SYSTEMS AND METHODS FOR EXTRACTING RARE EARTH ELEMENTS WITH ENGINEERED MICROORGANISMS

Information

  • Patent Application
  • 20240132993
  • Publication Number
    20240132993
  • Date Filed
    February 18, 2022
    2 years ago
  • Date Published
    April 25, 2024
    8 months ago
  • Inventors
    • BARSTOW; Buz (Ithaca, NY, US)
    • SCHMITZ; Alexa (Ithaca, NY, US)
    • PIAN; Brooke (Ithaca, NY, US)
    • MEDIN; Sean (Ithaca, NY, US)
  • Original Assignees
Abstract
Provided are modified bacteria for use in bioleaching rare earth elements (REEs). The modified bacteria contain at least one engineered genetic change that is correlated with improved bioleaching of the REEs, relative to REE bioleaching by unmodified bacteria of the same species as the modified bacteria. Also provided is a method for extracting REEs by contacting a composition containing REEs with biolixiviant produced by the modified bacteria. Kits that include containers that hold the modified bacteria are also provided.
Description
SEQUENCE LISTING

The instant application contains a Sequence Listing which has been submitted electronically in ASCII format and is hereby incorporated by reference in its entirety. Said ASCII copy, created on Feb. 17, 2022, is named 018617_01341_SL.txt and is 979,969 bytes in size.


BACKGROUND

Rare earth elements (REE) are essential for the manufacturing of modern electronics, sustainable energy technologies including electric motors and wind turbine generators; solid state lighting; battery anodes; high-temperature superconductors; and high-strength lightweight alloys. All of these applications place increasing demands on the global REE supply chain. As the world demand for sustainable energy grows, finding a reliable and sustainable source of REE is critical.


Current methods for refining REE often involve harsh chemicals, high temperatures, high pressures and generate a considerable amount of toxic waste. These processes give sustainable energy technologies reliant on REE a high environmental and carbon footprint. As a consequence, due to its high environmental standards, the United States has no capacity to produce purified REE.


There is growing interest in biological methods to supplement, if not completely replace traditional REE extraction and purification methods. Bioleaching is used to extract 5% of the world's gold, and ≈15% of the world's copper supply, and biomining in Chile alone accounts for 10% of the world's Cu supply.


The performance of REE-bioleaching lags behind thermochemical processes. For example, while thermochemical methods have 89-98% REE extraction efficiency from monazite ore, Aspergillus species can only achieve≈3-5%. The acid-producing microbe Gluconobacter oxydans B58 can recover≈50% of REE from FCC catalysts. However, techno-economic analysis indicates that even this extraction efficiency is still not high enough for commercial viability.


Recent efforts to improve bioleaching have focused exclusively on process optimization. It is believed that no previous genetic approaches have yet been taken for any bioleaching microbe. With recent advances in tools for reading and writing genomes, genetic engineering is an attractive solution for enhancing bioleaching. However, applying these tools to non-model microorganisms like G. oxydans can be a significant challenge. While there have been some advances for editing the genome of G. oxydans it has remained unknown where the genome can be edited to improve bioleaching results. Thus, there is an ongoing and unmet need for improved compositions, engineered organisms, and methods for separating REEs from compositions that contain them. The present disclosure is pertinent to this need.


BRIEF SUMMARY

The present disclosure provides a description of a whole genome knockout collection for Gluconobacter oxydans B58, and use of it to comprehensively characterize the genomics of rare earth elements (REEs) bioleaching. In total, 304 genes that notably alter production of G. oxydans' acidic bio-lixiviant, including 165 that make statistically significant changes, were identified. Based in part on this analysis, the present disclosure provides modified bacteria for use in bioleaching REEs. The modified bacteria comprise at least one engineered genetic change that is correlated with improved bioleaching of the REEs, relative to REE bioleaching by unmodified bacteria of the same species as the modified bacteria. The at least one genetic change results in decreased expression, or increased expression, of at least one gene. In non-limiting embodiments, at least one gene for which expression is modified encodes a protein that participates in phosphate-specific transport system signaling, or encodes a protein that participates in pyrroloquinoline quinone (PQQ) synthesis. In non-limiting examples, expression of a gene that encodes a protein that participates in the phosphate-specific transport system signaling is suppressed. In certain embodiments, the suppressed gene is pstS, pstB or pstC. In certain embodiments, a gene that encodes a protein that participates in the PQQ synthesis is increased. In non-limiting embodiments, the expression of at least one of the genes pqqA, pqqB, pqqC, pqqD, pqqE, tldD and tldE, is increased. In addition to these and other genetic modifications described herein, the modified bacteria exhibit increase expression of mgdh relative to expression of mgdh by unmodified bacteria. In certain embodiments, expression of pstS, pstB, pstC, or a combination thereof is reduced, or expression of pqqA, pqqB, pqqC, pqqD, pqqE, tldD, tldE, or a combination thereof is increased. In these contexts expression of mgdh may also be increased.


In another aspect, the disclosure provides for contacting a composition comprising the REEs with a composition produced by the described modified bacteria. The composition produced by the bacteria may be considered a lixiviant, or a biolixiviant because it is produced by the described bacteria. The disclosure provides separating REEs from the composition after contacting the composition with the biolixiviant. The separated REEs are suitable for use in a wide range of applications that will be apparent to those skilled in the art.


In another aspect, the disclosure provides kits that contain one or more sealable containers in which the described modified bacteria are held. The kits may further comprise printed material, such as instructions for use of the modified bacteria to form a biolixiviant, and/or to extract REEs from a composition where they are present.





