc]
[CL:conserved hypothetical P115 protein]
[OR:Bacillus subtilis]
SPX1898189845592657952064.40E-31“[GI:4062428]178
[LN:D90722]
[AC:D90722:AB001340]
[PN:Hypothetical 30.2 kd protein in idh-deoR]
[OR:Escherichia coli]
[SR:Escherichia coli(strain:K12) DNA, clone:Kohara clone #209]”
SPX1899189945602738192203.10E-42[LN:YIDA_ECOLI]150
[AC:P09997:P76737]
[GN:YIDA]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 29.7 KD PROTEIN IN IBPA-GYRB INTERGENIC REGION]
[SP:P09997:P76737]
SPX19001900456143012906751.30E-113[GI:2633967]184
[LN:BSUB0009]
[AC:Z99112:AL009126]
[PN:signal recognition particle (docking protein)]
[GN:ftsY]
[FN:involved in secretion of extracellular proteins]
[OR:Bacillus subtilis]
SPX190119014562419125720391.30E-284[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX190219024563852553502.40E-45[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX1903190345641093272881.40E-35[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX1904190445651735198585.70E-116[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX19051905456649614887796.50E-166[LN:G6PD_BACSU]110
[AC:P54547]
[GN:ZWF]
[OR:Bacillus subtilis]
[EC:1.1.1.49]
[DE:PROTEIN 11) (VEG11)]
[SP:P54547]
SPX1906190645672477417724.80E-102[LN:H69334]162
[AC:H69334]
[PN:glutamine transport protein glnQ]
[GN:glnQ]
[CL:inner membrane protein malK:ATP-binding cassette homology]
[OR:Archaeoglobus fulgidus]
SPX19071907456849314795082.50E-80[GI:6560693]148
[LN:AF141644]
[AC:AF141644]
[PN:putative integral membrane protein]
[FN:putative inner membrane component of a]
[OR:Lactococcus lactis]
SPX190819084569237711910.00087“[LN:S76167]116
[AC:S76167]
[PN:hypothetical protein]
[OR:Synechocystis sp.]
[SR:PCC 6803, , PCC 6803]
[SR:PCC 6803, ]”
SPX19091909457090270804.20E-05[LN:T34651]102
[AC:T34651]
[PN:probable transmembrane protein]
[GN:SC1A9.02]
[OR:Streptomyces coelicolor]
SPX191019104571663198933500[LN:UVRB_STRPN]118
[AC:Q54986]
[GN:UVRB:UVS402]
[OR:Streptococcus pneumoniae]
[DE:EXCINUCLEASE ABC SUBUNIT B]
[SP:Q54986]
SPX1911191145721885641103.20E-15[LN:G75474]96
[AC:G75474]
[PN:probable acetyltransferase]
[GN:DR0796]
[OR:Deinococcus radiodurans]
SPX191219124573130390651.50E-06[LN:T39482]169
[AC:T39482]
[PN:N-acetyltransferase]
[GN:SPBC15D4.06]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]
[OR:Schizosaccharomyces pombe]
SPX1913191345741564681103.50E-09[LN:G70031]121
[AC:G70031]
[PN:mutator MutT protein homolog yvcI]
[GN:yvcI]
[CL:mutT domain homology]
[OR:Bacillus subtilis]
SPX1914191445751725162067.90E-37“[LN:F72234]116
[AC:F72234]
[PN:transcription regulator, biotin repressor family]
[GN:TM1602]
[OR:Thermotoga maritima]”
SPX191519154576194582NO-HIT6
SPX191619164577167501814.70E-09[GI:806536]92
[LN:BAMALAMYA]
[AC:Z22520]
[PN:membrane protein]
[OR:Bacillus acidopullulyticus]
SPX1917191745781845524652.50E-59[LN:DFP_STRMU]138
[AC:Q54433]
[GN:DFP]
[OR:Streptococcus mutans]
[DE:DNA/PANTOTHENATE METABOLISM FLAVOPROTEIN HOMOLOG (FRAGMENT)]
[SP:Q54433]
SPX1918191845792537591202.90E-19[LN:D69029]230
[AC:D69029]
[PN:pantothenate metabolism flavoprotein dfp homolog MTH1216:probable aspartate 1-decarboxylase activase]
[GN:MTH1216]
[CL:pantothenate metabolism flavoprotein dfp]
[OR:Methanobacterium thermoautotrophicum]
SPX191919194580181543NO-HIT6
SPX192019204581557167124750[LN:FTHS_STRMU]132
[AC:Q59925:Q59926]
[GN:FHS]
[OR:Streptococcus mutans]
[EC:6.3.4.3]
[DE:SYNTHETASE) (FHS) (FTHFS)]
[SP:Q59925:Q59926]
SPX192119214582802401459.20E-16[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX19221922458339211769894.20E-132[GI:6782414]166
[LN:SPN271596]
[AC:AJ271596]
[PN:A/G specific adenine glycosylase]
[GN:mutY]
[FN:antimutator prevents C to A transversions]
[OR:Streptococcus pneumoniae]
SPX19231923458423570511949.00E-161[GI:5830523]104
[LN:SPAJ6392]
[AC:AJ006392]
[PN:response regulator]
[GN:rr02]
[OR:Streptococcus pneumoniae]
SPX192419244585452135622490[GI:5830524]102
[LN:SPAJ6392]
[AC:AJ006392]
[PN:histidine kinase]
[GN:hk02]
[OR:Streptococcus pneumoniae]
SPX19251925458627081013795.30E-185[GI:6689278]112
[LN:SPN012049]
[AC:AJ012049]
[PN:VicX protein]
[GN:vicX]
[FN:unknown]
[OR:Streptococcus pneumoniae]
SPX19261926458781243NO-HIT6
SPX19271927458888264931.90E-06[LN:D70886]100
[AC:D70886]
[PN:hypothetical protein Rv2866]
[GN:Rv2866]
[OR:Mycobacterium tuberculosis]
SPX1928192845892587741623.00E-20[LN:C72692]98
[AC:C72692]
[PN:probable potassium channel APE0955]
[GN:APE0955]
[OR:Aeropyrum pernix]
SPX192919294590170510NO-HIT6
SPX19301930459133399916529.40E-223[GI:2275101]146
[LN:SPR6LDH]
[AC:AJ000336]
[PN:L-lactate dehydrogenase]
[GN:ldh]
[FN:conversion of pyruvate to lactate]
[OR:Streptococcus pneumoniae]
SPX19311931459231694816173.30E-219“[LN:GYRA_STRPN]150
[AC:P72524:Q54716:P72536]
[GN:GYRA]
[OR:Streptococcus pneumoniae]
[EC:5.99.1.3]
[DE:DNA GYRASE SUBUNIT A,]
[SP:P72524:Q54716:P72536]”
SPX1932193245931193572147.70E-24“[LN:GYRA_STRPN]150
[AC:P72524:Q54716:P72536]
[GN:GYRA]
[OR:Streptococcus pneumoniae]
[EC:5.99.1.3]
[DE:DNA GYRASE SUBUNIT A,]
[SP:P72524:Q54716:P72536]”
SPX193319334594507152123000[GI:4138535]105
[LN:SPN5815]
[AC:AJ005815]
[PN:DNA gyrase subunit A]
[GN:gyrA]
[OR:Streptococcus pneumoniae]
SPX1934193445952487442995.50E-36[GI:488339]153
[LN:SYNGIP3124]
[AC:M77279]
[PN:alpha-amylase]
[OR:unidentified cloning vector]
[SR:Cloning vector (sub_species Cloning vector pGIP3124) DNA]
SPX1935193545962667981846.20E-26[GI:4433636]132
[LN:AF029224]
[AC:AF029224:AF029225]
[PN:NirC]
[GN:nirC]
[FN:putative nitrite transporter]
[OR:Staphylococcus carnosus]
SPX19361936459737211164266.30E-115“[LN:T44655]186
[AC:T44655]
[PN:O-acetylhomoserine (thiol)-lyase, [imported]
:O-acetylhomoserine sulfhydrylase]
[CL:O-succinylhomoserine (thiol)-lyase]
[OR:Leptospira meyeri]
[EC:4.2.99.10]”
SPX19371937459842512751014.30E-18[GI:6899348]116
[LN:AE002133]
[AC:AE002133:AF222894]
[PN:conserved hypothetical]
[GN:UU367]
[OR:Ureaplasma urealyticum]
SPX1938193845992938796615.10E-86[LN:TRUB_BACSU]103
[AC:P32732]
[GN:TRUB]
[OR:Bacillus subtilis]
[EC:4.2.1.70]
[DE:HYDROLYASE)]
[SP:P32732]
SPX193919394600101303NO-HIT6
SPX1940194046012397177073.50E-93[LN:G69728]99
[AC:G69728]
[PN:uridine kinase udk]
[GN:udk]
[CL:uridine kinase]
[OR:Bacillus subtilis]
SPX19411941460244713416331.60E-115[LN:EX7L_BACSU]110
[AC:P54521]
[GN:YQIB]
[OR:Bacillus subtilis]
[EC:3.1.11.6]
[DE:VII LARGE SUBUNIT)]
[SP:P54521]
SPX194219424603712131133.50E-10[LN:EX7S_ECOLI]105
[AC:P22938]
[GN:XSEB]
[OR:Escherichia coli]
[EC:3.1.11.6]
[DE:SMALL SUBUNIT)]
[SP:P22938]
SPX1943194346042928765351.30E-78“[LN:ISPA_MICLU]140
[AC:O66126]
[GN:FPS]
[OR:Micrococcus luteus]
[SR:,Micrococcus lysodeikticus]
[EC:2.5.1.10]
[DE:(FPP SYNTHASE)]
[SP:O66126]”
SPX1944194446052467383531.20E-79[LN:YQXC_BACSU]142
[AC:P19672]
[GN:YQXC:YQIF]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 29.7 KD PROTEIN IN FOLD-AHRC INTERGENIC REGION]
[SP:P19672]
SPX1945194546061444321824.10E-26[GI:4127534]133
[LN:BSAJ10954]
[AC:AJ010954]
[PN:arginine repressor]
[GN:argR]
[FN:ADN binding protein]
[OR:Bacillus stearothermophilus]
SPX1946194646072988943174.20E-76[LN:RECN_BACSU]141
[AC:P17894:P19671]
[GN:RECN]
[OR:Bacillus subtilis]
[DE:DNA REPAIR PROTEIN RECN (RECOMBINATION PROTEIN N)]
[SP:P17894:P19671]
SPX1947194746082617833953.20E-68[LN:RECN_BACSU]141
[AC:P17894:P19671]
[GN:RECN]
[OR:Bacillus subtilis]
[DE:DNA REPAIR PROTEIN RECN (RECOMBINATION PROTEIN N)]
[SP:P17894:P19671]
SPX194819484609243729974.90E-15[GI:2352096]69
[LN:U97022]
[AC:U97022]
[OR:Fervidobacterium islandicum]
SPX194919494610345103512849.40E-173[LN:LEPA_BACSU]102
[AC:P37949]
[GN:LEPA]
[OR:Bacillus subtilis]
[DE:GTP-BINDING PROTEIN LEPA]
[SP:P37949]
SPX19501950461130491211581.80E-156[LN:LEPA_BACSU]102
[AC:P37949]
[GN:LEPA]
[OR:Bacillus subtilis]
[DE:GTP-BINDING PROTEIN LEPA]
[SP:P37949]
SPX195119514612111333957.80E-05“[LN:T04991]110
[AC:T04991]
[PN:hypothetical protein T16L1.230]
[OR:Arabidopsis thaliana]
[SR:, mouse-ear cress]”
SPX1952195246131123362943.40E-35[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX19531953461496288NO-HIT6
SPX195419544615230690703.10E-05[LN:G75468]90
[AC:G75468]
[PN:hypothetical protein]
[GN:DR0857]
[OR:Deinococcus radiodurans]
SPX19551955461660180NO-HIT6
SPX19561956461782246NO-HIT6
SPX19571957461870210NO-HIT6
SPX195819584619682041383.20E-14“[LN:LAFX_LACJO]132
[AC:Q48509]
[GN:LAFX]
[OR:Lactobacillus johnsonii]
[DE:BACTERIOCIN LACTACIN F, SUBUNIT LAFX PRECURSOR]
[SP:Q48509]”
SPX195919594620852551148.90E-21[GI:5441255]144
[LN:AB029612]
[AC:AB029612]
[PN:gassericin T1]
[GN:gatA]
[OR:Lactobacillus gasseri]
[SR:Lactobacillus gasseri (strain:SBT2055) DNA]
SPX19601960462156168790.00078[GI:6751696]98
[LN:ATAC018908]
[AC:AC018908]
[GN:T7P1.21]
[OR:Arabidopsis thaliana]
[SR:thale cress]
SPX1961196146221825463792.90E-48[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX1962196246231333993648.90E-50[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX19631963462455165NO-HIT6
SPX19641964462568204NO-HIT6
SPX19651965462669207NO-HIT6
SPX19661966462768204550.00018[GI:6457574]106
[LN:AF200347]
[AC:AF200347]
[PN:lactocin 705 beta-subunit precursor]
[OR:Lactobacillus casei]
SPX19671967462873219NO-HIT6
SPX196819684629718215422690[LN:COMA_STRPN]119
[AC:Q03727]
[GN:COMA]
[OR:Streptococcus pneumoniae]
[DE:TRANSPORT ATP-BINDING PROTEIN COMA]
[SP:Q03727]
SPX19691969463083249800.00032[LN:G72510]92
[AC:G72510]
[PN:hypothetical protein APE2061]
[GN:APE2061]
[OR:Aeropyrum pernix]
SPX19701970463145413626977.40E-90[GI:1698422]129
[LN:SGU40139]
[AC:U40139]
[PN:ComB]
[GN:comB]
[OR:Streptococcus gordonii]
[SR:Streptococcus gordonii strain=Challis]
SPX19711971463267201NO-HIT6
SPX197219724633110330NO-HIT6
SPX197319734634447134120621.10E-288[GI:5830551]102
[LN:SPAJ6401]
[AC:AJ006401]
[PN:histidine kinase]
[GN:hk13]
[OR:Streptococcus pneumoniae]
SPX1974197446352156459723.30E-133[GI:5830550]104
[LN:SPAJ6401]
[AC:AJ006401]
[PN:response regulator]
[GN:rr13]
[OR:Streptococcus pneumoniae]
SPX197519754636611832394.40E-28[GI:5830550]104
[LN:SPAJ6401]
[AC:AJ006401]
[PN:response regulator]
[GN:rr13]
[OR:Streptococcus pneumoniae]
SPX197619764637113339690.000063[GI:1495671]107
[LN:LPATOVGNS]
[AC:X94434]
[PN:response regulator PlnC]
[GN:plnC]
[OR:Lactobacillus plantarum]
SPX197719774638110330NO-HIT6
SPX19781978463969207NO-HIT6
SPX1979197946403249721504.10E-24[LN:ECSB_BACSU]95
[AC:P55340]
[GN:ECSB:PRST]