BRIEF DESCRIPTION OF THE FIGURES


FIG. 1. Knockout Sudoku was used to curate a saturating coverage transposon insertion mutant collection for Gluconobacter oxydans B58. (A) The G. oxydans B58 genome contains 3,283 genes. 2,570 genes were fully annotated with a BLAST hit, Interpro ID, and gene ontology (GO) group. An additional 163 genes have an annotation and GO group, but lack an Interpro ID, 399 only retrieved a BLAST hit, but no GO group, and 150 were unable to be assigned any annotation. (B) A Monte Carlo (MC) estimate of the number of genes represented by at least one mutant as a function of the number of mutants collected demonstrated that picking 25,000 mutants would yield at least one disruption for 95% of genes, while picking 50,000 mutants would yield at least one disruption for 99% of genes. In total, we picked 49,256 single-gene disruption mutants and located at least one disruption for 2,733 genes. A Monte Carlo simulation of picking with random drawing from the sequenced progenitor collection (PC) without replacements demonstrates that the genome coverage was truly saturated. The center of each curve is the mean value of the unique gene disruption count from 1,000 simulations while the upper and lower part of each curve represent two standard deviations around this mean. (C) A Fisher's Exact Test for gene ontology enrichment among the non-disrupted (putatively essential) genes revealed significant enrichment (p<0.05, yellow line) of genes involved in translation and other ribosome-related functions. (D) The curated condensed collection (CC) contains 17,706 isolated colonies across 185 plates. High-throughput sequencing of the CC confirmed the location for 4,419 unique disruption strains, representing disruptions in 2,556 genes. 177 genes located in the PC were not located in the CC. No disruption mutant was detected in 550 genes.



FIG. 2. throughput pH screens of the G. oxydans whole genome knockout collection were used to identify genes that control REE bioleaching. (A) Thymol blue (TB) was used to measure the endpoint acidity of biolixiviant produced by each well of the condensed collection. The ratio of TB absorbance (A) at 435 and 545 nm is linearly related to pH between 2 and 3.4. CC plate 65 contains biolixiviant produced by δpstB strain in wells F7 and G7 (arrowhead), whose absorbance at 435 nm and 545 nm is shown, along with the average absorbance of all wells on the plate. The dashed line represents a typical absorbance spectrum for WT-produced biolixiviant. The A435/A545 ratio for these two wells compared with the average ratio of the plate is well below the lower bound (LB) for the plate, indicating that δpstB produces a much more acidic biolixiviant than the average strain. (B) Bromophenol blue (BPB) was used to measure rate of change in pH at the onset of glucose conversion to organic acids. Rate was measured over a six minute period within five minutes of adding bacteria to a glucose and BPB solution. Condensed collection (CC) plate 162 contains the δtldE strain in wells F11-C12 (arrowheads), whose changes in absorbance over time are graphed along with the average for that plate. A comparison of the normalized rate over OD for each well versus the plate average shows how V/OD for these wells was below the lower bound for CC plate 162. (C) All 185 plates of the CC were screened for acidification using the TB and BPB assays. Hits from both screens were verified in comparison with proxy WT strains. In total, 176 disruption strains were shown to significantly contribute to acidification by t-test with a Bonferroni-corrected alpha (ζ=0.05/#of comparisons). (D) The 25 largest reductions in biolixiviant pH, and 50 largest increases in biolixiviant pH. (E) All significant changes in acidification rate.



FIG. 3. Genes involved in phosphate signaling, carbohydrate metabolism and PQQ synthesis were significantly overrepresented in the significant hits from high-throughput screens of acidification by G. oxydans. Fisher's Exact Test was used to test for gene ontology enrichment (p<0.05, yellow dashed line). Numbers at base of bars are how many genes from the significant hits are from that gene ontology (GO), out of the total in the genome (in parentheses). Genes selected for further analysis of endpoint pH and bioleaching (FIG. 4) that contribute to an enriched GO are listed above the bars. (A and B) Enriched GO among genes that decrease and increase end point pH. (C and D) Enriched GO among genes that increase and decrease initial acidification rate. Abbreviations: FBP: fructose-bisphosphate; GDP-Man:DolP: dolichyl-phosphate beta-D-mannosyltransferase; GGT: glutathione hydrolase; G6P: glucose 6-phosphate; HTA: homoserine O-acetyltransferase; DD-transepeptidase: D-Ala-D-Ala carboxypeptidase; HAG: hydroxyacylglutathione; Membr: membraneMoco: Mo-molybdopterin cofactor; MS: monosaccharide; MT: mannosyltransferase; M6P: mannose-6-phosphate; Pi: inorganic phosphate; PLP: pyridoxal phosphate; PQQ: pyrroloquinoline quinone; PSK: phosphorelay sensor kinase; Q: queuosine; RNase H: DNA-RNA hybrid ribonuclease; SAM: S-adenosyl-L-methionine; TPP: thiamine pyrophosphate; TOP1: topoisomerase type 1; HK: histidine kinase; UDP-G: uracil-diphosphate glucose; 6-PGL: 6-phosphogluconolactonase.



FIG. 4. Increased acidification strains of G. oxydans B58 are able to increase rare earth extraction from retorted phosphor powder (RPP). (A and B) A subset of 20 disruption strains were tested for acidification with direct pH measurement. pH measurements significantly different from pWT (black circle) are labeled with asterisks: *, p<0.05; **, p<0.01; ***, p<0.001 (n=5, df=18). Error bars represent standard deviation. (C and D) Ten disruption strains with the lowest final biolixiviant pH and four with the highest were tested for RPP bioleaching capabilities. Outer gray bars represent total REE extracted. Inner multi-colored bars represent fractional contributions of each REE and are Y, La, Ce, Eu, GD, Tb from bottom to top in each bar. Error bars represent standard error for total REE extracted. Percentages are total REE extraction efficiency (based on previously published REE amounts in the RPP). (C) Using a two-tailed t-test between each mutant and pWT demonstrated eight strains were significantly better or worse at bioleaching total REE (+, p<0.05; n=5, df=18). With a Bonferonni correction, only one was significantly better (**, p<0.01/12), but two of the higher pH biolixiviants that extracted detectable REE were significantly attenuated in bioleaching capability (***, p<0.001/12). (D) Disruption mutants for mgdh and pqqC are only able to extract less than 1% of the REE that wild-type G. oxydans can, but still extract significantly more REE than glucose alone when measured at a lesser dilution (***, p<0.001/2). (E) Total REE extraction linearly correlates with pH. Error bars represent standard deviation for pH and standard error for total REE extracted.



FIG. 5. Clean insertion and deletion mutations targeting genes of interest confer improvements in REE extraction relative to unmodified (WT) bacteria. Biolixiviants produced using modified strains that have increased expression of mgdh driven by an introduced tufB promoter, or clean deletions of pstS or pstB improved REE extraction by 12% and 34% over wild type, respectively. Biolixiviant produced by a clean deletion of mgdh with almost no REE extraction capabilities is included as a control.





DETAILED DESCRIPTION

Unless defined otherwise herein, all technical and scientific terms used in this disclosure have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure pertains.


Every numerical range given throughout this specification includes its upper and lower values, as well as every narrower numerical range that falls within it, as if such narrower numerical ranges were all expressly written herein.


The disclosure includes all polynucleotide and amino acid sequences described herein. Each RNA sequence includes its DNA equivalent, and each DNA sequence includes its RNA equivalent. Complementary and anti-parallel polynucleotide sequences are included. Every DNA and RNA sequence encoding polypeptides disclosed herein is encompassed by this disclosure. Amino acids of all protein sequences and all polynucleotide sequences encoding them are also included, including but not limited to sequences included by way of sequence alignments. Sequences of from 80.00%-99.99% identical to any sequence (amino acids and nucleotide sequences) of this disclosure are included.


The disclosure includes all polynucleotide and all amino acid sequences that are identified herein by way of a database entry. Such sequences are incorporated herein as they exist in the database on the effective filing date of this application or patent.


The disclosure includes modified microorganisms having any modified single gene, and modifications of all combinations of genes described herein in the text, figures, figure legends, and tables of this disclosure.


Any gene and any combination of the genes that are described herein may be excluded from the claims of this disclosure. In embodiments, a modified microorganism of the disclosure may comprise or consist of only one modification of a single gene. In embodiments, a modified microorganism of the disclosure may comprise or consist of any combination of gene modifications described herein. In embodiments, only one or only a combination of genes that influence bioleaching of REEs are modified.


In non-limiting embodiments, the disclosure provides modified bacteria in which the expression of at least one of the genes pqqA, pqqB, pqqC, pqqD, pqqE, tldD and tldE, is increased. In certain embodiments, expression of pstS, pstB, pstC, or a combination thereof is reduced, or expression of pqqA, pqqB, pqqC, pqqD, pqqE, tldD, tldE, or a combination thereof is increased. In certain embodiments, the modified bacteria exhibit increased expression of mgdh relative to expression of mgdh by unmodified bacteria, wherein the increased expression of mgdh is in the context of at least one other described genetic modification.


In embodiments, the modified bacteria comprises or consist of mutations that are selected from mutations in all of the genes listed in Table A, and including all numbers and ranges of numbers of genes between 1 gene and the total genes in Table A.


The disclosure includes modifications that disrupt one or a combination of genes, modifications that increase expression of one or a combination of genes, or a combination of modifications that decrease expression of one or more genes and modifications that increase expression of one or more genes. Thus, the modifications involve altering the expression of one or more genes. Increasing, e.g., overexpressing a gene, can be achieved using various techniques that will be apparent to those skilled in the art when given the benefit of the present disclosure. In embodiments, increasing expression of a gene is achieved by substituting an endogenous promoter with a promoter that increases expression of the gene, relative to expression of the gene that is produced by the endogenous promoter. By “substituting” a promoter it is meant that the endogenous promoter (e.g., the promoter that is ordinarily operatively linked to the gene of interest without genetic engineering) has been changed so that is does not drive expression of the gene in the modified bacteria, and therefore the substituted promoter drives gene expression. By making this change, more mRNA is transcribed, thus facilitating production of more protein encoded by the pertinent gene that is operatively linked to the promoter. Substituting a promoter can include inserting a new promoter, while leaving the endogenous promoter in place, or inserting the new promoter in place of the endogenous promoter. The promoter that is inserted so that it is operably linked to and therefore drives expression of the described gene(s) can be heterologous to the bacteria, meaning it is taken or derived from a different organism, or it may be endogenous to the organism but has been introduced into a new location such that it can drive expression of the described gene(s). Various prokaryotic promoters that are suitable for this purpose are known in the art and include, for example, tufa and tufB. The substituted promoter (e.g., the promoter that is introduced into the bacteria) may be a constitutive or inducible promoter. The substituted promoter may be a core promoter, a proximal promoter, or a distal promoter.