[OR:Bacillus subtilis]
[DE:PROTEIN ECSB]
[SP:P55340]
SPX19801980464174222NO-HIT6
SPX1981198146421153453334.00E-42[LN:ECSA_BACSU]128
[AC:P55339]
[GN:ECSA:PRST]
[OR:Bacillus subtilis]
[DE:ABC-TYPE TRANSPORTER ATP-BINDING PROTEIN ECSA]
[SP:P55339]
SPX1982198246431263783912.60E-49[LN:ECSA_BACSU]128
[AC:P55339]
[GN:ECSA:PRST]
[OR:Bacillus subtilis]
[DE:ABC-TYPE TRANSPORTER ATP-BINDING PROTEIN ECSA]
[SP:P55339]
SPX1983198346441374113348.80E-42[LN:HIT_BACSU]87
[AC:O07513]
[GN:HIT]
[OR:Bacillus subtilis]
[DE:HIT PROTEIN]
[SP:O07513]
SPX19841984464596288NO-HIT6
SPX19851985464685255NO-HIT6
SPX198619864647379113718854.90E-254[LN:DNAJ_STRPN]108
[AC:P95830]
[GN:DNAJ]
[OR:Streptococcus pneumoniae]
[DE:DNAJ PROTEIN (FRAGMENT)]
[SP:P95830]
SPX198719874648471411257.20E-10[GI:5305335]104
[LN:AF071081]
[AC:AF071081]
[PN:proline-rich mucin homolog]
[OR:Mycobacterium tuberculosis]
SPX198819884649119357NO-HIT6
SPX19891989465086258NO-HIT6
SPX199019904651608182430080[LN:DNAK_STRPN]143
[AC:P95829:O66035]
[GN:DNAK]
[OR:Streptococcus pneumoniae]
[DE:DNAK PROTEIN (HEAT SHOCK PROTEIN 70) (HSP70)]
[SP:P95829:O66035]
SPX199119914652120360NO-HIT6
SPX199219924653218654NO-HIT6
SPX1993199346541835493463.60E-74“[LN:GRPE_LACLA]132
[AC:P42369]
[GN:GRPE]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:GRPE PROTEIN]
[SP:P42369]”
SPX199419944655356106817126.90E-235[GI:4566769]125
[LN:AF117740]
[AC:AF117740]
[PN:heat shock transcription repressor HrcA]
[GN:hrcA]
[OR:Streptococcus pneumoniae]
SPX199519954656170510NO-HIT6
SPX19961996465777823345709.20E-238[LN:I41291]104
[AC:I41291]
[PN:EcoA type I restriction-modification enzyme R subunit]
[OR:Escherichia coli]
SPX19971997465848814648461.80E-144[LN:I41293]165
[AC:I41293]
[PN:EcoE type I restriction modification enzyme M subunit]
[CL:site-specific methyltransferase (adenine-specific) EcoK]
[OR:Escherichia coli]
SPX19981998465951715513231.60E-37[GI:6899439]141
[LN:AE002141]
[AC:AE002141:AF222894]
[PN:type I restriction enzyme S protein (fragment)]
[GN:hsdS-5]
[OR:Ureaplasma urealyticum]
SPX19991999466043012903281.40E-38[GI:6899439]141
[LN:AE002141]
[AC:AE002141:AF222894]
[PN:type I restriction enzyme S protein (fragment)]
[GN:hsdS-5]
[OR:Ureaplasma urealyticum]
SPX20002000466174222NO-HIT6
SPX200120014662449134712656.40E-246[GI:1815634]111
[LN:SAU61271]
[AC:U61271]
[PN:glutamine synthetase type 1]
[GN:glnA]
[OR:Streptococcus agalactiae]
SPX2002200246631193572447.30E-29[LN:GLNR_BACCE]99
[AC:P19083]
[GN:GLNR]
[OR:Bacillus cereus]
[DE:REGULATORY PROTEIN GLNR]
[SP:P19083]
SPX2003200346641765281001.00E-06[LN:H69815]87
[AC:H69815]
[PN:hypothetical protein ygaE]
[GN:ygaE]
[OR:Bacillus subtilis]
SPX2004200446651263781371.10E-11[LN:S72776]74
[AC:S72776]
[PN:B1496_F1_41 protein]
[OR:Mycobacterium leprae]
SPX20052005466639911976226.20E-166[GI:4490614]106
[LN:SAU133520]
[AC:AJ133520]
[PN:phosphoglycerate kinase]
[GN:pgk]
[OR:Staphylococcus aureus]
SPX200620064667164749412073.10E-63[GI:4204919]109
[LN:APU59168]
[AC:U59168]
[PN:endo-beta-N-acetylglucosaminidase]
[OR:Arthrobacter protophormiae]
SPX200720074668171513NO-HIT6
SPX20082008466954416322493.20E-57“[LN:H71283]165
[AC:H71283]
[PN:conserved hypothetical integral membrane protein TP0771]
[GN:TP0771]
[OR:Treponema pallidum subsp. pallidum]
[SR:, syphilis spirochete]”
SPX200920094670536160823030[LN:LAJ10153]97
[AC:AJ010153]
[PN:CTP synthetase]
[GN:pyrG]
[OR:Lactococcus lactis subsp. cremoris]
SPX201020104671441321376.60E-15[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX2011201146721965881691.20E-25“[LN:RPOE_BACSU]135
[AC:P12464]
[GN:RPOE]
[OR:Bacillus subtilis]
[EC:2.7.7.6]
[DE:DNA-DIRECTED RNA POLYMERASE DELTA SUBUNIT,]
[SP:P12464]”
SPX201220124673150450NO-HIT6
SPX201320134674130390NO-HIT6
SPX2014201446752176511795.00E-19[LN:S32217]76
[AC:S32217]
[PN:hypothetical protein 2]
[OR:Bacillus megaterium]
SPX2015201546761885642583.20E-32[LN:YPAA_BACSU]136
[AC:P50726]
[GN:YPAA]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 20.5 KD PROTEIN IN SERA-FER INTERGENIC REGION]
[SP:P50726]
SPX20162016467773219NO-HIT6
SPX2017201746781564682436.60E-44[GI:1381681]117
[LN:BSU58864]
[AC:U58864]
[PN:CspR]
[GN:cspR]
[OR:Bacillus subtilis]
[SR:Bacillus subtilis strain=JH642]
SPX201820184679277831834.70E-12[LN:Y181_MYCPN]119
[AC:Q50292]
[OR:Mycoplasma pneumoniae]
[DE:HYPOTHETICAL PROTEIN MG181 HOMOLOG (GT9_ORF434)]
[SP:Q50292]
SPX20192019468041612483431.40E-50[LN:G64435]181
[AC:G64435]
[PN:cobalt transport ATP-binding protein O homolog]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Methanococcus jannaschii]
SPX2020202046811283842301.10E-25[LN:G71192]189
[AC:G71192]
[PN:probable cobalt transport ATP-binding protein]
[GN:PH1815]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Pyrococcus horikoshii]
SPX20212021468271213NO-HIT6
SPX20222022468386258NO-HIT6
SPX2023202346841835494941.60E-73[GI:6165407]91
[LN:LLA012388]
[AC:AJ012388]
[PN:hypothetical protein]
[OR:Lactococcus lactis]
SPX2024202446852928765462.00E-98[LN:E64608]91
[AC:E64608]
[PN:conserved hypothetical protein HP0709]
[OR:Helicobacter pylori]
SPX20252025468645013502581.20E-60[LN:F69354]177
[AC:F69354]
[PN:TRK potassium uptake system protein (trkA-2) homolog]
[CL:Methanococcus jannaschii TRK system potassium uptake protein A]
[OR:Archaeoglobus fulgidus]
SPX20262026468747914372327.20E-73[LN:G69354]142
[AC:G69354]
[PN:TRK potassium uptake system protein (trkH) homolog]
[CL:potassium uptake protein trkG]
[OR:Archaeoglobus fulgidus]
SPX20272027468856016807771.20E-171[LN:PTLB_STRMU]118
[AC:P50976]
[GN:LACE]
[OR:Streptococcus mutans]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EII-LAC)]
[SP:P50976]
SPX20282028468947114136435.80E-164“[GI:153755]122
[LN:STRPBGSL]
[AC:M19454]
[OR:Lactococcus lactis subsp. cremoris]
[SR:S.lactis (strain Z268) DNA, clone X25]”
SPX20292029469065195NO-HIT6
SPX2030203046911153452988.20E-37[LN:PTLA_LACCA]118
[AC:P11502]
[GN:LACF]
[OR:Lactobacillus casei]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EIII-LAC)]
[SP:P11502]
SPX2031203146926471941NO-HIT6
SPX20322032469344113233951.00E-89“[LN:PTCC_BACST]157
[AC:Q45400]
[GN:CELB]
[OR:Bacillus stearothermophilus]
[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]
[SP:Q45400]”
SPX20332033469440812241472.50E-21[LN:XYLR_BACSU]94
[AC:P16557]
[GN:XYLR]
[OR:Bacillus subtilis]
[DE:XYLOSE REPRESSOR]
[SP:P16557]
SPX20342034469573219NO-HIT6
SPX20352035469658174NO-HIT6
SPX20362036469762186NO-HIT6
SPX203720374698952851672.40E-18[GI:2707293]77
[LN:AF036720]
[AC:AF036720]
[PN:unknown]
[OR:Lactococcus lactis]
SPX2038203846991735198796.50E-119[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX20392039470025676812351.10E-172[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX20402040470142112639484.80E-188[GI:2687821]87
[LN:STIS1193]
[AC:Y13713]
[PN:transposase]
[OR:Streptococcus thermophilus]
SPX204120414702862581491.10E-14[GI:2198546]78
[LN:SPCPS14E]
[AC:X85787]
[GN:tasA]
[OR:Streptococcus pneumoniae]
SPX204220424703775232537740[GI:3168596]145
[LN:AB014686]
[AC:AB014686]
[PN:pyruvate formate-lyase]
[GN:pfl]
[OR:Streptococcus bovis]
[SR:Streptococcus bovis (strain:JB-1) DNA]
SPX204320434704922761337.70E-20[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX20442044470578234NO-HIT6
SPX20452045470635710714912.70E-83[GI:7380303]126
[LN:NMA5Z2491]
[AC:AL162756:AL157959]
[PN:impB/mucB/samB family protein]
[GN:NMA1661]
[OR:Neisseria meningitidis]
SPX20462046470763189NO-HIT6
SPX2047204747082828462896.60E-52[GI:5739401]91
[LN:AF169967]
[AC:AF169967]
[PN:BacA]
[GN:bacA]
[OR:Flavobacterium johnsoniae]
SPX2048204847092176511393.00E-12[LN:YIS1_STRCO]140
[AC:P19780]
[GN:SC3C8.10]
[OR:Streptomyces coelicolor]
[DE:INSERTION ELEMENT IS110 HYPOTHETICAL 43.6 KD PROTEIN]
[SP:P19780]
SPX20492049471062186NO-HIT6
SPX2050205047116311893953.20E-08[LN:H64496]86
[AC:H64496]
[PN:hypothetical protein MJ1577]
[OR:Methanococcus jannaschii]
SPX20512051471252215663319.10E-53“[LN:A72357]146
[AC:A72357]
[PN:amino acid ABC transporter, permease protein]
[GN:TM0592]
[CL:histidine permease protein M]
[OR:Thermotoga maritima]”
SPX2052205247132477413889.60E-89[LN:F81363]138
[AC:F81363]
[PN:probable glutamine transport ATP-binding protein Cj0902 [imported]]
[GN:glnQ:Cj0902]
[OR:Campylobacter jejuni]
SPX20532053471472216NO-HIT6
SPX20542054471577231NO-HIT6
SPX205520554716661982541.20E-29[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX2056205647171283845112.70E-66[GI:5739312]126
[LN:AF161700]
[AC:AF161700]
[PN:ComX1]
[GN:comX1]
[FN:transcriptional regulator of]
[OR:Streptococcus pneumoniae]
SPX2057205747181845524421.30E-63[LN:NUSG_BACSU]120
[AC:Q06795]
[GN:NUSG]
[OR:Bacillus subtilis]
[DE:TRANSCRIPTION ANTITERMINATION PROTEIN NUSG]
[SP:Q06795]
SPX20582058471959177NO-HIT6
SPX205920594720732219637140[GI:6165960]116
[LN:AF101780]
[AC:AF101780]
[PN:penicillin-binding protein 2a]
[GN:pbp2a]
[OR:Streptococcus pneumoniae]
SPX2060206047212928762294.10E-34[LN:YHCT_BACSU]137
[AC:P54604]
[GN:YHCT]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 33.7 KD PROTEIN IN CSPB-GLPP INTERGENIC REGION]
[SP:P54604]
SPX206120614722360108010612.30E-215“[LN:A42963]186
[AC:A42963:B42963:JH0750]
[PN:glyceraldehyde-3-phosphate dehydrogenase,:plasmin receptor]
[CL:glyceraldehyde-3-phosphate dehydrogenase]
[OR:Streptococcus sp.]
[EC:1.2.1.12]”
SPX20622062472392276NO-HIT6
SPX2063206347243179511241.80E-15[LN:Y797_METJA]114
[AC:Q58207]
[GN:MJ0797]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL PROTEIN MJ0797]
[SP:Q58207]
SPX2064206447251133395522.20E-73[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX20652065472687261NO-HIT6
SPX2066206647271163485775.80E-76[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX2067206747283009004822.20E-71[LN:B70375]160
[AC:B70375]
[PN:quinolinate phosphoribosyl transferase]
[GN:nadC]
[CL:nicotinate-nucleotide pyrophosphorylase (carboxylating)]
[OR:Aquifex aeolicus]
SPX20682068472943713114482.70E-105[LN:C81402]119
[AC:C81402]
[PN:probable integral membrane protein Cj0555 [imported]]
[GN:Cj0555]
[OR:Campylobacter jejuni]
SPX20692069473062186NO-HIT6
SPX207020704731651951117.10E-09“[LN:H81018]137
[AC:H81018]
[PN:iron(III) ABC transporter, ATP-binding protein NMB1993 [imported]]
[GN:NMB1993]
[OR:Neisseria meningitidis]”
SPX2071207147322437293523.20E-72“[GI:4512387]143
[LN:AB011838]
[AC:AB011838]
[GN:ydhQ]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.]”