Representative and non-limiting embodiments of promoters that can be used to increase expression of one or more genes as described herein include:

    • PtufB which has the sequence:











(SEQ ID NO: 1)



Ccgaaggcatcgtttacggtgctctcgaagtcatgcgccg







tcgcggcggcacgactgcagatccggtggccatgttccac







tcggctctggataacgtgaagcctgcggttgaagtccgct







cgcgtcgcgtcggtggcgcaacctatcaggttccggttga







agtccgcgccgagcgccgtcaggctctcgcgatccgctgg







ctgatcgatgcctcccgcaagcgtggcgagaacacgatgc







aggagcgtctgtccaacgaactgatggatgcggtcaacaa







ccgtggctccgctgtcaagaagcgcgaagacacgcaccgc







atggctgaagccaacaaggcattcagccactatcgctggt







aatcagaaccggttaaagggcttccggcagtgtgtcgatc







tcaggatcgtgcactgactggtttgaactttcagtcttac







tcccgttccaggtggagcggggttttggagaaagacg;








    • P112, which has the sequence:














(SEQ ID NO: 2)



Ggaactgactcctgatttcgttctgttttcatgggatcaa







tgaacggtcaggcgaaaatgttgcatcggggtgcaggaaa







tttcccgaaaaaaggaaaagacaggctggagcccgcggaa







atcaggcaaaaatcaggtgatatttttttcggattccgtt







tccggaggttcggtatttttcgtcgcaagctcggcgagct







gggctcgggcacgggaaacacgggccctcatcgttccggg







ggcacatcgcagacgcgggcggcatcttcataggacagtt







cctgtgctcccacgagaatcagggcctcccgcaacagatc







gggcagcttccacagcagttctcccaggtcctgaacggca







tcgcgggcattctggcgtgacggtgcagccgtggaaggct







gcatgtcctgctcgatgtcgagcatgatttcctgctcgcg







gctgcgacggcgcgtctgctcgtagaaggcatttctctgt







attgtgaacagccaggctttgaggaccgttccctgctgga







actg








    • P114, which has the sequence:














(SEQ ID NO: 3)



Gtggcagatgttgagaaatatccgcagttccttccctggt







gtgtgaaggcaagcatccggacccagacggaacaggagct







tgtggcggatctgacgatcgggttcggcccgttccgcgag







accttcaccagccgcgtgacgctggagcggccttcgcgta







tccgggtgcgctacgagaaagggcctttccgttacctgaa







taatgtctggacgttcacgccggatccgcggggctgtctg







gtcgatttcttcgtggatttcgagttccgttcgcgccttc







tgcagaatgcgatgggtgtcgtgttcaatgagggcgtgcg







cctgatggtctccgccttcatcaagcgggcacgggacatt







tacggcacgcaggcgacgaaagcggtccccccggcaccgg







gcctttcccaaaggacataaaatttcgtattatttccaca







accattcggtgcgtgggccgttacaggtctcaagcaccgt







catggtgacatgaaaaggattacgta






As an alternative or in addition to promoter modification, the disclosure includes addition of and/or repositioning of enhancer elements to increase expression of the described gene(s).


As an alternative or in addition to changing promoters, the disclosure includes increasing copy number of the gene that is to be overexpressed. In embodiments, one or more copies of the gene can be inserted into a bacterial chromosome, or can be introduced into bacteria using a plasmid. A list of genes for which overexpression is encompassed by the disclosure is provided on Table A. The additional copies of the gene may be in tandem, such as in a polycistronic configuration, or may be separated by segments of the bacterial chromosome or plasmid. In embodiments, a composition comprising the described bacteria are modified by transformation using one or more plasmids, which may be configured to be replicated and transferred to other bacteria in a bacterial population, such as by horizontal transfer.


In another embodiment, the disclosure comprises decreasing expression of genes. Decreasing expression can be achieved using any suitable approach. In embodiments, decreasing expression comprises disrupting the gene such that the protein encoded by the gene is not produced, or a protein produced by the gene does not function in the same way as if it had not been modified. In embodiments, a protein that is encoded by a modified gene of this disclosure is produced but does not function to impede bioleaching of REEs from a composition comprising them. In embodiments, a modification of a gene comprises a knock-out of some or all of the gene. Modifications of the genes can be achieved using any suitable genetic engineering techniques. In non-limiting embodiments, the modification comprises an insertion, a deletion, or a combination thereof. The disclosure includes insertion within, or a deletion of any segment of a gene, including but not limited to a insertion or deletion of a single nucleotide, such that the encoded protein is not produced or its function is eliminated or reduced. In embodiments, an insertion replaces some or all of the described gene(s). In a non-limiting embodiment, the described gene(s) is modified by insertion of a transposable element. In non-limiting embodiments, the genes are modified using compositions and methods described in U.S. Pat. No. 11,053,493, from which the entire description is incorporated herein by reference. In embodiments, a modification of a gene comprises an insertion as described in Anzai, Isao A., et al. “Rapid curation of gene disruption collections using Knockout Sudoku.” Nature Protocols 12.10: 2110-2137 (2017), from which the entire disclosure is incorporated herein by reference. In alternative approaches, site specific nuclease, such as Cas nucleases, can be used to modify any of the described genes. In embodiments, a type I, type II or type III CRISPR system can be used. Thus, in embodiments, a guide-RNA directed nuclease can make any of the described modifications. In embodiments, recombination of a chromosome or plasmid can be used, such as by introducing a recombination template comprising additional copies of a gene, and/or a promoter, to facilitate recombination of the recombination template into a desired location. In an embodiment, homologous recombination is used, and as such, the recombination template includes left and right homology arms to specify the location of recombination. In embodiments, a transposon system can be used to interrupt a gene sequence, such as the Sleeping Beauty transposon system.


In embodiments, the modified bacteria comprise a modification of at least one gene described in FIG. 1, FIG. 2, or FIG. 3. In embodiments, the modified bacteria comprise a modification of at least one gene as in Table A. Table A includes gene names and additional information regarding the type of analysis that were used in determining the effects of each gene in the assays that are further described below. In Table A, H=high acidity; L=low acidity; F=fast acidification; S=slow acidification. Table A includes the amino acid sequences of the proteins encoded by the listed genes. The disclosure includes all amino acid sequences that are 80-99% identical to the described amino acid sequences, and all polynucleotide sequences encoding said amino acid sequences. Polynucleotides that encode the described amino acids constitute the coding regions of the described genes.


In embodiments, the disclosure comprises increasing expression of at least one gene described in Table A. In embodiments, the disclosure comprises decreasing expression of at least one gene described in Table A. In embodiments, the disclosure comprises increasing expression of at least one gene and decreasing expression of at least one gene described in Table A. In non-limiting embodiments, modified bacteria of this disclosure are modified such that they exhibit decreased expression of at least one of the following genes: GO_1415, pstA, pstB, pstC, pstS, ggtl, surA, petP, ykoH, speC, and tonB. In non-limiting embodiments, modified bacteria of this disclosure are modified such that they exhibit increased expression of at least mgdh, and/or genes involved in PQQ synthesis (e.g., pqqA, pqqB, pqqC, pqqD, pqqE, and tldD, also referred to as pqqABCDE as an operon, and tldE), or a combination thereof. In embodiments, any one or any combination of proteins expressed by the pqqA, pqqB, pqqC, pqqD, pqqE, and tldD genes can be modified to increase their activity, such as by modifying amino acids in an active site, or amino acids that improve structural stability, and the like.


Combinations of modifications that increase and decrease expression of genes are included in the disclosure. The disclosure also includes mixed populations of bacteria, wherein some of the members of the population have different genetic modifications than other members of the population.
















TABLE A









BPB








TB
Acidifi-








Final
cation








pH
Rate








Screen
Screen
Up or

SEQ


Locus
Gene
Features
Pheno-
Pheno-
Down
Amino Acid
ID


Tag
Name
Disrupted
type
type
Regulate
Sequence
NO:






















GO_
ettA
Energy-
H
F
Both
MAAYQYVYVMKDLTKSYPGGREVFK
4


3277

dependent



GITLSFLPGVKIGVLGVNGAGKSTL





translational



LKIMAGIEKEYGGEAWAAEGARIGY





throttle



LEQEPKLDESLTVGENVAQGFGELK





proteinEttA



KAVDRFNEISMKFAEPMSDDEMTAL









LAEQADLQEKIDAGDGWELDRKLEI









ALDALRCPSADSPVTNLSGGEKRRV









ALCRLLLEKPDILLLDEPTNHLDAE









SVSWLEKTLRDYAGTVMVITHDRYF









LDNVTNWILEIERGRGYPFEGNYSS









WLTQKRKRLAQEEKEESSRQRALAA









EQEWISSSPKARQAKSKARITKYEE









MLAANAEKAGGTADIVITPGPRLGG









TVIEAENLTKGFGDRLLIDNLSFKL









PPGGIVGVIGPNGAGKSTLFKMITG









DDQPDSGSLKIGETVKLGYVDQSRN









TLDDSKTVWEEISGGTDVIQLGKRT









VPSRAYVGAFNFKGSDQQKRVGVLS









GGERNRVHLAKMLKQDSNVILLDEP









TNDLDVDTLRALEDALAEFAGCAVI









ITHDRWFLDRLATHILAFEGDSHVE









WFEGNFQDYEADKRRRLGPDATEPG









RIKYRPLAR






GO_
glpX
Fructose-1,6-
H
F
Both
MIDPQNVLPYRVTDRNLALELVRVT
5


1534

bisphosphatase,



EAAAIASAHWTGRGQKNEADGAAVQ





GlpX type



AMRAAFDTVAIDGVVTIGEGEMDEA





(EC 3.1.3.11)



PMLYIGEKVGSGGPAMDIAVDPLEG









TNLCAKSLPNALTVVALAERGKFLH









APDIYMEKIVVGPDLPEGVVDLDAS









IGNNLRSLAKAKKRDVSDMVLCALD









RERHEELIAHAREAGARVMLLSDGD









VAAAIATCVDGGGVDLYAGSGGAPE









GVLAAAAIRCMEGQMQGRLLFEDDT









QRERAREMANGLDPARKLFLHDMAS









GHVLFSATGVTSGPLLKGVERPSPS









RARTHSIVMRSKSGTVRYIESHHTF









KPKVKAAS






GO_
GO_
hypothetical
H
F
Both
MDLCWTTSCRSTTSRGRAATSACRD
6


289
0289
protein



YTASHHDHSPPTIGATLRNGALATP









RLCLGAGPLVLDSARLHLAKRLVAA









LVNSFV






GO_
GO_
D-alany1-
H
F
Both
MQVALEPETLPATIFRSEAVRQMRF
7


1067
1067
D-alanine



PFQKAFLLCAMTAMGLGSAKAQYAG





carboxypeptidase



HISSYVMDARTGAVLSATDAELQRY





(EC 3.4.16.4)