SPX20722072473347014108088.30E-181[LN:D69785]127
[AC:D69785]
[PN:beta-glucosidase homolog ydhP]
[GN:ydhP]
[CL:Agrobacterium beta-glucosidase]
[OR:Bacillus subtilis]
SPX20732073473443212963307.00E-64“[LN:PTCC_BACSU]152
[AC:P46317]
[GN:CELB:LICC]
[OR:Bacillus subtilis]
[DE:PERMEASE IIC COMPONENT) (PHOSPHOTRANSFERASE ENZYME II, C COMPONENT)]
[SP:P46317]”
SPX207420744735129387NO-HIT6
SPX2075207547361033091912.70E-30[LN:PTCB_BACST]115
[AC:Q45399]
[GN:CELA]
[OR:Bacillus stearothermophilus]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69)]
[SP:Q45399]
SPX2076207647371033092106.00E-24[LN:PTCA_BACSU]121
[AC:P46319]
[GN:CELC:LICA]
[OR:Bacillus subtilis]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69) (EIII-CEL)]
[SP:P46319]
SPX20772077473875225NO-HIT6
SPX207820784739891267322720“[LN:ADH2_ENTHI]176
[AC:Q24803:Q27649]
[GN:ADH2]
[OR:Entamoeba histolytica]
[EC:1.1.1.1:1.2.1.10]
[DE:(EC 1.1.1.1) (ADH); ALCETALDEHYDE DEHYDROGENASE, (ACDH)]]
[SP:Q24803:Q27649]”
SPX2079207947401374111684.10E-18[GI:6010051]113
[LN:ECA270205]
[AC:AJ270205]
[PN:putative phosphatidylinositol-4-phosphate]
[OR:Entodinium caudatum]
SPX208020804741143429917.10E-26“““[LN:E69808]161
[AC:E69808]
[PN:protein-tyrosine phosphatase homolog yfkJ]
[GN:yfkJ]
[CL:protein-tyrosine-phosphatase, low molecular weight]
[OR:Bacillus subtilis]”
SPX2081208147421003001779.30E-20[GI:1402532]130
[LN:D78257]
[AC:D78257]
[PN:ORF11]
[GN:orf11]
[OR:Enterococcus faecalis]
[SR:Enterococcus faecalis plasmid:pYI17 DNA]
SPX208220824743659197716710“[LN:TKT_STRPN]127
[AC:P22976]
[GN:RECP]
[OR:Streptococcus pneumoniae]
[EC:2.2.1.1]
[DE:PROBABLE TRANSKETOLASE, (TK)]
[SP:P22976]”
SPX208320834744812431711.00E-17“[LN:TKT_STRPN]127
[AC:P22976]
[GN:RECP]
[OR:Streptococcus pneumoniae]
[EC:2.2.1.1]
[DE:PROBABLE TRANSKETOLASE, (TK)]
[SP:P22976]”
SPX2084208447451023062771.50E-33“[LN:TKT_STRPN]127
[AC:P22976]
[GN:RECP]
[OR:Streptococcus pneumoniae]
[EC:2.2.1.1]
[DE:PROBABLE TRANSKETOLASE, (TK)]
[SP:P22976]”
SPX2085208547462457355468.30E-96[LN:YJFR_ECOLI]136
[AC:P39300]
[GN:YJFR]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 40.1 KD PROTEIN IN AIDB-SGAT INTERGENIC REGION]
[SP:P39300]
SPX2086208647471364084303.30E-54[LN:YJFR_ECOLI]136
[AC:P39300]
[GN:YJFR]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 40.1 KD PROTEIN IN AIDB-SGAT INTERGENIC REGION]
[SP:P39300]
SPX20872087474855816741786.30E-20“[GI:4512373]144
[LN:AB011837]
[AC:AB011837]
[GN:yjdC]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”
SPX2088208847492357054893.20E-93[GI:5616307]123
[LN:AF160811]
[AC:AF160811]
[PN:L-ribulose 5-phosphate 4-epimerase]
[GN:araD]
[OR:Bacillus stearothermophilus]
SPX2089208947502888647773.20E-106“[LN:SGBU_HAEIN]153
[AC:P44990]
[GN:SGBU:HI1026]
[OR:Haemophilus influenzae]
[EC:5.-.-.-]
[DE:PUTATIVE HEXULOSE-6-PHOSPHATE ISOMERASE, (HUMPI)]
[SP:P44990]”
SPX2090209047512226663491.00E-70[LN:SGAH_ECOLI]132
[AC:P39304]
[GN:SGAH]
[OR:Escherichia coli]
[EC:4.1.2.-]
[DE:3-HEXULOSE 6-PHOSPHATE FORMALDEHYDE LYASE)]
[SP:P39304]
SPX2091209147521624862661.10E-45[LN:PTXA_ECOLI]104
[AC:P39303]
[GN:SGAA]
[OR:Escherichia coli]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69)]
[SP:P39303]
SPX209220924753942821116.80E-22[LN:PTXB_ECOLI]104
[AC:P39302]
[GN:SGAB]
[OR:Escherichia coli]
[EC:2.7.1.69]
[DE:(EC 2.7.1.69)]
[SP:P39302]
SPX20932093475450915272755.90E-99[LN:SGAT_ECOLI]108
[AC:P39301]
[GN:SGAT]
[OR:Escherichia coli]
[DE:PUTATIVE TRANSPORT PROTEIN SGAT]
[SP:P39301]
SPX2094209447552086242101.10E-38“[GI:6681651]183
[LN:AB016077]
[AC:AB016077]
[PN:sakacin A production response regulator]
[GN:sapR]
[OR:Streptococcus mutans]
[SR:Streptococcus mutans (strain:MT8148) DNA, clone:pYT570]”
SPX2095209547563299871451.90E-24[LN:JAG_BACSU]116
[AC:Q01620]
[GN:JAG]
[OR:Bacillus subtilis]
[DE:JAG PROTEIN (SPOIIIJ ASSOCIATED PROTEIN)]
[SP:Q01620]
SPX2096209647572778313571.00E-51[LN:SP3J_BACSU]122
[AC:Q01625]
[GN:SPOIIIJ]
[OR:Bacillus subtilis]
[DE:STAGE III SPORULATION PROTEIN J PRECURSOR]
[SP:Q01625]
SPX2097209747581243721733.10E-31“[GI:5672645]137
[LN:AB013492]
[AC:AB013492]
[GN:rnpA]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA, clone:ALBAC001]”
SPX20982098475939711918221.30E-149“[LN:ACKA_BACSU]122
[AC:P37877]
[GN:ACKA]
[OR:Bacillus subtilis]
[EC:2.7.2.1]
[DE:ACETATE KINASE, (ACETOKINASE)]
[SP:P37877]”
SPX2099209947603189542974.70E-44[LN:YTXK_BACSU]137
[AC:P37876]
[GN:YTXK]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 37.4 KD PROTEIN IN ACKA-SSPA INTERGENIC REGION]
[SP:P37876]
SPX2100210047611965881322.90E-10[LN:H70323]90
[AC:H70323]
[PN:hypothetical protein aq_262]
[GN:aq_262]
[OR:Aquifex aeolicus]
SPX210121014762138414NO-HIT6
SPX2102210247631695071571.60E-30[GI:3287181]89
[LN:LLC3107]
[AC:Y15043]
[GN:orf150]
[OR:Lactococcus lactis subsp. cremoris]
SPX2103210347641013031239.50E-12[GI:3287182]115
[LN:LLC3107]
[AC:Y15043]
[PN:hypothetical protein]
[GN:orf128]
[OR:Lactococcus lactis subsp. cremoris]
SPX2104210447651354056263.00E-81[GI:3211751]104
[LN:AF052207]
[AC:AF052207]
[PN:competence protein]
[GN:cglD]
[OR:Streptococcus pneumoniae]
SPX2105210547661093275125.80E-66[GI:3211750]104
[LN:AF052207]
[AC:AF052207]
[PN:competence protein]
[GN:cglC]
[OR:Streptococcus pneumoniae]
SPX210621064767348104414403.30E-199[GI:3211749]104
[LN:AF052207]
[AC:AF052207]
[PN:competence protein]
[GN:cglB]
[OR:Streptococcus pneumoniae]
SPX21072107476831494215924.30E-217[GI:3211748]104
[LN:AF052207]
[AC:AF052207]
[PN:competence protein]
[GN:cglA]
[OR:Streptococcus pneumoniae]
SPX2108210847691243724689.20E-61[GI:2058543]100
[LN:SGU81957]
[AC:U81957]
[PN:putative DNA binding protein]
[OR:Streptococcus gordonii]
SPX21092109477035310596391.60E-125[LN:T36961]179
[AC:T36961]
[PN:probable zinc-containing dehydrogenase]
[GN:SCJ1.28c]
[CL:alcohol dehydrogenase:long-chain alcohol dehydrogenase homology]
[OR:Streptomyces coelicolor]
SPX211021104771142426NO-HIT6
SPX21112111477238411528193.90E-108[GI:6683552]118
[LN:AB024532]
[AC:AB024532]
[GN:SA8A11-1]
[OR:Enterococcus seriolicida]
[SR:Enterococcus seriolicida DNA]
SPX21122112477360618181732.40E-27[LN:C69975]90
[AC:C69975]
[PN:acyltransferase homolog yrhL]
[GN:yrhL]
[OR:Bacillus subtilis]
SPX211321134774381114314693.70E-200[LN:TGT_BACSU]134
[AC:O32053]
[GN:TGT]
[OR:Bacillus subtilis]
[EC:2.4.2.29]
[DE:TRANSGLYCOSYLASE) (GUANINE INSERTION ENZYME)]
[SP:O32053]
SPX211421144775286858909.00E-05[LN:S32215]76
[AC:S32215]
[PN:hypothetical protein 1]
[OR:Bacillus megaterium]
SPX2115211547762156457691.20E-104[LN:PCP_STRPY]149
[AC:Q01328]
[GN:PCP]
[OR:Streptococcus pyogenes]
[EC:3.4.19.3]
[DE:PEPTIDASE) (PYROGLUTAMYL-PEPTIDASE I) (PGP-I) (PYRASE)]
[SP:Q01328]
SPX21162116477790270NO-HIT6
SPX2117211747781203602211.90E-43“[LN:YTRP_LACLA]155
[AC:Q02009]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:HYPOTHETICAL 13.3 KD PROTEIN IN TRPE 5′REGION]
[SP:Q02009]”
SPX2118211847791424261633.50E-17[LN:D69783]139
[AC:D69783]
[PN:transcription regulator MarR family homolog ydgJ]
[GN:ydgJ]
[CL:regulatory protein mprA]
[OR:Bacillus subtilis]
SPX211921194780692071072.10E-10[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX21202120478137111133828.00E-79[GI:517204]65
[LN:SPU09352]
[AC:U09352]
[OR:Streptococcus pyogenes]
SPX2121212147822076211537.60E-14[LN:A57362]81
[AC:A57362]
[PN:gyrb protein]
[GN:gyrb]
[OR:Streptococcus pneumoniae]
SPX21222122478342712812161.10E-45[LN:H72331]139
[AC:H72331]
[PN:conserved hypothetical protein]
[GN:TM0815]
[CL:conserved hypothetical protein HI1612]
[OR:Thermotoga maritima]
SPX21232123478449514854124.80E-66[LN:B64532]96
[AC:B64532]
[PN:threonine synthase]
[CL:threonine synthase]
[OR:Helicobacter pylori]
SPX2124212447854261278700.00014“[LN:T05142]158
[AC:T05142:S60128:S45018]
[PN:gamma-glutamylcysteine synthetase:protein F7H19.290]
[OR:Arabidopsis thaliana]
[SR:, mouse-ear cress]
[EC:6.3.2.2]”
SPX212521254786591771001.30E-08[LN:C64671]81
[AC:C64671]
[PN:hypothetical protein HP1211]
[OR:Helicobacter pylori]
SPX21262126478761183819.30E-05[LN:E72688]143
[AC:E72688]
[PN:hypothetical protein APE0925]
[GN:APE0925]
[CL:Aeropyrum pernix hypothetical protein APE0925]
[OR:Aeropyrum pernix]
SPX212721274788782341434.90E-15[LN:F71245]95
[AC:F71245]
[PN:hypothetical protein PHS004]
[GN:PHS004]
[OR:Pyrococcus horikoshii]
SPX212821284789822462471.10E-29[LN:F81737]131
[AC:F81737]
[PN:hypothetical protein TC0129 [imported]]
[GN:TC0129]
[OR:Chlamydia muridarum:Chlamydia trachomatis MoPn]
SPX21292129479052156803.00E-05[LN:D75542]90
[AC:D75542]
[PN:hypothetical protein]
[GN:DR0254]
[OR:Deinococcus radiodurans]
SPX213021304791105315NO-HIT6
SPX2131213147921464384861.80E-62[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX21322132479335410628246.40E-132[GI:1915907]95
[LN:LLPEPPGEN]
[AC:Y08842]
[PN:aminopeptidase P]
[GN:pepP]
[OR:Lactococcus lactis]
SPX213321334794944283220290[LN:UVRA_BACSU]104
[AC:O34863]
[GN:UVRA]
[OR:Bacillus subtilis]
[DE:EXCINUCLEASE ABC SUBUNIT A]
[SP:O34863]
SPX2134213447953159452361.50E-26[LN:A75272]140
[AC:A75272]
[PN:probable transport protein]
[GN:DR2463]
[CL:magnesium and cobalt transport protein]
[OR:Deinococcus radiodurans]
SPX21352135479668204NO-HIT6
SPX213621364797213639NO-HIT6
SPX213721374798511531231.60E-12[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX2138213847993441032861.10E-19[LN:E75325]91
[AC:E75325]
[PN:probable mccF protein]
[GN:DR2000]
[OR:Deinococcus radiodurans]
SPX213921394800226678663.80E-08[GI:6470197]77
[LN:AF188935]
[AC:AF188935]
[PN:pXO2-46]
[OR:Bacillus anthracis]
SPX2140214048011885644653.30E-63[LN:3MGA_HAEIN]121
[AC:P44321]
[GN:TAG:HI0654]
[OR:Haemophilus influenzae]
[EC:3.2.2.20]
[DE:GLYCOSIDASE) (TAG)]
[SP:P44321]
SPX214121414802186558NO-HIT6
SPX2142214248031985942351.00E-38[LN:RUVA_BACSU]122
[AC:O05392]
[GN:RUVA]
[OR:Bacillus subtilis]
[DE:PROBABLE HOLLIDAY JUNCTION DNA HELICASE RUVA]
[SP:O05392]
SPX21432143480470210NO-HIT6
SPX21442144480536711018886.00E-128“[LN:RIBD_ACTPL]177
[AC:P50853]
[GN:RIBD:RIBG]
[OR:Actinobacillus pleuropneumoniae]
[SR:,Haemophilus pleuropneumoniae]
[EC:3.5.4.-]
[DE:RIBOFLAVIN-SPECIFIC DEAMINASE,]
[SP:P50853]”
SPX2145214548062126366011.70E-81“[LN:RISA_ACTPL]179
[AC:P50854]
[GN:RIBE:RIBB]
[OR:Actinobacillus pleuropneumoniae]
[SR:,Haemophilus pleuropneumoniae]
[EC:2.5.1.9]
[DE:RIBOFLAVIN SYNTHASE ALPHA CHAIN,]
[SP:P50854]”
SPX214621464807412123612661.80E-170“[LN:GCH2_ACTPL]153
[AC:P50855]
[GN:RIBA]
[OR:Actinobacillus pleuropneumoniae]
[SR:,Haemophilus pleuropneumoniae]
[EC:3.5.4.25]
[DE:SYNTHASE)]]
[SP:P50855]”
SPX2147214748081564685461.30E-70“[LN:RISB_ACTPL]194
[AC:P50856]
[GN:RIBH]
[OR:Actinobacillus pleuropneumoniae]
[SR:,Haemophilus pleuropneumoniae]
[EC:2.5.1.9]
[DE:(LUMAZINE SYNTHASE) (RIBOFLAVIN SYNTHASE BETA CHAIN)]
[SP:P50856]”
SPX214821484809650195032860[LN:HEXB_STRPN]117
[AC:P14160]
[GN:HEXB]
[OR:Streptococcus pneumoniae]
[DE:DNA MISMATCH REPAIR PROTEIN HEXB]
[SP:P14160]
SPX21492149481084252NO-HIT6
SPX21502150481197291NO-HIT6
SPX215121514812611831221.10E-12[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX2152215248131745222319.30E-27“[GI:1196936]144
[LN:STRHEXB]
[AC:M29686]
[PN:unknown protein]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (clone: pSP(8,41).) DNA]”
SPX215321534814153459NO-HIT6
SPX2154215448151263783331.60E-40[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX2155215548162116337627.90E-101[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX2156215648172016034997.70E-65[LN:C81084]109
[AC:C81084]
[PN:hypothetical protein NMB1426 [imported]]
[GN:NMB1426]
[OR:Neisseria meningitidis]
SPX21572157481864192NO-HIT6
SPX2158215848192186544612.50E-67[LN:C81084]109
[AC:C81084]
[PN:hypothetical protein NMB1426 [imported]]
[GN:NMB1426]
[OR:Neisseria meningitidis]
SPX2159215948202016033533.50E-53[GI:6782392]125
[LN:SDY18363]
[AC:Y18363]