PASLTKLMTLYLTFRALEAHQITLD









EQVPVSIHASIQAPSKLGLVPGTRL









TVEQGILGLVTKSANDAACALGEFL









GGGDEVRFAQLMTQQARALGMTNTT









FRNASGLPDPDQVTTAHDLALLSQH









LISDFPQYYHYFNVPSFYFHRRMVP









NHDPMLKIYAGADGLKTGYTDLAGH









NLITSAQRGNVRLIGVVMGAPNNTR









RSMEMVSLLDKGFADEGVAPQPLLH









PVAPSGVLMASARRRGHFRHSVLLA









SSRPMEVADAPTSPRRYGRISHHGA









AVRMVSARHVVAHKKRSRHS






GO_
GO_
ABC-type
H
F
Both
MICRFSPKVTLSLLSACLLT
8


1076
1076
transport



GPVAMTALSSVALAQTAGAV





system involved in



SPADAASAVTPISALYDALK





resistance



AAQKTGKTAQQRATMIAPAV





to organic



DRAFDLEAILRRSVGVRYNS





solvents,



LSPSDRTRLLGSFRQFTIAR





auxiliary



YASSFKPEAPAAFTVSPQTR





component



PNPTGGLIVDTTIGGTDGGD









VTPIDYIMTNGTSGWRITDV









LLNAHISQVAAQRADFGGAL









SSGGASGLADHLDSKTAHFL









HD“






GO_
GO_
Sphingosine
H
F
Both
MRIALIHNARSRKNRRNGSS
01


1658
1658
kinase



FAVEAQALLGKDFVPSDTRE





and enzymes



GTTEHVRQLYERGIDTILID





related to



GGDGTVSTALTAIARAYPAD





eukaryotic



RLPDIVVLASGNTNLIAGDV





diacylglycerol



GFGLRGMEAIQRLRQGDLRS





kinase



SVRTPIRLSWPGTDRMPVLG









LFGGCAGYARAVRIAHSPTV









LRFAPHDLAVGITLLSTFVS









LMFRKSREEWLRGDPLRIET









GGHVYDGQSFMFLTTGLSHL









SRGIWPFWDAEPNVEGLRYL









DVSAWPDSLLRATAALLCGR









APRWLRRHPDYVSGRTDDMT









LVTESDFVLDGEVFSAAPGG









VLRLERASRFRFLHA






GO_
GO_
Putative
H
F
Both
MAGGLLVGMGILAAGTTLAA
10


1865
1865
membrane-



ARHIGDGSLAFSLLRAGSRA





spanning



GVVGGLADWFAVTALFRHPL





protein



GLPIPHTAILPRQKERLGQA









LGRFISGQFFTEDDVRRALS









KIDLSGLIADMLNDPANRQT









LVTSMRSAIPLMFDRMEDGR









AKTAISRALPVLLNGEEMAP









LVSRGMRAMVDSEMHQEVLS









FLLERIKTTVTSRESDLRHF









VEERVREQGGRFLGWAIGGS









VASRVLMALHAEFERVDPMD









SELRHGFTTWVRGEIDRIEN









DPARRKDMADTITSVLTHTS









LKGWSSELWDRLRRMVEEDS









GREDGWSATVIDAAIVQLAS









ALRSNESLRLKVNQAVESTV









QRILPGLREKLSGFIAAVMA









GWDGNDLAARLESRVGRDLA









YIRINGTVVGFLAGAALDGV









SRLFFGV






GO_
GO_
ATP-dependent
H
F
Both
MYAVKESLESHLSAKTTSGP
11


1873
1873
RNA



SKPRTTATPRRGRPSASRTA





helicase



AAATSPTVADKGETSPVTET





Atu1833



PASKAPRTRRTKTAATATEK









TAEVKTPARRTRKAATPAAE









SATESEAPAPKTTGRRKKAV









TEPEAVTELAEAAVAAPAPR









RRRSTKAPEAVTEEAEAAPK









RRGRPRKTPVVEQPAAEVIT









EETVKAPAAPRRRGRPRKVD









VAVAETPVEAPVEKKARQSR









RKASAPVMEAPEPAAEETPA









VQTESTKGEKPARRRRTKAA









AATSAVVEKTVEAPAVVETI









VVAEDVSDRPRFADLGLGEP









IMRAIEELGYEHPTPIQAQA









IPEVLKGHDVLGVAQTGTGK









TASFTLPMLQKLAGSRARAR









MPRSLILEPTRELALQVAEN









FKLYGKYLRLTHALLIGGES









MAEQRDVLNRGVDVLIATPG









RLLDLFGRGGLLLTQTSTLV









IDEADRMLDMGFIPDIEKIV









ALLPAHRQTLFFSATMAPEI









RRLADAFLRHPVEITVSRQS









SVATTIEEALVIVPEDEKRR









TLKKLLRRENVQSAIVFCNR









KRDVDMIQQYLTKHGIEAGH









LHGDLAQSLRFSTLERFRSG









DLKFLVCSDVAARGIDIGGL









SHVFNYDLPFNAEDYVHRIG









RTGRAGNEGHAFSLATPRDR









RLLEAIETLTGKVIARPVLE









GITTVDWAPEDGERRPAETA









TPAPQDVAEEGEQRLRKRRR









GGRKRNRGDRDENETVQEVA









PTAVASVAVIEAPVSHRSVE









LAPAFENDGPKTGFGGDTPA









FMLVPRRRKVTVSGSTDPAA









PVQHDGRHYGNE






GO_
yqg
Putative
H
F
Both
MPLFNPHDLRNLLQSGQRVL
12


2019

pre-16S



GLDPGSKTIGVALTDVSLML





rRNA



ASPLIGLKRRKLGENAQELA





nuclease Yqg



KIVRAQDVGALVVGLPLSLD









GSFGPAARAASDWTQALSEK









LGIPAGLWDERLSSSAVNRF









LIKDADMTRGRRAEVVDKMA









AAYMLQGWLDASRPESPEIF






GO_
GO_
Phosphogluconate
H
F
Both
MSLNSVVESVTARIIERSKI
13


210
210
dehydratase (EC



SRRRYLALMERNRAKGVLRP





4.2.1.12)