[PN:ribonucleotide reductase-like (Nrd-like)]
[GN:nrd]
[OR:Streptococcus dysgalactiae]
SPX216021604821194582NO-HIT6
SPX216121614822429128721766.20E-298[GI:5830536]104
[LN:SPAJ6396]
[AC:AJ006396]
[PN:response regulator]
[GN:rr07]
[OR:Streptococcus pneumoniae]
SPX216221624823568170411837.00E-160[GI:5830535]102
[LN:SPAJ6396]
[AC:AJ006396]
[PN:histidine kinase]
[GN:hk07]
[OR:Streptococcus pneumoniae]
SPX216321634824205615NO-HIT6
SPX216421644825190570NO-HIT6
SPX2165216548262316933951.90E-87[GI:6165406]91
[LN:LLA012388]
[AC:AJ012388]
[PN:hypothetical protein]
[OR:Lactococcus lactis]
SPX21662166482735410626164.50E-130[GI:6165405]91
[LN:LLA012388]
[AC:AJ012388]
[PN:hypothetical protein]
[OR:Lactococcus lactis]
SPX21672167482873219948.50E-07[LN:G72536]92
[AC:G72536]
[PN:hypothetical protein APE1580]
[GN:APE1580]
[OR:Aeropyrum pernix]
SPX21682168482945813742197.10E-53[LN:E75327]99
[AC:E75327]
[PN:ArgE/DapE/Acy1 family protein]
[GN:DR2017]
[OR:Deinococcus radiodurans]
SPX2169216948302858553191.50E-63[GI:6165404]91
[LN:LLA012388]
[AC:AJ012388]
[PN:hypothetical protein]
[OR:Lactococcus lactis]
SPX21702170483166198NO-HIT6
SPX2171217148321845521091.10E-12[LN:YXEM_BACSU]110
[AC:P54952]
[GN:YXEM:LP9E]
[OR:Bacillus subtilis]
[DE:INTERGENIC REGION PRECURSOR]
[SP:P54952]
SPX21722172483362186NO-HIT6
SPX2173217348342256751295.60E-10[LN:G75494]121
[AC:G75494]
[PN:AzlC family protein]
[GN:DR0633]
[CL:hypothetical protein b2682]
[OR:Deinococcus radiodurans]
SPX2174217448351374113282.80E-41[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX21752175483680240NO-HIT6
SPX21762176483775225NO-HIT6
SPX2177217748384101230802.70E-10[GI:3582221]114
[LN:AE001272]
[AC:AE001272]
[PN:conserved hypothetical protein]
[GN:ORF00049]
[OR:Lactococcus lactis]
SPX217821784839222666711.80E-05[LN:E69787]87
[AC:E69787]
[PN:hypothetical protein ydiL]
[GN:ydiL]
[OR:Bacillus subtilis]
SPX21792179484066198NO-HIT6
SPX2180218048412968885874.20E-77[GI:4102023]134
[LN:AF007761]
[AC:AF007761]
[PN:MutR]
[GN:mutR]
[FN:positive transcriptional regulator of mutA]
[OR:Streptococcus mutans]
SPX21812181484269207NO-HIT6
SPX2182218248432066184791.40E-72[LN:UDG5_ECOLI]111
[AC:Q47329]
[GN:KFID]
[OR:Escherichia coli]
[EC:1.1.1.22]
[DE:(UDP-GLCDH) (UDPGDH)]
[SP:Q47329]
SPX218321834844252756863.90E-08[GI:4689219]92
[LN:AF115779]
[AC:AF115779]
[PN:unknown]
[GN:mitC]
[OR:Streptomyces lavendulae]
SPX21842184484574222NO-HIT6
SPX218521854846115345NO-HIT6
SPX21862186484781243NO-HIT6
SPX21872187484853916172941.70E-34“[LN:D72267]180
[AC:D72267]
[PN:ABC transporter, ATP-binding protein]
[GN:TM1328]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Thermotoga maritima]”
SPX2188218848493189541375.90E-20[LN:B75096]144
[AC:B75096]
[PN:glycosyl transferase PAB0772]
[GN:PAB0772]
[CL:Neisseria meningitidis glycosyl transferase A]
[OR:Pyrococcus abyssi]
SPX2189218948501755251796.60E-17[GI:1276880]90
[LN:STU40830]
[AC:U40830]
[PN:EpsG]
[GN:epsG]
[OR:Streptococcus thermophilus]
SPX219021904851188564NO-HIT6
SPX2191219148521073211873.70E-21[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX219221924853882641962.60E-23[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX21932193485435510658938.00E-121[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX2194219448551293874902.90E-65[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX219521954856712131192.60E-10[GI:2198546]78
[LN:SPCPS14E]
[AC:X85787]
[GN:tasA]
[OR:Streptococcus pneumoniae]
SPX21962196485733710119136.50E-132[LN:YDIE_BACSU]138
[AC:O05518]
[GN:YDIE]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 36.8 KD PROTEIN IN PHOB-GROES INTERGENIC REGION]
[SP:O05518]
SPX219721974858146438921.00E-09[LN:E69786]190
[AC:E69786]
[PN:ribosomal-protein-alanine N-acetyltransfer homolog ydiD]
[GN:ydiD]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimI]
[OR:Bacillus subtilis]
SPX2198219848592286843031.40E-53[GI:3341437]101
[LN:EFY17797]
[AC:Y17797]
[PN:hypothetical protein]
[GN:ydiC]
[OR:Enterococcus faecalis]
SPX21992199486062186NO-HIT6
SPX22002200486177231NO-HIT6
SPX22012201486278234782.50E-10[LN:D69871]87
[AC:D69871]
[PN:hypothetical protein ykzG]
[GN:ykzG]
[OR:Bacillus subtilis]
SPX220222024863560168018416.00E-251[LN:YKQC_BACSU]137
[AC:Q45493]
[GN:YKQC]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 61.5 KD PROTEIN IN ADEC-PDHA INTERGENIC REGION]
[SP:Q45493]
SPX220322034864121363NO-HIT6
SPX220422044865638191416982.50E-282“[LN:GIDA_LACLC]171
[AC:O32806]
[GN:GIDA]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[DE:GLUCOSE INHIBITED DIVISION PROTEIN A (FRAGMENT)]
[SP:O32806]”
SPX220522054866158474NO-HIT6
SPX220622064867161483732.50E-06[LN:F75354]95
[AC:F75354]
[PN:MutT/nudix family protein]
[GN:DR1776]
[OR:Deinococcus radiodurans]
SPX22072207486839211765781.10E-170[LN:TRMU_BACSU]105
[AC:O35020]
[GN:TRMU]
[OR:Bacillus subtilis]
[EC:2.1.1.61]
[DE:(EC 2.1.1.61)]
[SP:O35020]
SPX22082208486960180NO-HIT6
SPX22092209487066198NO-HIT6
SPX221022104871551165313247.00E-210[LN:A41971]169
[AC:A41971:A60282:A33134]
[PN:surface protein pspA precursor:pneumococcal surface protein A]
[GN:pspA]
[CL:cpl repeat homology]
[OR:Streptococcus pneumoniae]
SPX22112211487279237981.60E-06[GI:311109]169
[LN:YSCISCLRP]
[AC:L16900]
[PN:intrastrand crosslink recognition protein]
[GN:Ixr1]
[OR:Saccharomyces cerevisiae]
[SR:Saccharomyces cerevisiae (strain ) DNA]
SPX22122212487364192770.00063[LN:B72392]86
[AC:B72392]
[PN:hypothetical protein]
[GN:TM0315]
[OR:Thermotoga maritima]
SPX221322134874103309870.0009[GI:7292943]106
[LN:AE003494]
[AC:AE003494:AE002593]
[GN:CG11075]
[OR:Drosophila melanogaster]
[SR:fruit fly]
SPX221422144875106318NO-HIT6
SPX2215221548761033094598.20E-56[GI:6752385]90
[LN:AF071807]
[AC:AF071807]
[PN:PspA]
[GN:pspA]
[OR:Streptococcus pneumoniae]
SPX22162216487793279NO-HIT6
SPX221722174878100300NO-HIT6
SPX22182218487971213NO-HIT6
SPX221922194880253759NO-HIT6
SPX222022204881129387NO-HIT6
SPX222122214882301903NO-HIT6
SPX22222222488361183NO-HIT6
SPX222322234884125375NO-HIT6
SPX22242224488562186NO-HIT6
SPX222522254886227681NO-HIT6
SPX22262226488776228NO-HIT6
SPX22272227488831995717393.00E-234“[LN:ALYS_BPHB3]162
[AC:P32762]
[GN:HBL]
[OR:Streptococcus pneumoniae phage HB-3]
[EC:3.5.1.28]
[DE:LYTIC AMIDASE, (N-ACETYLMURAMOYL-L-ALANINE AMIDASE)]
[SP:P32762]”
SPX222822284889111333NO-HIT6
SPX222922294890139417971.20E-08[LN:VG14_BPB03]110
[AC:Q37895]
[GN:14]
[OR:Bacteriophage B103]
[DE:LYSIS PROTEIN (LATE PROTEIN GP14)]
[SP:Q37895]
SPX223022304891117351NO-HIT6
SPX22312231489268204NO-HIT6
SPX223222324893212063601541.40E-22[GI:4530154]134
[LN:AF085222]
[AC:AF085222]
[PN:putative tail-host specificity protein]
[OR:Streptococcus thermophilus bacteriophage DT1]
SPX22332233489479237NO-HIT6
SPX223422344895117351NO-HIT6
SPX223522354896121836542362.10E-30[GI:2392838]76
[LN:AF011378]
[AC:AF011378]
[PN:unknown]
[OR:Bacteriophage sk1]
SPX2236223648971875611062.00E-07[GI:5305335]104
[LN:AF071081]
[AC:AF071081]
[PN:proline-rich mucin homolog]
[OR:Mycobacterium tuberculosis]
SPX22372237489870210NO-HIT6
SPX22382238489973219NO-HIT6
SPX223922394900127381NO-HIT6
SPX224022404901138414NO-HIT6
SPX224122414902123369770.00049[LN:T13522]132
[AC:T13522]
[PN:hypothetical protein 33]
[CL:Bacillus phage phi-105 hypothetical protein 33]
[OR:Bacillus phage phi-105]
SPX224222424903172516717.90E-06[LN:T42287]65
[AC:T42287]
[PN:hypothetical protein]
[OR:phage SPP1]
SPX22432243490461183NO-HIT6
SPX224422444905113339NO-HIT6
SPX224522454906104312NO-HIT6
SPX22462246490763189NO-HIT6
SPX22472247490861183730.0003[LN:F75258]90
[AC:F75258]
[PN:hypothetical protein]
[GN:DR2560]
[OR:Deinococcus radiodurans]
SPX2248224849092828462262.60E-48[GI:1369939]92
[LN:BTP9011]
[AC:X84706]
[PN:major head protein]
[GN:mhp]
[OR:Bacteriophage B1]
SPX224922494910195585NO-HIT6
SPX22502250491186258NO-HIT6
SPX22512251491276228NO-HIT6
SPX2252225249134681404801.20E-06[LN:T13317]87
[AC:T13317]
[PN:hypothetical protein 28]
[OR:Streptococcus phage phi-O1205]
SPX22532253491449014701543.40E-39[LN:T13620]90
[AC:T13620]
[PN:hypothetical protein gp502]
[OR:Streptococcus phage phi-Sfi11]
SPX22542254491543312993306.80E-48[LN:TERL_BPSPP]105
[AC:P54308]
[GN:2]
[OR:Bacteriophage SPP1]
[DE:TERMINASE LARGE SUBUNIT (G2P)]
[SP:P54308]
SPX2255225549161604802152.30E-32[GI:4680607]105
[LN:AF125198]
[AC:AF125198]
[PN:terminase small subunit]
[GN:TS1]
[OR:bacteriophage phi-FC1]
SPX2256225649171354051544.60E-16[GI:4530181]103
[LN:AF085222]
[AC:AF085222]
[PN:unknown]
[OR:Streptococcus thermophilus bacteriophage DT1]
SPX225722574918124372NO-HIT6
SPX2258225849191464381151.00E-14[GI:5001708]80
[LN:AF109874]
[AC:AF109874]
[PN:unknown]
[OR:Bacteriophage Tuc2009]
SPX225922594920153459NO-HIT6
SPX226022604921872611099.50E-12[GI:4530179]103
[LN:AF085222]
[AC:AF085222]
[PN:unknown]
[OR:Streptococcus thermophilus bacteriophage DT1]
SPX2261226149222326962031.70E-24[LN:T13308]87
[AC:T13308]
[PN:hypothetical protein 19]
[OR:Streptococcus phage phi-O1205]
SPX22622262492345013503581.30E-46[GI:2689558]63
[LN:U93688]
[AC:U93688]
[OR:Staphylococcus aureus]
SPX2263226349242748224707.10E-87[LN:T13301]87
[AC:T13301]
[PN:hypothetical protein 12]
[OR:Streptococcus phage phi-O1205]
SPX22642264492578234NO-HIT6
SPX22652265492666198NO-HIT6
SPX226622664927169507NO-HIT6
SPX226722674928276828NO-HIT6
SPX226822684929106318NO-HIT6
SPX2269226949303981194NO-HIT6
SPX227022704931163489NO-HIT6
SPX227122714932120360NO-HIT6
SPX2272227249331614832562.10E-45[GI:2352435]92
[LN:AF004379]
[AC:AF004379]
[OR:Streptococcus thermophilus bacteriophage Sfi21]
SPX227322734934258774NO-HIT6
SPX22742274493577231NO-HIT6
SPX227522754936114342NO-HIT6
SPX22762276493763189NO-HIT6
SPX22772277493887261NO-HIT6
SPX22782278493991273NO-HIT6
SPX22792279494080240NO-HIT6
SPX22802280494164192NO-HIT6
SPX22812281494268204NO-HIT6
SPX22822282494367201NO-HIT6
SPX228322834944722161013.70E-09[LN:Y272_METJA]132
[AC:Q57720]
[GN:MJ0272]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL TRANSCRIPTIONAL REGULATOR MJ0272]
[SP:Q57720]
SPX22842284494568204NO-HIT6
SPX228522854946230690NO-HIT6
SPX2286228649472647921124.00E-15[LN:T13264]82
[AC:T13264]
[PN:repressor protein]
[OR:Lactococcus lactis phage BK5-T]
SPX2287228749483179511025.00E-09[LN:F59095]94
[AC:F59095]
[PN:hypothetical protein pXO1-38]
[GN:pXO1-38]
[OR:Bacillus anthracis]
SPX22882288494958174NO-HIT6
SPX22892289495037611282123.50E-43[GI:2689564]87
[LN:U93688]
[AC:U93688]
[PN:integrase]
[GN:int]
[OR:Staphylococcus aureus]
SPX22902290495162186NO-HIT6
SPX2291229149523531059810.00071[LN:AF147045]138
[AC:AF147045]
[PN:cytochrome c oxidase subunit 1]
[GN:COI]
[OR:Mitochondrion Dolichoderus lutosus]
[SR:Dolichoderus lutosus]
SPX22922292495364192NO-HIT6
SPX22932293495471213NO-HIT6
SPX22942294495581243NO-HIT6
SPX229522954956149447NO-HIT6
SPX22962296495760180NO-HIT6
SPX2297229749581173511373.30E-14[GI:4760910]86
[LN:AF099088]
[AC:AF099088]
[PN:EntT]
[GN:entT]
[OR:Enterococcus faecium]
SPX2298229849592888641174.70E-08[GI:4102023]134
[LN:AF007761]
[AC:AF007761]
[PN:MutR]
[GN:mutR]
[FN:positive transcriptional regulator of mutA]
[OR:Streptococcus mutans]
SPX229922994960125375NO-HIT6
SPX23002300496176228NO-HIT6
SPX230123014962127381NO-HIT6
SPX23022302496375225NO-HIT6
SPX23032303496470210NO-HIT6
SPX23042304496568204NO-HIT6
SPX2305230549662888641174.70E-08[GI:4102023]134
[LN:AF007761]
[AC:AF007761]
[PN:MutR]
[GN:mutR]
[FN:positive transcriptional regulator of mutA]
[OR:Streptococcus mutans]
SPX2306230649671735198406.50E-114[GI:663278]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX230723074968122366NO-HIT6
SPX230823084969962882791.60E-35[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX23092309497025676812351.10E-172[GI:663279]138
[LN:STRCOMAA]
[AC:M36180:L15190]
[PN:transposase]
[OR:Streptococcus pneumoniae]
[SR:Streptococcus pneumoniae (strain RX1) DNA]
SPX2310231049711574713756.90E-56[LN:ASSY_BACSU]98
[AC:O34347]
[GN:ARGG]
[OR:Bacillus subtilis]
[EC:6.3.4.5]
[DE:LIGASE)]
[SP:O34347]
SPX2311231149722667982006.10E-32“[LN:B72357]181
[AC:B72357]
[PN:amino acid ABC transporter, periplasmic amino acid-binding protein]
[GN:TM0593]
[CL:lysine-arginine-ornithine-binding protein]
[OR:Thermotoga maritima]”
SPX2312231249732146424201.80E-51[LN:F81408]125
[AC:F81408]
[PN:ABC-type transmembrane transport protein Cj0607 [imported]]
[GN:Cj0607]
[OR:Campylobacter jejuni]
SPX23132313497459177801.80E-07[LN:F72598]92
[AC:F72598]
[PN:hypothetical protein APE1254]
[GN:APE1254]
[OR:Aeropyrum pernix]
SPX2314231449754391317NO-HIT6
SPX2315231549763711113NO-HIT6
SPX23162316497772216NO-HIT6
SPX23172317497884252NO-HIT6
SPX2318231849792888641174.70E-08[GI:4102023]134
[LN:AF007761]
[AC:AF007761]
[PN:MutR]
[GN:mutR]
[FN:positive transcriptional regulator of mutA]
[OR:Streptococcus mutans]
SPX2319231949801965883001.00E-34[GI:1619598]108
[LN:LGAPFA]
[AC:Y08498]
[PN:aggregation promoting protein]
[GN:apfA]
[OR:Lactobacillus gasseri]
SPX23202320498197291NO-HIT6
SPX2321232149822246722768.70E-69[LN:SDHB_BACSU]115
[AC:O34635]
[GN:YLOW]
[OR:Bacillus subtilis]
[EC:4.2.1.13]
[DE:DEAMINASE) (SDH) (L-SD)]
[SP:O34635]
SPX2322232249832918738779.00E-119[LN:SDHA_BACSU]115
[AC:O34607]
[GN:YLPA]
[OR:Bacillus subtilis]
[EC:4.2.1.13]
[DE:DEAMINASE) (SDH) (L-SD)]
[SP:O34607]
SPX232323234984178534NO-HIT6
SPX2324232449852116331231.50E-15[GI:7576264]95
[LN:ECH277403]
[AC:AJ277403]
[PN:IndB protein]
[GN:indB]
[OR:Erwinia chrysanthemi]
SPX23252325498672216NO-HIT6
SPX232623264987617185110063.00E-136[GI:6601348]86
[LN:AF155805]
[AC:AF155805]
[PN:Cps9E]
[GN:cps9E]
[OR:Streptococcus suis]
SPX232723274988842521356.70E-14[LN:S28486]72
[AC:S28486]
[PN:hypothetical protein 2]
[OR:Vibrio cholerae]
SPX23282328498939211761237.20E-25[LN:T44514]93
[AC:T44514]
[PN:hypothetical protein 6P [imported]]
[OR:Plesiomonas shigelloides]
SPX232923294990102306NO-HIT6
SPX2330233049912497471425.40E-29[LN:YYCB_BACSU]137
[AC:P37482]
[GN:YYCB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 43.2 KD PROTEIN IN DNAC-RPLI INTERGENIC REGION]
[SP:P37482]
SPX2331233149921434291439.10E-15[LN:PQ0016]80
[AC:PQ0016]
[PN:hypothetical 9K protein]
[OR:Lactobacillus confusus]
SPX2332233249931093271024.10E-07[LN:D75250]100
[AC:D75250]
[PN:conserved hypothetical protein]
[GN:DR2629]
[OR:Deinococcus radiodurans]
SPX233323334994198594NO-HIT6
SPX233423344995304912NO-HIT6
SPX233523354996123369NO-HIT6
SPX23362336499735510651183.00E-07[LN:T18283]82
[AC:T18283]
[PN:hypothetical protein G5]
[OR:Dictyostelium discoideum]
SPX233723374998318954NO-HIT6
SPX2338233849993299879251.60E-165[GI:2565150]89
[LN:LLU92974]
[AC:U92974:M90760:M90761]
[PN:unknown]
[OR:Lactococcus lactis]
SPX23392339500069207NO-HIT6
SPX2340234050015151545NO-HIT6
SPX234123415002134402NO-HIT6
SPX2342234250033089243891.50E-61[GI:1483212]104
[LN:ATCELD]
[AC:Z77855]
[PN:sugar-binding transport protein]
[OR:Anaerocellum thermophilum]
SPX2343234350043209606019.60E-95[GI:1483211]104
[LN:ATCELD]
[AC:Z77855]
[PN:sugar-binding transport protein]
[OR:Anaerocellum thermophilum]
SPX23442344500570210NO-HIT6
SPX234523455006120360NO-HIT6
SPX2346234650071163485775.80E-76[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX2347234750081775312993.70E-73[LN:A37146]182
[AC:A37146:A44901:S11354:C69699:I39962]
[PN:ribosomal protein S4:ribosomal protein BS4 (rpsD)]
[GN:rpsD]
[CL:Escherichia coli ribosomal protein S4]
[OR:Bacillus subtilis]
SPX234823485009359107717092.00E-231[GI:5830539]102
[LN:SPAJ6397]
[AC:AJ006397]
[PN:histidine kinase]
[GN:hk08]
[OR:Streptococcus pneumoniae]
SPX23492349501023369911961.40E-161[GI:5830538]104
[LN:SPAJ6397]
[AC:AJ006397]
[PN:response regulator]
[GN:rr08]
[OR:Streptococcus pneumoniae]
SPX235023505011124372NO-HIT6
SPX23512351501289126731060.00022[GI:7293562]105
[LN:AE003511]
[AC:AE003511:AE002593]
[GN:CG7874]
[OR:Drosophila melanogaster]
[SR:fruit fly]
SPX235223525013190570NO-HIT6
SPX235323535014137411NO-HIT6
SPX2354235450151795371992.70E-20[GI:3550634]151
[LN:SPAJ6986]
[AC:AJ006986]
[PN:glycosyl transferase]
[GN:cap33fH]
[FN:synthesis of capsular polysaccharide]
[OR:Streptococcus pneumoniae]
SPX2355235550162226663461.00E-42[LN:YKQB_BACSU]144
[AC:P39760]
[GN:YKQB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 24.3 KD PROTEIN IN KINC-ADEC INTERGENIC REGION (ORF4)]
[SP:P39760]
SPX23562356501746013803397.90E-94[LN:G75367]99
[AC:G75367]
[PN:potassium uptake protein KtrB]
[GN:DR1668]
[OR:Deinococcus radiodurans]
SPX235723575018621861621.60E-17[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX235823585019255765758.50E-08[LN:D72516]143
[AC:D72516]
[PN:probable uridine phosphorylase APE2105]
[GN:APE2105]
[CL:purine-nucleoside phosphorylase pnp]
[OR:Aeropyrum pernix]
SPX23592359502063189918.80E-06“[GI:6332762]194
[LN:AB033763]
[AC:AB033763:AB014419:AB014429:AB014439]
[PN:hypothetical protein]
[OR:Staphylococcus aureus]
[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”
SPX236023605021992971536.00E-20[LN:YQHL_BACSU]141
[AC:P54510]
[GN:YQHL]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 14.6 KD PROTEIN IN GCVT-SPOIIIAA INTERGENIC REGION]
[SP:P54510]
SPX236123615022121363NO-HIT6
SPX236223625023982941941.30E-21“[GI:6332750]194
[LN:AB033763]
[AC:AB033763:AB014419:AB014429:AB014439]
[PN:hypothetical protein]
[OR:Staphylococcus aureus]
[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”
SPX236323635024822461678.40E-17[LN:A75356]100
[AC:A75356]
[PN:conserved hypothetical protein]
[GN:DR1764]
[OR:Deinococcus radiodurans]
SPX2364236450251323961752.80E-26[LN:T44495]90
[AC:T44495]
[PN:hypothetical protein YFIE [imported]]
[OR:Bacillus halodurans]
SPX23652365502634610382192.60E-44[GI:6562808]119
[LN:SC4A7]
[AC:AL133423]
[PN:putative aldose 1-epimerase]
[GN:SC4A7.35]
[OR:Streptomyces coelicolor A3(2)]
SPX236623665027153459NO-HIT6
SPX23672367502838911674733.90E-95[LN:AGAS_ECOLI]89
[AC:P42907]
[GN:AGAS]
[OR:Escherichia coli]
[DE:AGAS PROTEIN]
[SP:P42907]
SPX23682368502983249776.20E-05[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX2369236950301354051033.80E-13[GI:5669855]128
[LN:AF130465]
[AC:AF130465]
[PN:mannose-specific phosphotransferase system]
[GN:manL]
[OR:Streptococcus salivarius]
SPX2370237050312778311444.90E-34“[LN:PTPD_ECOLI]102
[AC:P42911]
[GN:AGAD]
[OR:Escherichia coli]
[DE:ENZYME II, D COMPONENT)]
[SP:P42911]”
SPX2371237150323029061286.60E-16[GI:1732200]115
[LN:VFU65015]
[AC:U65015]
[PN:PTS permease for mannose subunit IIPMan]
[GN:manY]
[OR:Vibrio furnissii]
SPX2372237250331594772982.50E-36[GI:6690421]105
[LN:AF129168]
[AC:AF129168]
[PN:EIIB sorbose-PTS homolog]
[GN:sorB]
[OR:Lactobacillus casei]
SPX23732373503450915272653.30E-90“[LN:JC5618]134
[AC:JC5618]
[PN:beta-galactosidase,:lactase]
[GN:bgaC]
[CL:beta-galactosidase bga]
[OR:Bacillus circulans]
[EC:3.2.1.23]”
SPX2374237450351313933585.70E-44“[LN:JC5618]134
[AC:JC5618]
[PN:beta-galactosidase,:lactase]
[GN:bgaC]
[CL:beta-galactosidase bga]
[OR:Bacillus circulans]
[EC:3.2.1.23]”
SPX2375237550362397171427.80E-15[LN:F69750]144
[AC:F69750]
[PN:transcription regulator GntR family homolog ybgA]
[GN:ybgA]
[CL:transcription regulator GntR]
[OR:Bacillus subtilis]
SPX2376237650371304391263240“[LN:STRH_STRPN]139
[AC:P49610]
[GN:STRH]
[OR:Streptococcus pneumoniae]
[EC:3.2.1.52]
[DE:BETA-N-ACETYLHEXOSAMINIDASE PRECURSOR,]
[SP:P49610]”
SPX237723775038130390NO-HIT6
SPX237823785039433129916781.40E-227[LN:PUR8_BACSU]140
[AC:P12047]
[GN:PURB:PURE]
[OR:Bacillus subtilis]
[EC:4.3.2.2]
[DE:(GLUTAMYL-TRNA SYNTHETASE REGULATORY FACTOR)]
[SP:P12047]
SPX23792379504076228NO-HIT6
SPX23802380504138411522861.70E-65[GI:5051462]155
[LN:NME242842]
[AC:AJ242842]
[PN:putative phosphoribosylaminoimidazole]
[GN:purK]
[FN:purine nucleotide synthesis]
[OR:Neisseria meningitidis]
SPX2381238150421554655155.30E-66[GI:3892884]75
[LN:LLJ000883]
[AC:AJ000883]
[GN:purE]
[OR:Lactococcus lactis]
SPX23822382504342112635892.10E-157[GI:3892883]75
[LN:LLJ000883]
[AC:AJ000883]
[GN:purD]
[OR:Lactococcus lactis]
SPX238323835044227681NO-HIT6
SPX23842384504552315698812.30E-213[LN:PUR9_BACSU]130
[AC:P12048]
[GN:PURH:PURHJ]
[OR:Bacillus subtilis]
[EC:2.1.2.3:3.5.4.10]
[DE:(IMP SYNTHETASE) (ATIC)]]
[SP:P12048]
SPX2385238550461705101369.10E-15“[LN:VANZ_ENTFC]123
[AC:Q06242]
[GN:VANZ]
[OR:Enterococcus faecium]
[SR:,Streptococcus faecium]
[DE:VANZ PROTEIN]
[SP:Q06242]”
SPX238623865047116348NO-HIT6
SPX2387238750481825465532.20E-72[GI:6446399]115
[LN:SPU70775]
[AC:U70775]
[PN:phosphoribosylglycinamide formyltransferase]
[OR:Streptococcus pyogenes]
SPX238823885049341102310847.20E-148[GI:3150047]140
[LN:AF016634]
[AC:AF016634]
[PN:phosphoribosylformylglycinamide cyclo-ligase]
[GN:pur5]
[OR:Lactococcus lactis subsp. cremoris]
SPX238923895050481144317277.50E-248[GI:4097534]122
[LN:LLU64311]
[AC:U64311]
[PN:phosphoribosylpyrophosphate amidotransferase]
[GN:purF]
[OR:Lactococcus lactis]
SPX239023905051124337291493.00E-49“[LN:C69492]217
[AC:C69492]
[PN:phosphoribosylformylglycinamidine synthase, component II:formylglycinamide ribotide amidotransferase:phosphoribosylformylglycinamidine synthetase]
[OR:Archaeoglobus fulgidus]
[EC:6.3.5.3]”
SPX23912391505245135NO-HIT6
SPX2392239250532046128759.90E-117[LN:PUR7_STRPN]117
[AC:Q07296]
[GN:PURC]
[OR:Streptococcus pneumoniae]
[EC:6.3.2.6]
[DE:(SAICAR SYNTHETASE)]
[SP:Q07296]
SPX2393239350541243721751.90E-17“[LN:H75412]160
[AC:H75412]
[PN:spermidine/putrescine ABC transporter, periplasmic spermidine/putrescine-binding protein]
[GN:DR1305]
[OR:Deinococcus radiodurans]”
SPX239423945055431129321592.90E-302[GI:2804700]87
[LN:AF030361]
[AC:AF030361]
[PN:transposase]
[OR:Streptococcus pneumoniae]
SPX23952395505686258NO-HIT6
SPX2396239650571664983008.70E-37[LN:YEBR_ECOLI]163
[AC:P76270:O07976:O07978]
[GN:YEBR]
[OR:Escherichia coli]
[DE:HYPOTHETICAL 20.3 KD PROTEIN IN PRC-PPHA INTERGENIC REGION]
[SP:P76270:O07976:O07978]
SPX23972397505855216567497.10E-135“[LN:S13786]245
[AC:S13786:S00745:S66049:B69618]
[PN:DNA-directed DNA polymerase, III chain dnaX:DNA polymerase III (gamma and tau subunits) dnaX]
[GN:dnaX:dnaZX]
[CL:DNA-directed DNA polymerase III gamma chain]
[OR:Bacillus subtilis]
[EC:2.7.7.7]”
SPX23982398505965195NO-HIT6
SPX2399239950602577719481.70E-125[LN:V296_BACSU]109
[AC:P80866]
[GN:YURI]
[OR:Bacillus subtilis]
[DE:VEGETATIVE PROTEIN 296 (VEG296)]
[SP:P80866]
SPX24002400506142012605831.90E-87[LN:G70019]161
[AC:G70019]
[PN:conserved hypothetical protein yurX]
[GN:yurX]
[CL:Methanobacterium thermoautotrophicum ABC transporter Ycf24]
[OR:Bacillus subtilis]
SPX24012401506240912276228.60E-181[LN:F70019]105
[AC:F70019]
[PN:nifS protein homolog yurW]
[GN:yurW]
[CL:nifS protein]
[OR:Bacillus subtilis]
SPX2402240250631574712291.90E-43[LN:E70019]177
[AC:E70019]
[PN:nitrogen fixation protein nifU homolog yurV]
[GN:yurV]
[CL:Yeast nitrogen fixation protein:nitrogen fixation protein homology]
[OR:Bacillus subtilis]
SPX240324035064470141017211.20E-229[LN:D70019]161
[AC:D70019]
[PN:conserved hypothetical protein yurU]
[GN:yurU]
[CL:Methanobacterium thermoautotrophicum ABC transporter Ycf24]
[OR:Bacillus subtilis]
SPX24042404506565195NO-HIT6
SPX240524055066621861128.10E-11[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX240624065067414124220596.00E-276“[GI:1620468]105
[LN:SPDACAO]
[AC:X99400]
[PN:D,D-carboxypeptidase]
[GN:dacA]
[OR:Streptococcus pneumoniae]”
SPX240724075068370111018075.00E-255[GI:1620467]89
[LN:SPDACAO]
[AC:X99400]
[PN:membrane protein]
[OR:Streptococcus pneumoniae]
SPX24082408506973219NO-HIT6
SPX24092409507067201NO-HIT6
SPX2410241050712477412587.40E-41[LN:B69627]138
[AC:B69627]
[PN:transcription repressor of fructose operon fruR]
[GN:fruR]
[CL:regulatory protein gutR]
[OR:Bacillus subtilis]