KLACGNLAHAIAASSPDKPD









LMRPTGTNIGVITTYNDMLS









AHQPYGRYPEQIKLFAREVG









ATAQVAGGAPAMCDGVTQGQ









EGMELSLFSRDVIAMSTAVG









LSHGMFEGVALLGICDKIVP









GLLMGALRFGHLPAMLIPAG









PMPSGLPNKEKQRIRQLYVQ









GKVGQDELMEAENASYHSPG









TCTFYGTANTNQMMVEIMGL









MMPDSAFINPNTKLRQAMTR









SGIHRLAEIGLNGEDVRPLA









HCVDEKAIVNAAVGLLATGG









STNHSIHLPAIARAAGILID









WEDISRLSSAVPLITRVYPS









GSEDVNAFNRVGGMPTVIAE









LTRAGMLHKDILTVSRGGFA









DYARRASLEGDELVYSHAKP









STDTDILRDVAAPFRPDGGM









RLMTGNLGRAIYKSSAIAAE









HLTVEAPARVFQDQHDVITA









YQNGELERDVVVVVRFQGPE









ANGMPELHKLTPTLGVLQDR









GFKVALLTDGRMSGASGKVP









AAIHVGPEAQVGGPIARVRD









GDMIRVCAVTGQIEVLVDAA









EWESRRPVPPPLPALGTGRE









LFALMRSVHDPAEAGGSAML









AQMDRVIEAVGDDIH






GO_
GO_
Phytoene
H
F
Both
MVFSRMRASSGLPCAQADLD
14


2105
2105
synthase



HVERIVTASGTSFARGMSIL





(EC 2.5.1.32)



PPDRRQAMFAVYAFCRQVDD









IADGDAGVADPMAALQEWHR









RIDQLYEGVATDALDRILIV









AIHRYQLQAKDFHDVIDGMA









MDCGAPIVAPDEATLDLYCD









RVASAVGRLSVCVFGDSSDN









ARRVAYHLGRALQLTNILRD









IAEDAGRGRLYLPAELLTRF









DVPKDPQEALYAHGLDQVAR









ILAERAKDHFREARNAMRLC









DSTAMRPARMMAASYAPILS









ALEKRGWKTPDIAPKVCKPW









RQLRTLAAYVK






GO_
GO_
Adenosyl
H
F
Both
MGSKGHFMTTQDYKVRDITL
15


2223
2223
homocysteinase



ADWGRKEISIAEGEMPGLMA





(EC 3.3.1.1)



LREEYKDSQPLKGARIAGCL









HMTIQTAVLIETLIALGATV









RWSSCNIFSTQDHAAAAIAA









AGIPVFAWKGLTEEEFNWCI









EQTIHGPDGWTPNMILDDGG









DLTIMMHDKYPEMLKDVRGI









SEETTTGVHRLWEMSKKGTL









KVPAINVNDSVTKSKFDNLY









GCRESLVDAIRRGTDVMMAG









KVAVVAGYGDVGKGSAASLR









NAGCRVLVTEVDPICALQAA









MEGYEVVTMENAAPRGDIFV









TCTGNVDIITIDHMREMKDR









AIVCNIGHFDSEIQVEALRN









YRWNNIKPQVDEIELAPNRR









IILLSEGRLVNLGNATGHPS









FVMSASFTNQTLAQIELWTA









KPGQYEVKVYTLPKALDEKV









AALHLAKVGAELSKMSQKQA









DYIDVPVNGPFKHEEYRY






GO_
GO_
Riboflavin
H
F
Both
MFSGIIERLGTVRSACVRDR
16


2309
2309
synthase



AMDLTVETGFPDLELGESVA





eubacterial/



VNGVCLTVETFDAAGVATFH





eukaryotic



LSGETLSRTPLDQLKTGSRV





(EC 2.5.1.9)\



NLERAVAASTRLSGHIVQGH





Diamino



VDGVATLASVEKAGDSYALR





hydroxyphosphoribosyl



VFVPQALRQYVVEKGSITFD





aminopyrimidine



GISLTVNELHDDITRGNQAG





deaminase (EC



FEVGLTIIPHTWEHTNLSTL





3.5.4.26)