SPX2411241150723049127252.80E-94[LN:A69627]123
[AC:A69627]
[PN:fructose 1-phosphate kinase fruB]
[GN:fruB]
[CL:6-phosphofructokinase 2]
[OR:Bacillus subtilis]
SPX24122412507376228NO-HIT6
SPX24132413507465119533714.60E-168“[LN:H69626]246
[AC:H69626]
[PN:PTS fructose-specific enzyme IIBC component fruA]
[GN:fruA]
[CL:phosphotransferase system enzyme II, fructose-specific:phosphotransferase system mannitol-specific enzyme II factor III homology]
[OR:Bacillus subtilis]”
SPX24142414507573822149344.10E-198[LN:SP3E_BACSU]126
[AC:P21458:P21459]
[GN:SPOIIIE]
[OR:Bacillus subtilis]
[DE:STAGE III SPORULATION PROTEIN E]
[SP:P21458:P21459]
SPX24152415507684252820.00017[GI:2257458]153
[LN:AB000222]
[AC:AB000222]
[GN:epr]
[FN:glycylglycine endopeptidase resistance]
[OR:Staphylococcus capitis]
[SR:Staphylococcus capitis DNA]
SPX241624165077952851247.00E-12“[LN:A70132]117
[AC:A70132]
[PN:cell division protein homolog]
[OR:Borrelia burgdorferi]
[SR:, Lyme disease spirochete]”
SPX24172417507872216NO-HIT6
SPX2418241850792206601020.00013“[LN:T06029]127
[AC:T06029]
[PN:hypothetical protein T28I19.100]
[GN:T28I19.100]
[OR:Arabidopsis thaliana]
[SR:, mouse-ear cress]”
SPX24192419508040112036988.70E-120“[LN:NIFS_LACDE]131
[AC:P31672]
[OR:Lactobacillus delbrueckii]
[SR:,subspbulgaricus]
[DE:NIFS PROTEIN HOMOLOG (FRAGMENT)]
[SP:P31672]”
SPX24202420508140512159821.40E-130[LN:THII_BACSU]121
[AC:O34595]
[GN:THII]
[OR:Bacillus subtilis]
[DE:PROBABLE THIAMINE BIOSYNTHESIS PROTEIN THII]
[SP:O34595]
SPX2421242150822106301153.40E-15[LN:G75475]100
[AC:G75475]
[PN:conserved hypothetical protein]
[GN:DR0779]
[OR:Deinococcus radiodurans]
SPX242224225083116348NO-HIT6
SPX242324235084112336NO-HIT6
SPX242424245085144432NO-HIT6
SPX24252425508661183NO-HIT6
SPX2426242650873891167822.50E-06[LN:T35924]101
[AC:T35924]
[PN:hypothetical protein SC9B5.04]
[GN:SC9B5.04]
[OR:Streptomyces coelicolor]
SPX24272427508849814941372.50E-32[GI:1841495]95
[LN:SEHSDRMS]
[AC:Y11005]
[PN:StySKI methylase]
[GN:hsdM]
[OR:Salmonella enterica]
SPX24282428508937411221093.30E-14[LN:YC18_METJA]114
[AC:Q58615]
[GN:MJ1218]
[OR:Methanococcus jannaschii]
[DE:HYPOTHETICAL PROTEIN MJ1218]
[SP:Q58615]
SPX24292429509079237NO-HIT6
SPX243024305091138414NO-HIT6
SPX2431243150922768281531.90E-22[LN:A75153]164
[AC:A75153]
[PN:integrase/recombinase xerd PAB0255]
[GN:xerD-like:PAB0255]
[CL:probable site-specific integrase/recombinase XerC]
[OR:Pyrococcus abyssi]
SPX24322432509336911071484.50E-19[GI:3057063]84
[LN:AF013165]
[AC:AF013165]
[PN:HsdS]
[GN:hsds]
[OR:Lactococcus lactis]
SPX243324335094111733511536.50E-30“[LN:T1R_ECOLI]139
[AC:P08956]
[GN:HSDR:HSR]
[OR:Escherichia coli]
[EC:3.1.21.3]
[DE:TYPE I RESTRICTION ENZYME ECOK I R PROTEIN,]
[SP:P08956]”
SPX2434243450951574711321.60E-24[LN:AHRC_BACSU]117
[AC:P17893]
[GN:AHRC]
[OR:Bacillus subtilis]
[DE:ARGININE HYDROXIMATE RESISTANCE PROTEIN]
[SP:P17893]
SPX243524355096758227412981.20E-249“[LN:PEPX_LACLC]195
[AC:P22093]
[GN:PEPX]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[EC:3.4.14.11]
[DE:PEPTIDASE) (X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE) (X-PDAP)]
[SP:P22093]”
SPX243624365097103431025635.40E-170“[LN:DP3A_BACSU]125
[AC:O34623]
[GN:DNAE]
[OR:Bacillus subtilis]
[EC:2.7.7.7]
[DE:DNA POLYMERASE III, ALPHA CHAIN,]
[SP:O34623]”
SPX24372437509863189NO-HIT6
SPX243824385099336100813562.50E-182“[LN:K6PF_LACLA]157
[AC:Q07636]
[GN:PFKA:PFK]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[EC:2.7.1.11]
[DE:(PHOSPHOHEXOKINASE)]
[SP:Q07636]”
SPX24392439510023670810078.20E-134[GI:6708108]153
[LN:AF172173]
[AC:AF172173]
[PN:pyruvate kinase]
[GN:pyk]
[FN:conversion of phosphoenolpyruvate to pyruvate]
[OR:Streptococcus thermophilus]
SPX24402440510130591510999.10E-150[GI:6708108]153
[LN:AF172173]
[AC:AF172173]
[PN:pyruvate kinase]
[GN:pyk]
[FN:conversion of phosphoenolpyruvate to pyruvate]
[OR:Streptococcus thermophilus]
SPX244124415102742221371.60E-13[LN:G71171]95
[AC:G71171]
[PN:hypothetical protein PH0571]
[GN:PH0571]
[OR:Pyrococcus horikoshii]
SPX24422442510367201733.00E-08[LN:VINT_BPL54]87
[AC:P20709]
[GN:INT]
[OR:Bacteriophage L54a]
[DE:INTEGRASE]
[SP:P20709]
SPX244324435104101303953.10E-05[GI:763050]84
[LN:BTU21935]
[AC:U21935]
[PN:repressor protein]
[OR:Bacteriophage T270]
SPX24442444510585255891.90E-08[GI:509672]128
[LN:TU2CIRPRSR]
[AC:L26219]
[PN:repressor protein]
[GN:cI]
[OR:Bacteriophage Tuc2009]
[SR:Bacteriophage Tuc2009 DNA]
SPX2445244551062918733931.90E-60[GI:4580015]78
[LN:AF049342]
[AC:AF049342]
[PN:unknown]
[OR:Treponema denticola]
SPX2446244651071283843643.60E-46[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX244724475108104312NO-HIT6
SPX244824485109239717NO-HIT6
SPX244924495110132396NO-HIT6
SPX2450245051112728161842.20E-58[LN:D69759]136
[AC:D69759]
[PN:hypothetical protein ycgQ]
[GN:ycgQ]
[CL:Bacillus subtilis hypothetical protein ycgQ]
[OR:Bacillus subtilis]
SPX2451245151123029063697.00E-86[LN:E69759]87
[AC:E69759]
[PN:hypothetical protein ycgR]
[GN:ycgR]
[OR:Bacillus subtilis]
SPX24522452511371021306441.20E-222[LN:G69773]128
[AC:G69773]
[PN:conserved hypothetical protein ydcI]
[GN:ydcI]
[CL:hypothetical protein ydcI]
[OR:Bacillus subtilis]
SPX2453245351141504502567.80E-44[GI:7007441]129
[LN:AB031213]
[AC:AB031213]
[PN:YdcK]
[GN:ydcK]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA]
SPX24542454511585255907.80E-11[LN:E70043]87
[AC:E70043]
[PN:hypothetical protein yvlC]
[GN:yvlC]
[OR:Bacillus subtilis]
SPX24552455511664192NO-HIT6
SPX2456245651172537594868.70E-81[LN:A70001]188
[AC:A70001]
[PN:ABC transporter (ATP-binding protein) homolog ytsC]
[GN:ytsC]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Bacillus subtilis]
SPX24572457511875225763.20E-05[LN:G72510]92
[AC:G72510]
[PN:hypothetical protein APE2061]
[GN:APE2061]
[OR:Aeropyrum pernix]
SPX24582458511966319892491.70E-50[LN:B70001]101
[AC:B70001]
[PN:ABC transporter (permease) homolog ytsD]
[GN:ytsD]
[OR:Bacillus subtilis]
SPX2459245951201975912302.10E-25[LN:SPBC1683]121
[AC:AL355920]
[PN:hypothetical protein]
[GN:SPBC1683.10c]
[OR:Schizosaccharomyces pombe]
[SR:fission yeast]
SPX246024605121365109511438.40E-154[GI:517210]65
[LN:SPU11799]
[AC:U11799]
[OR:Streptococcus pyogenes]
SPX24612461512261183NO-HIT6
SPX24622462512349214765853.60E-138“[LN:DCLY_BACSU]134
[AC:P21885:P26934]
[GN:CAD]
[OR:Bacillus subtilis]
[EC:4.1.1.18]
[DE:LYSINE DECARBOXYLASE, (LDC)]
[SP:P21885:P26934]”
SPX24632463512479237NO-HIT6
SPX246424645125176528831.20E-07“[GI:6009430]140
[LN:AB024946]
[AC:AB024946]
[GN:orf54]
[OR:Escherichia coli]
[SR:Escherichia coli (sub_species:enteropathogenic, strain:B171]”
SPX2465246551262878614395.40E-79[LN:SPEE_BACSU]99
[AC:P70998]
[GN:SPEE]
[OR:Bacillus subtilis]
[EC:2.5.1.16]
[DE:(SPDSY)]
[SP:P70998]
SPX246624665127420126010902.30E-187[LN:C81435]107
[AC:C81435]
[PN:hypothetical protein Cj0172c [imported]]
[GN:Cj0172c]
[OR:Campylobacter jejuni]
SPX24672467512837611284117.60E-103[LN:E75398]104
[AC:E75398]
[PN:carboxynorspermidine decarboxylase]
[GN:DR1410]
[OR:Deinococcus radiodurans]
SPX24682468512936210865303.80E-94[GI:5712716]80
[LN:AF153708]
[AC:AF153708]
[PN:unknown]
[OR:Pseudomonas sp. BG33R]
SPX2469246951302928765851.20E-110[GI:5262946]106
[LN:LES19104]
[AC:Y19104]
[PN:beta-alanine synthase]
[OR:Lycopersicon esculentum]
[SR:tomato]
SPX2470247051312708102096.80E-43[LN:YXEH_BACSU]141
[AC:P54947]
[GN:YXEH:IP1B]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 30.2 KD PROTEIN IN IDH-DEOR INTERGENIC REGION]
[SP:P54947]
SPX24712471513274222NO-HIT6
SPX247224725133224672902.30E-09[LN:E69787]87
[AC:E69787]
[PN:hypothetical protein ydiL]
[GN:ydiL]
[OR:Bacillus subtilis]
SPX2473247351343039092295.80E-46[LN:T44638]172
[AC:T44638]
[PN:capsular polysaccharide biosynthesis protein cpsY [imported]]
[GN:cpsY]
[CL:probable transcription regulator lsyR]
[OR:Streptococcus agalactiae]
SPX2474247451351544621971.80E-31[LN:LSPA_BACSU]140
[AC:Q45479]
[GN:LSPA:LSP]
[OR:Bacillus subtilis]
[EC:3.4.23.36]
[DE:PEPTIDASE) (SIGNAL PEPTIDASE II) (SPASE II)]
[SP:Q45479]
SPX2475247551362968888881.80E-117[LN:YLYB_BACSU]158
[AC:Q45480:O31732]
[GN:YLYB]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 33.7 KD PROTEIN IN LSP-PYRR INTERGENIC REGION (ORF-X)]
[SP:Q45480:O31732]
SPX24762476513762818844611.70E-56[GI:1914872]88
[LN:SPZ82001]
[AC:Z82001]
[PN:PCPA]
[GN:pcpA]
[OR:Streptococcus pneumoniae]
SPX247724775138377113113874.40E-185[LN:F81125]107
[AC:F81125]
[PN:glutamate 5-kinase NMB1069 [imported]]
[GN:NMB1069]
[OR:Neisseria meningitidis]
SPX247824785139421126315301.10E-204[GI:7413448]130
[LN:AE002457]
[AC:AE002457:AE002098]
[PN:gamma-glutamyl phosphate reductase]
[GN:NMB1068]
[OR:Neisseria meningitidis]
SPX2479247951402667983963.30E-67“[LN:PROC_ARATH]176
[AC:P54904]
[GN:PROC1]
[OR:Arabidopsis thaliana]
[SR:,Mouse-ear cress]
[EC:1.5.1.2]
[DE:PYRROLINE-5-CARBOXYLATE REDUCTASE, (P5CR) (P5C REDUCTASE)]
[SP:P54904]”
SPX2480248051412136395284.30E-68“[LN:KTHY_BACSU]125
[AC:P37537]
[GN:TMK]
[OR:Bacillus subtilis]
[EC:2.7.4.9]
[DE:THYMIDYLATE KINASE, (DTMP KINASE)]
[SP:P37537]”
SPX24812481514284252NO-HIT6
SPX2482248251432978912444.80E-37“[LN:HOLB_BACSU]128
[AC:P37540]
[GN:HOLB]
[OR:Bacillus subtilis]
[EC:2.7.7.7]
[DE:DNA POLYMERASE III, DELTA′SUBUNIT,]
[SP:P37540]”
SPX2483248351441063181039.60E-09[LN:YABA_BACSU]137
[AC:P37542]
[GN:YABA]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 14.1 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]
[SP:P37542]
SPX2484248451452908706181.60E-84[LN:YABC_BACSU]137
[AC:P37544]
[GN:YABC]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 33.0 KD PROTEIN IN XPAC-ABRB INTERGENIC REGION]
[SP:P37544]
SPX2485248551461825463622.50E-61[LN:S62019]177
[AC:S62019]
[PN:hypothetical protein YDR540c:hypothetical protein D3703.8]
[GN:YDR540c]
[CL:Saccharomyces hypothetical protein YDR540c]
[OR:Saccharomyces cerevisiae]
SPX248624865147168504822.90E-09[GI:6690333]102
[LN:AF117259]
[AC:AF117259]
[PN:replication protein]
[GN:repX]
[OR:Staphylococcus aureus]
SPX2487248751481504504005.20E-51[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX2488248851491344023701.00E-54[LN:S52544]71
[AC:S52544]
[PN:ISL2 protein]
[OR:Lactobacillus helveticus]
SPX24892489515091273NO-HIT6
SPX24902490515144513355851.40E-196[LN:GID_BACSU]87
[AC:P39815]
[GN:GID]
[OR:Bacillus subtilis]
[DE:GID PROTEIN]
[SP:P39815]
SPX2491249151522467387932.20E-104[LN:F69708]120
[AC:F69708]
[PN:uridylate kinase smbA]
[GN:smbA]
[CL:uridine 5′-monophosphate kinase]
[OR:Bacillus subtilis]
SPX249224925153146438NO-HIT6
SPX2493249351541865585452.50E-69[LN:G69626]121
[AC:G69626]
[PN:ribosome recycling factor frr]
[GN:frr]
[CL:ribosome releasing factor]
[OR:Bacillus subtilis]
SPX249424945155139417NO-HIT6
SPX2495249551562858551803.70E-45[GI:2145404]71
[LN:BSY09476]
[AC:Y09476]
[PN:YitL]
[OR:Bacillus subtilis]
SPX249624965157722161341.00E-13[LN:A69931]87
[AC:A69931]
[PN:hypothetical protein yozE]
[GN:yozE]
[OR:Bacillus subtilis]
SPX2497249751583239699561.30E-128[LN:PHOL_BACSU]95
[AC:P46343]
[GN:PHOH]
[OR:Bacillus subtilis]
[DE:PHOH-LIKE PROTEIN]
[SP:P46343]
SPX24982498515965195NO-HIT6
SPX249924995160167501870.00031[LN:E75272]90
[AC:E75272]
[PN:hypothetical protein]
[GN:DR2441]
[OR:Deinococcus radiodurans]
SPX250025005161922762531.30E-28“[LN:DHA_BACSU]151
[AC:Q08352]
[GN:ALD:SPOVN]
[OR:Bacillus subtilis]
[EC:1.4.1.1]
[DE:ALANINE DEHYDROGENASE, (STAGE V SPORULATION PROTEIN N)]
[SP:Q08352]”
SPX250125015162651951685.10E-17“[LN:JE0388]152
[AC:JE0388]
[PN:alanine dehydrogenase,]
[CL:alanine dehydrogenase:alanine dehydrogenase homology]
[OR:Enterobacter aerogenes]
[EC:1.4.1.1]”
SPX250225025163732192393.30E-27“[LN:S74638]233
[AC:S74638]
[PN:alanine dehydrogenase:hypothetical protein sll1682:hypothetical protein sll1682]
[CL:alanine dehydrogenase:alanine dehydrogenase homology]
[OR:Synechocystis sp.]
[SR:PCC 6803, , PCC 6803]
[SR:PCC 6803, ]”
SPX2503250351641424264052.90E-56“[LN:DHA_BACSU]151
[AC:Q08352]
[GN:ALD:SPOVN]
[OR:Bacillus subtilis]
[EC:1.4.1.1]
[DE:ALANINE DEHYDROGENASE, (STAGE V SPORULATION PROTEIN N)]
[SP:Q08352]”
SPX2504250451651965881478.00E-20[LN:C69895]170
[AC:C69895]
[PN:conserved hypothetical protein yoaA]
[GN:yoaA]
[CL:Escherichia coli ribosomal-protein-alanine N-acetyltransferase rimJ]
[OR:Bacillus subtilis]
SPX25052505516621765110626.40E-138[GI:3211753]104
[LN:AF052208]
[AC:AF052208]
[PN:competence protein]
[GN:celA]
[OR:Streptococcus pneumoniae]
SPX250625065167459137722130[GI:3211754]104
[LN:AF052208]
[AC:AF052208]
[PN:competence protein]
[GN:celB]
[OR:Streptococcus pneumoniae]
SPX25072507516830691812151.90E-162[GI:3211754]104
[LN:AF052208]
[AC:AF052208]
[PN:competence protein]
[GN:celB]
[OR:Streptococcus pneumoniae]
SPX2508250851691965881641.60E-26[LN:YYBJ_BACSU]95
[AC:P37494]
[GN:YYBJ]
[OR:Bacillus subtilis]
[DE:INTERGENIC REGION]
[SP:P37494]
SPX2509250951703921176NO-HIT6
SPX25102510517188264NO-HIT6
SPX2511251151721965885894.10E-77[LN:IF3_LISMO]116
[AC:O53084]
[GN:INFC]
[OR:Listeria monocytogenes]
[DE:TRANSLATION INITIATION FACTOR IF-3]
[SP:O53084]
SPX251225125173672012351.10E-28[LN:R5BS35]137
[AC:S05347]
[PN:ribosomal protein L35]
[GN:rpmI]
[CL:Escherichia coli ribosomal protein L35]
[OR:Bacillus stearothermophilus]
SPX2513251351741203604769.30E-63[LN:RL20_BACSU]103
[AC:P55873]
[GN:RPLT]
[OR:Bacillus subtilis]
[DE:50S RIBOSOMAL PROTEIN L20]
[SP:P55873]
SPX2514251451751273811306.20E-24[LN:LGUL_HAEIN]147
[AC:P44638]
[GN:GLOA:HI0323]
[OR:Haemophilus influenzae]
[EC:4.4.1.5]
[DE:(S-D-LACTOYLGLUTATHIONE METHYLGLYOXAL LYASE)]
[SP:P44638]
SPX2515251551761905703542.10E-55[LN:YLXD_BACCL]139
[AC:P46536]
[OR:Bacillus caldolyticus]
[DE:HYPOTHETICAL 27.6 KD PROTEIN IN PYRAB-PYRD INTERGENIC REGION (ORF2)]
[SP:P46536]
SPX251625165177942821727.70E-23[LN:YLXD_BACCL]139
[AC:P46536]
[OR:Bacillus caldolyticus]
[DE:HYPOTHETICAL 27.6 KD PROTEIN IN PYRAB-PYRD INTERGENIC REGION (ORF2)]
[SP:P46536]
SPX2517251751783139395638.20E-147“[LN:PYDB_LACLC]159
[AC:P54322]
[GN:PYRDB]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[EC:1.3.3.1]
[DE:(DHODEHASE B) (DHODB)]
[SP:P54322]”
SPX251825185179722216623900[GI:4218533]167
[LN:SPN010312]
[AC:AJ010312]
[PN:endo-beta-N-acetylglucosaminidase]
[GN:lytB]
[FN:cell wall degradation and cell separation]
[OR:Streptococcus pneumoniae]
SPX251925195180561168327670[GI:6175915]132
[LN:AF181976]
[AC:AF181976]
[PN:adherence and virulence protein A]
[GN:pavA]
[FN:adhesin]
[OR:Streptococcus pneumoniae]
SPX25202520518177231NO-HIT6
SPX2521252151821664987055.20E-92[GI:2749950]66
[LN:AF000954]
[AC:AF000954]
[OR:Streptococcus mutans]
SPX2522252251831323965076.90E-71[LN:A36933]134
[AC:A36933]
[PN:diacylglycerol kinase homolog]
[CL:Bacillus subtilis diacylglycerol kinase dgkA]
[OR:Streptococcus mutans]
SPX25232523518430090015021.40E-204[GI:5305399]95
[LN:AF072811]
[AC:AF072811]
[PN:GTPase Era]
[GN:era]
[OR:Streptococcus pneumoniae]
SPX2524252451852758258921.90E-119[LN:FPG_STRMU]110
[AC:P55045]
[GN:MUTM:FPG]
[OR:Streptococcus mutans]
[EC:3.2.2.23]
[DE:GLYCOSYLASE)]
[SP:P55045]
SPX25252525518661183NO-HIT6
SPX2526252651872036091672.40E-32“[LN:Y553_SYNY3]140
[AC:Q55515]
[GN:SLR0553]
[OR:Synechocystis sp]
[SR:,strain PCC 6803]
[DE:HYPOTHETICAL 22.5 KD PROTEIN SLR0553]
[SP:Q55515]”
SPX25272527518867201NO-HIT6
SPX252825285189400120019899.60E-280[GI:3820455]118
[LN:SPN7367]
[AC:AJ007367]
[PN:multi-drug resistance efflux pump]
[GN:pmrA]
[OR:Streptococcus pneumoniae]
SPX252925295190501501778.70E-20“[LN:RL33_LACLA]145
[AC:P27167]
[GN:RPMG]
[OR:Lactococcus lactis]
[SR:,subsplactis:Streptococcus lactis]
[DE:50S RIBOSOMAL PROTEIN L33]
[SP:P27167]”
SPX25302530519178234828.20E-06[LN:A70028]120
[AC:A70028]
[PN:hypothetical protein yvaL]
[GN:yvaL]
[CL:protein-export protein secG]
[OR:Bacillus subtilis]
SPX25312531519278523555644.00E-180[LN:G70027]144
[AC:G70027]
[PN:conserved hypothetical protein yvaJ]
[GN:yvaJ]
[CL:virulence-associated protein vacB homolog]
[OR:Bacillus subtilis]
SPX2532253251931564687931.30E-104[GI:3211758]88
[LN:AF052209]
[AC:AF052209]
[PN:VacB homolog]
[OR:Streptococcus pneumoniae]
SPX25332533519428786114998.30E-203[GI:4883699]119
[LN:AF079807]
[AC:AF079807]
[PN:tellurite resistance protein TehB]
[GN:tehB]
[OR:Streptococcus pneumoniae]
SPX2534253451951293873265.30E-41[GI:3211758]88
[LN:AF052209]
[AC:AF052209]
[PN:VacB homolog]
[OR:Streptococcus pneumoniae]
SPX25352535519674222NO-HIT6
SPX2536253651973189548005.10E-182[GI:3211759]104
[LN:AF052209]
[AC:AF052209]
[PN:competence protein]
[GN:coiA]
[OR:Streptococcus pneumoniae]
SPX253725375198601180321592.10E-292“[LN:PEPB_STRAG]129
[AC:Q53778]
[GN:PEPB]
[OR:Streptococcus agalactiae]
[EC:3.4.24.-]
[DE:GROUP B OLIGOPEPTIDASE PEPB,]
[SP:Q53778]”
SPX2538253851992387146804.90E-90[GI:1771204]86
[LN:LLLVSFPEP]
[AC:X99710]
[PN:methyltransferase]
[OR:Lactococcus lactis]
SPX2539253952003149421893.10E-32[LN:PRTM_LACPA]121
[AC:Q02473]
[GN:PRTM]
[OR:Lactobacillus paracasei]
[DE:PROTEASE MATURATION PROTEIN PRECURSOR]
[SP:Q02473]
SPX2540254052011143425674.00E-74[GI:1490399]90
[LN:SPPARCETP]
[AC:Z67739]
[PN:DNA transposase]
[OR:Streptococcus pneumoniae]
SPX2541254152021915734222.30E-53[LN:B30868]81
[AC:B30868]
[PN:hypothetical protein 1]
[OR:Streptococcus agalactiae]
SPX25422542520391273NO-HIT6
SPX25432543520464192NO-HIT6
SPX254425445205207621864.90E-12“[LN:T46083]190
[AC:T46083]
[PN:hypothetical protein T20E23.120]
[CL:Aquifex aeolicus phosphoglycerate mutase:phosphoglycerate mutase homology]
[OR:Arabidopsis thaliana]
[SR:, mouse-ear cress]”
SPX2545254552061614832101.70E-35“[LN:EBSC_ENTFA]115
[AC:P36922]
[OR:Enterococcus faecalis]
[SR:,Streptococcus faecalis]
[DE:EBSC PROTEIN]
[SP:P36922]”
SPX2546254652072818431286.60E-17[LN:B72411]96
[AC:B72411]
[PN:conserved hypothetical protein]
[GN:TM0164]
[OR:Thermotoga maritima]
SPX2547254752082637891022.10E-09[GI:1865711]116
[LN:BPPLYBA]
[AC:Y11477]
[PN:endolysin]
[GN:plyBa]
[FN:cell wall hydrolase]
[OR:Bacteriophage Bastille]
SPX254825485209460138011801.90E-156[LN:S66080]237
[AC:S66080:I40018:C69629:S05371:S18903]
[PN:UDP-N-acetylglucosamine pyrophosphorylase gcaD:cell division protein tms26:tms protein]
[GN:gcaD:tms26]
[CL:N-acetylglucosamine-1-phosphate uridyltransferase]
[OR:Bacillus subtilis]
SPX2549254952101825461672.40E-45[LN:YQKG_BACSU]137
[AC:P54570]
[GN:YQKG]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 21.0 KD PROTEIN IN GLNQ-ANSR INTERGENIC REGION]
[SP:P54570]
SPX255025505211105315NO-HIT6
SPX2551255152122316934771.60E-61[LN:PFS_ECOLI]110
[AC:P24247]
[GN:PFS]
[OR:Escherichia coli]
[EC:3.2.2.16:3.2.2.9]
[DE:(EC 3.2.2.9)]]
[SP:P24247]
SPX2552255252131644921241.90E-12[GI:2769573]79
[LN:LLCPJW565]
[AC:Y12736]
[OR:Lactococcus lactis subsp. cremoris]
SPX2553255352141975911371.00E-08“[LN:DPO3_BACSU]154
[AC:P13267]
[GN:POLC:DNAF:MUTI]
[OR:Bacillus subtilis]
[EC:2.7.7.7]
[DE:DNA POLYMERASE III, ALPHA CHAIN POLC-TYPE, (POLIII)]
[SP:P13267]”
SPX2554255452152577711051.40E-11[LN:E69827]159
[AC:E69827]
[PN:glycerophosphodiester phosphodiesterase homolog yhdW]
[GN:yhdW]
[CL:glycerophosphodiester phosphodiesterase]
[OR:Bacillus subtilis]
SPX2555255552161163485775.80E-76[GI:4200438]96
[LN:AF026471]
[AC:AF026471]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX255625565217471411865.40E-22[GI:5019553]97
[LN:SPN239004]
[AC:AJ239004]
[PN:putative transposase]
[OR:Streptococcus pneumoniae]
SPX25572557521867201NO-HIT6
SPX255825585219211633NO-HIT6
SPX255925595220100300840.00082[GI:1707287]148
[LN:BBU80959]
[AC:U80959:L78251]
[PN:putative outer membrane protein]
[GN:ospFi]
[OR:Borrelia burgdorferi]
[SR:Lyme disease spirochete]
SPX2560256052212367082671.40E-53[LN:YE54_HAEIN]141
[AC:P44202]
[GN:HI1454]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI1454]
[SP:P44202]
SPX2561256152221865582396.40E-28[LN:YE53_HAEIN]136
[AC:Q57127:O05062]
[GN:HI1453]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI1453 PRECURSOR]
[SP:Q57127:O05062]
SPX25622562522346413924811.60E-122[LN:D69814]120
[AC:D69814]
[PN:metabolite transporter homolog yfnA]
[GN:yfnA]
[CL:arginine permease]
[OR:Bacillus subtilis]
SPX2563256352243089249857.10E-129[LN:T46757]95
[AC:T46757]
[PN:lipoprotein lmb [validated]]
[GN:lmb]
[OR:Streptococcus agalactiae]
SPX25642564522583925174093.50E-104[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX256525655226104031204001.50E-93[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX25662566522763189NO-HIT6
SPX256725675228631892401.40E-26[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX256825685229672011043.80E-14[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX2569256952301614831524.70E-20[LN:T46758]90
[AC:T46758]
[PN:hypothetical protein [imported]]
[OR:Streptococcus agalactiae]
SPX25702570523180240NO-HIT6
SPX25712571523286258NO-HIT6
SPX2572257252331454351076.20E-05[GI:7228476]121
[LN:AF163151]
[AC:AF163151]
[PN:dentin sialophosphoprotein precursor]
[GN:DSPP]
[OR:Homo sapiens]
[SR:human]
SPX25732573523440812249617.20E-190“[LN:PEPT_LACLC]185
[AC:P42020]
[GN:PEPT]
[OR:Lactococcus lactis]
[SR:,subspcremoris:Streptococcus cremoris]
[EC:3.4.11.-]
[DE:PEPTIDASE T, (AMINOTRIPEPTIDASE) (TRIPEPTIDASE)]
[SP:P42020]”
SPX25742574523536510952154.70E-41[LN:HEMZ_BACSU]108
[AC:P32396]
[GN:HEMH:HEMF]
[OR:Bacillus subtilis]
[EC:4.99.1.1]
[DE:SYNTHETASE)]
[SP:P32396]
SPX2575257552361263781492.80E-25[GI:6136300]90
[LN:AF065159]
[AC:AF065159]
[PN:MscL]
[GN:mscL]
[OR:Bradyrhizobium japonicum]
SPX25762576523787261NO-HIT6
SPX2577257752381293871803.60E-29“[LN:T44787]136
[AC:T44787]
[PN:glucokinase, [imported]]
[CL:glucose kinase:glucose kinase homology]
[OR:Bacillus megaterium]
[EC:2.7.1.2]”
SPX25782578523988264610.0009[GI:2897104]145
[LN:AF020798]
[AC:AF020798]
[PN:putative host cell surface-exposed lipoprotein]
[OR:Streptococcus thermophilus bacteriophage TP-J34]
SPX2579257952402738192791.60E-30“[GI:4218526]153
[LN:SPAJ9639]
[AC:AJ009639]
[PN:1,4-beta-N-acetylmuramidase]
[GN:lytC]
[FN:lysis of cell wall peptidoglycan]
[OR:Streptococcus pneumoniae]”
SPX25802580524151015302896.20E-30“[GI:4218526]153
[LN:SPAJ9639]
[AC:AJ009639]
[PN:1,4-beta-N-acetylmuramidase]
[GN:lytC]
[FN:lysis of cell wall peptidoglycan]
[OR:Streptococcus pneumoniae]”
SPX25812581524257417223396.40E-76“[LN:A71951]140
[AC:A71951]
[PN:p-aminobenzoate synthetase]
[GN:pabB]
[OR:Helicobacter pylori]
[SR:strain J99, , strain J99]
[SR:strain J99, ]”
SPX2582258252431964589270270[GI:6911257]115
[LN:AF221126]
[AC:AF221126]
[PN:putative zinc metalloprotease]
[GN:zmpB]
[OR:Streptococcus pneumoniae]
SPX25832583524478234NO-HIT6
SPX258425845245108324717.10E-06[GI:501027]97
[LN:TBU01849]
[AC:U01849]
[OR:Kinetoplast Trypanosoma brucei]
[SR:Trypanosoma brucei]
SPX2585258552461885643921.60E-49[LN:YWLG_BACSU]147
[AC:P39157]
[GN:YWLG:IPC-33D]
[OR:Bacillus subtilis]
[DE:HYPOTHETICAL 19.4 KD PROTEIN IN SPOIIR-GLYC INTERGENIC REGION]
[SP:P39157]
SPX258625865247378113418627.80E-253[GI:6911256]111
[LN:AF221126]
[AC:AF221126]
[PN:putative histidine kinase]
[GN:zmpS]
[OR:Streptococcus pneumoniae]
SPX25872587524863189NO-HIT6
SPX2588258852491865588985.90E-119[GI:6911256]111
[LN:AF221126]
[AC:AF221126]
[PN:putative histidine kinase]
[GN:zmpS]
[OR:Streptococcus pneumoniae]
SPX25892589525024673812372.00E-167[GI:6911255]113
[LN:AF221126]
[AC:AF221126]
[PN:putative response regulator]
[GN:zmpR]
[OR:Streptococcus pneumoniae]
SPX259025905251371111311101.40E-147[LN:YE55_HAEIN]112
[AC:P45213]
[GN:HI1455]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI1455]
[SP:P45213]
SPX2591259152521985943359.20E-41[LN:YE53_HAEIN]136
[AC:Q57127:O05062]
[GN:HI1453]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL PROTEIN HI1453 PRECURSOR]
[SP:Q57127:O05062]
SPX2592259252532377111393.50E-49[LN:YE54_HAEIN]141
[AC:P44202]
[GN:HI1454]
[OR:Haemophilus influenzae]
[DE:HYPOTHETICAL CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI1454]
[SP:P44202]
SPX2593259352542878613124.30E-47[GI:3608389]79
[LN:AF071085]
[AC:AF071085]
[PN:Orfde2]
[OR:Enterococcus faecalis]
SPX25942594525568520555641.00E-82[LN:E70040]128
[AC:E70040]
[PN:conserved hypothetical protein yvgP]
[GN:yvgP]
[CL:hypothetical protein yvgP]
[OR:Bacillus subtilis]
SPX25952595525664192NO-HIT6
SPX25962596525785255NO-HIT6
SPX25972597525863189NO-HIT6
SPX2598259852591885642211.00E-42[LN:E69999]87
[AC:E69999]
[PN:hypothetical protein ytqB]
[GN:ytqB]
[OR:Bacillus subtilis]
SPX2599259952601494473296.50E-47[LN:D69999]165
[AC:D69999]
[PN:conserved hypothetical protein ytqA]
[GN:ytqA]
[CL:Methanococcus jannaschii conserved hypothetical protein MJ0486]
[OR:Bacillus subtilis]
SPX260026005261842522092.10E-24[LN:D69999]165
[AC:D69999]
[PN:conserved hypothetical protein ytqA]
[GN:ytqA]
[CL:Methanococcus jannaschii conserved hypothetical protein MJ0486]
[OR:Bacillus subtilis]
SPX2601260152621464382102.60E-23[LN:D69999]165
[AC:D69999]
[PN:conserved hypothetical protein ytqA]
[GN:ytqA]
[CL:Methanococcus jannaschii conserved hypothetical protein MJ0486]
[OR:Bacillus subtilis]
SPX260226025263120360NO-HIT6
SPX260326035264822461821.20E-19[GI:1022726]129
[LN:SHU35635]
[AC:U35635]
[PN:unknown]
[OR:Staphylococcus haemolyticus]
[SR:Staphylococcus haemolyticus strain=Y176]
SPX2604260452652086241561.10E-37“[GI:6332767]194
[LN:AB033763]
[AC:AB033763:AB014419:AB014429:AB014439]
[PN:hypothetical protein]
[OR:Staphylococcus aureus]
[SR:Staphylococcus aureus (strain:NCTC10442) DNA, clone_lib:Lambda das]”
SPX260526055266217365193092.70E-130[GI:6468240]129
[LN:SCF81]
[AC:AL133171]
[PN:putative secreted beta-galactosidase]
[GN:SCF81.25c]
[OR:Streptomyces coelicolor A3(2)]
SPX26062606526762186NO-HIT6
SPX26072607526864192NO-HIT6
SPX2608260852691444321846.10E-21[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX260926095270262786922.70E-11“[LN:SGCC_ECOLI]134
[AC:P39365]
[GN:SGCC]
[OR:Escherichia coli]
[DE:PUTATIVE PHOSPHOTRANSFERASE ENZYME II, C COMPONENT SGCC]
[SP:P39365]”
SPX2610261052712316932313.70E-25“[GI:1736815]201
[LN:D90848]
[AC:D90848:AB001340]
[PN:PTS system, Galactitol-specific IIC component]
[GN:gatC]
[OR:Escherichia coli]
[SR:Escherichia coli (strain:K12) DNA, clone_lib:Kohara lambda minise]”
SPX261126115272102306NO-HIT6
SPX261226125273159477955.10E-13“[GI:4512375]181
[LN:AB011837]
[AC:AB011837]
[PN:phosphotransferase system (PTS)]
[GN:fruA]
[OR:Bacillus halodurans]
[SR:Bacillus halodurans (strain:C-125) DNA, clone_lib:lambda no.9]”
SPX26132613527421396417105560[GI:5726291]134
[LN:AF127143]
[AC:AF127143]
[PN:cell wall-associated serine proteinase precursor]
[GN:prtA]
[OR:Streptococcus pneumoniae]
SPX261426145275682041362.70E-14[LN:T30285]79
[AC:T30285]
[PN:hypothetical protein]
[OR:Streptococcus pneumoniae]
SPX26152615527666198NO-HIT6
SPX2616261652772627861072.30E-18[GI:7635999]136
[LN:SCE6]
[AC:AL353832]
[PN:putative integral membrane transport protein.]
[GN:SCE6.32c]
[OR:Streptomyces coelicolor A3(2)]
SPX2617261752782878611132.80E-10[GI:7636000]126
[LN:SCE6]
[AC:AL353832]
[PN:putative integral membrane protein.]
[GN:SCE6.33c]
[OR:Streptomyces coelicolor A3(2)]
SPX2618261852793189546011.60E-83“[LN:G75548]184
[AC:G75548]
[PN:ABC transporter, ATP-binding protein]
[GN:DR0205]
[CL:unassigned ATP-binding cassette proteins:ATP-binding cassette homology]
[OR:Deinococcus radiodurans]”
SPX26192619528083249NO-HIT6
SPX262026205281132396NO-HIT6
SPX2621262152821584741233.70E-11[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX2622262252832306907659.20E-100[LN:RL1_BACST]111
[AC:P04447]
[GN:RPLA]
[OR:Bacillus stearothermophilus]
[DE:50S RIBOSOMAL PROTEIN L1]
[SP:P04447]
SPX2623262352841424265964.50E-77[LN:S38871]133
[AC:S38871]
[PN:ribosomal protein L11]
[GN:rplK]
[CL:Escherichia coli ribosomal protein L11]
[OR:Staphylococcus carnosus]
SPX26242624528575225NO-HIT6
SPX2625262552862397171333.00E-20[GI:2529473]96
[LN:AF006665]
[AC:AF006665]
[PN:YokZ]
[GN:yokZ]
[FN:unknown]
[OR:Bacillus subtilis]
SPX26262626528760180NO-HIT6
SPX2627262752881705101037.80E-07[LN:A81062]119
[AC:A81062]
[PN:conserved hypothetical protein NMB1619 [imported]]
[GN:NMB1619]
[OR:Neisseria meningitidis]
SPX262826285289722161871.80E-19[LN:B71121]142
[AC:B71121]
[PN:hypothetical protein PH0737]
[GN:PH0737]
[CL:thermophilic aminopeptidase I alpha chain]
[OR:Pyrococcus horikoshii]
SPX2629262952901995973064.10E-72[LN:C69830]131
[AC:C69830]
[PN:glucanase homolog yhfE]
[GN:yhfE]
[CL:thermophilic aminopeptidase I alpha chain]
[OR:Bacillus subtilis]
SPX2630263052911143421456.70E-14[GI:2315995]112
[LN:SAU87144]
[AC:U87144]
[PN:branched-chain amino acid carrier protein]
[OR:Staphylococcus aureus]
SPX26312631529244713413916.60E-90[LN:BRNQ_BACSU]124
[AC:P94499:O07082]
[GN:BRNQ]
[OR:Bacillus subtilis]
[DE:CHAIN AMINO ACID UPTAKE CARRIER)]
[SP:P94499:O07082]
SPX26322632529363189883.10E-06“[LN:YC61_SYNY3]140
[AC:P73801]
[GN:SLR1261]
[OR:Synechocystis sp]
[SR:,strain PCC 6803]
[DE:HYPOTHETICAL 19.1 KD PROTEIN SLR1261]
[SP:P73801]”
SPX263326335294802401001.90E-17[GI:1914870]81
[LN:SPZ82001]
[AC:Z82001]
[PN:unknown]
[OR:Streptococcus pneumoniae]
SPX2634263452951935795487.70E-95[GI:3212185]140
[LN:U32707]
[AC:U32707:L42023]
[PN:H. influenzae predicted coding region HI0220.2]
[GN:HI0220.2]
[OR:Haemophilus influenzae Rd]
SPX26352635529646714016464.20E-200[GI:2160707]79
[LN:LLU78036]
[AC:U78036]
[PN:dipeptidase]
[OR:Lactococcus lactis]
SPX2636263652972026061132.60E-17“[LN:NOX_THETH]158
[AC:Q60049:Q53306]
[GN:NOX]
[OR:Thermus aquaticus]
[SR:,subspthermophilus]
[EC:1.6.99.3]
[DE:(NADH:OXYGEN OXIDOREDUCTASE)]
[SP:Q60049:Q53306]”
SPX26372637529880240NO-HIT6
SPX2638263852992678011412.90E-22[GI:2108229]121
[LN:LFU97348]
[AC:U97348]
[PN:basic surface protein]
[FN:L-cystine transporter]
[OR:Lactobacillus fermentum]
SPX2639263953002788341066.20E-12[LN:G75297]167
[AC:G75297]
[PN:conserved hypothetical protein]
[GN:DR2233]
[CL:probable phosphoesterase MJ0912:phosphoesterase core homology]
[OR:Deinococcus radiodurans]
SPX264026405301615184518825.00E-256[LN:UVRC_BACSU]104
[AC:P14951]
[GN:UVRC]
[OR:Bacillus subtilis]
[DE:EXCINUCLEASE ABC SUBUNIT C]
[SP:P14951]
SPX264126415302241723NO-HIT6
SPX2642264253034111233953.90E-07[LN:SPN250764]120
[AC:AJ250764]
[PN:MurM protein]
[GN:murM]
[FN:serine/alanine adding enzyme]
[OR:Streptococcus pneumoniae]
SPX264326435304407122120883.50E-283[LN:SPN277484]152
[AC:AJ277484]
[PN:beta-lactam resistance factor]
[GN:fibA]
[FN:putative role in peptidoglycan crosslinking]
[OR:Streptococcus pneumoniae]
SPX2644264453052607804827.10E-100[GI:7453516]113
[LN:AF157484]
[AC:AF157484]
[PN:tributyrin esterase]
[GN:estA]
[OR:Lactococcus lactis subsp. lactis]
SPX26452645530655416625811.80E-136[LN:H69884]139
[AC:H69884]
[PN:conserved hypothetical protein ymfA]
[GN:ymfA]
[CL:conserved hypothetical protein MG139]
[OR:Bacillus subtilis]
SPX26462646530764719415293.20E-120[LN:H69980]113
[AC:H69980]
[PN:single-strand DNA-specific exonuclease homolog yrvE]
[GN:yrvE]
[OR:Bacillus subtilis]
SPX26472647530874122235298.40E-150[LN:H69980]113
[AC:H69980]
[PN:single-strand DNA-specific exonuclease homolog yrvE]
[GN:yrvE]
[OR:Bacillus subtilis]
SPX2648264853092537595278.90E-103[LN:GLNQ_BACST]132
[AC:P27675]
[GN:GLNQ]
[OR:Bacillus stearothermophilus]
[DE:GLUTAMINE TRANSPORT ATP-BINDING PROTEIN GLNQ]
[SP:P27675]
SPX26492649531065195690.00063[LN:E72756]92
[AC:E72756]
[PN:hypothetical protein APE0042]
[GN:APE0042]
[OR:Aeropyrum pernix]
SPX26502650531173219929.10E-12[LN:G72510]92
[AC:G72510]
[PN:hypothetical protein APE2061]
[GN:APE2061]
[OR:Aeropyrum pernix]
SPX2651265153122657954222.40E-66[LN:PEB1_CAMJE]131
[AC:P45678]
[GN:PEB1A]
[OR:Campylobacter jejuni]
[DE:MAJOR CELL-BINDING FACTOR PRECURSOR (CBF1) (PEB1)]
[SP:P45678]
SPX2652265253132266784003.80E-74[LN:G81365]144
[AC:G81365]
[PN:probable ABC-type amino-acid transporter permease protein Cj0920c [imported]]
[GN:Cj0920c]
[OR:Campylobacter jejuni]
SPX2653265353142206602342.00E-50[LN:F69633]145
[AC:F69633]
[PN:glutamine ABC transporter (membrane protein) glnP]
[GN:glnP]
[CL:histidine permease protein M]
[OR:Bacillus subtilis]
SPX2654265453154011203787.00E-08[GI:1255667]136
[LN:PSEORF1]
[AC:D84146]
[PN:reductase]
[GN:pahA]
[OR:Pseudomonas aeruginosa]
[SR:Pseudomonas aeruginosa (strain:PaK1) DNA]
SPX26552655531629488214983.00E-201“[LN:ALF_STRPN]130
[AC:O65944]
[GN:FBA]
[OR:Streptococcus pneumoniae]
[EC:4.1.2.13]
[DE:FRUCTOSE-BISPHOSPHATE ALDOLASE,]
[SP:O65944]”
SPX265626565317443132921741.90E-297[GI:4583524]133
[LN:AF140356]
[AC:AF140356]
[PN:VncS]
[GN:vncS]
[FN:putative histidine kinase/phosphatase]
[OR:Streptococcus pneumoniae]
SPX26572657531821965710891.00E-146[GI:4583523]123
[LN:AF140356]
[AC:AF140356]
[PN:VncR]
[GN:vncR]
[FN:putative response regulator]
[OR:Streptococcus pneumoniae]
SPX265826585319460138022730[GI:5712669]91
[LN:AF140784]
[AC:AF140784]
[PN:Vexp3]
[GN:vex3]
[OR:Streptococcus pneumoniae]
SPX26592659532021664810662.30E-141[GI:5712668]91
[LN:AF140784]
[AC:AF140784]
[PN:Vexp2]
[GN:vex2]
[OR:Streptococcus pneumoniae]
SPX266026605321426127820702.40E-280[GI:5712667]91
[LN:AF140784]
[AC:AF140784]
[PN:Vexp1]
[GN:vex1]
[OR:Streptococcus pneumoniae]
SPX26612661532285255NO-HIT6
|
Patent Application
20070009902