SVGDRMDVEVDVLSKYVENL









LRFSPSLGKVAS






GO_
GO_
hypothetical
H
F
Both
MRRCVAAIRKAALFGLVFAG
17


2456
2456
protein



IAGAGSASAAEAAWTASKCG









AEPQAPAVKAATVAQYNESV









DRVTAYEKAARVYNACVSAQ









ANREETAISQEASARISHVH









AGSAAVQSHIAASFQTLSSN









LAAASRKLGHH






GO_
GO_
TonB-dependent
H
F
Both
MRSRYCLCATTALALSVSAA
18


2571
2571
receptor



FAQSDVAPKSRSHRPTQTHK









SAATKEDSPSMMGSTSPTDE









ARSETVRVQGSRRSSPGAGL









MVHEDAAKSRSTVTQEFISK









QTPGVNPMQLIAMLPGVNTT









SVDPLGLNGGNMTMRGLNAS









QIGFTLEGFPINDIGNYAVY









PQEIVDSENLRSITVEQGSA









DLDSPHISASGGAVNMYLLD









PKDHFGGHLDGTYGSYNSRR









IFGRMDTGKIGNTNLKGYVS









FSAAHEDSWRGPGSQRKLHG









ETKWVNEWGQGNRISLAIVG









NQSNSTLFPSMSLANWNKYG









VNYTYTGKWNPSSPSTNYYK









LHQNPFTNIYASAPSTFTLT









DHLTLTETPYFWYGNGNGGG









AYNESLSSQQYGAQTLSASI









GQYNSSNTKSLLVYNPSNTQ









TYRPGAVTKLALHTGANRLM









IGYWFEYSKQIQTSPYSLVN









MATGTPLDVYGGGTNMVLSN









GVTAEYRDTLTQTRIHTLFI









DDSLSLLNNHLTLEAGLKYA









MVARQGHNFLPDTSTGPYIN









GSWNEPLPAASIRYKLNNEI









QLFASGTTNFRIPMNTALYD









SGTYTSGSGYSTKANTNMKP









EISISEEAGIRYQGALFNGT









LSYFHYNFTNRLYSETVVQS









NGAYYSTSVNGGSSHADGVD









FEIGTRPILYHLRPYISAEY









IDARTDSNVAAGGSTNDYVH









SKGKFAPQTAKVQVAFNLDY









DDGAFFSGFGLKYVGKQYAT









FNNDTSIPGYVTMDVHAGYR









FRNYGVLKNPVLKLNIQNIT









NNHYLGFVNGTASNGKATTG









VFGSAIAAGSTTYYVASPFF









VGGSASVDF






GO_
GO_
hypothetical
H
F
Both
MKKCHNPARLRGICRLAQDD
19


2699
2699
protein



RSQYIGIMRLLPTLPRLLLV









AALAMTPTILVPWHHAQAQD









ADDAEAEQEAEAAQKKAEAR









KAAQRAAPPSALPGAEASDD









DAGHARSDVNPTTALFDAIN









RGSLNAAKEALNRGADMGGH









NVLDQTPLDMAIDLNRKDIM









FLLLSMRTYNPDGKIENSVS









DEGVEMKNGSGHLTIGGKSV









TPKRSLVAASPHFDTSGGKP









DPSVGFLGFAGH






GO_
GO_
ROK family
H
F
Both
MADYRLGIDLGGTKIEIAVL
20


2761
2761
sugar



NRSGDLVLRERIPNPGIYNE





kinase or



AVLAIRDLVTDVDRRLGAVP





transcriptional



SHRVSAGQHTSTLGIGIPGS





regulator



ISPETGLIKNANATWLNNQP









FGQDLESALARPVRTENDAN









CAADGAAKGMLTVFGVIIGT









GMGAAIVNNGRVLEGRHHIA









GEWGHLPLPWPTEEDMPARD









CFCGNKGCMERYLCGPALAA









DWKGPGHRNTAGIEDAAANG









DQAAIAALGRYTERFARACA









MVINFLDPDVIVLGGGVSNL









HTLYERVPPLLAKHVITPVC









TTPIVRNKHGDSSGVRGAAW









LWDVTE






GO_
GO_
hypothetical
H
F
Both
MQKIFSLSEIGASDVSHDLV
21


2829
2829
protein



SFDIFDTLVYRRYLEVNEVH









DLASAYALSLLGQFGKENPG









ALTLTRYDITNVMKAAAHER









IEEPTLEAVWSRLFTARIGH









TEKALTLGRKVAAFEYEIDR









QNLYAVEGAAEMLAALKAQG









KTVIAISDMYFSQTEIEGIL









LQTGLARHIDRVFVSSQENL









TKHSGNLFTHVWKQFDIAPA









KTLHLGDNTHSDVAMPTSLG









GNAIHVAHAPLLRIKRPDYG









RRPDIHMEIGDLSKLFLTQL









LLCAQSDGSDRLFFLSRDGC









LLHKVLEKWNSPLFRNFFTP









IHSEDLFLSRAVTCWLNVNF









QDKWLLQSIGHAFWLHHGKA









TPRQISGMLGIDATPAGLDA









DKVYHSSMDTFTVLEAYEAS









GL VEEIRTALLHKRAMAAS









YLKDAGVLNHQSVHVCDVGY









SGTVVRDLNTFFLQEGPQGL









GGSIPQVYFHCIASNANYSG









NARTALPHVIFQKDVILNDG









LLPGELKDSFAWLEMFFKHP









LYGPLLGYRKDGDRTVPSYD









VAAQEDPHHPCHLILNTIKS









DPSDIVLLWMSAVGFWSQFT









SPLIERFLNPDESTIEQMLS









DVYEVDAVSGKTRSVVLVAP









ELSDDEIRHRAQREDYWIPG









SLVASRLARTRSAFETDAEQ









KSLVNKLRALANGGTAGKGS









KQAEKNQDAFDPAFYRRFYR









DLSALPNDRALEDHYFTHGK









LVGRYGSEAMMKREQAALEQ









RLPRDFDAGAYFMANPDLPV









TQPVSWTATRHYLNIGAVQN









RPYHYHFPGLDEAFEALLAT









NEISLSDAERKDYQDGVPAR









ILLLRRLGAISAPWFNMLDL









QEFSALNFEWCGKPASAAEA









ILTFLKDGIERIAPLSVSVA









FDPDFYRRQYTDTADLSDVD









AYRHWLEAGSLMHRAPSEEW









ALQHMIGQRTYPPAFHWDRF









QATDRARFARSTRLDLLDAF









LSTAVPPRDDLVGGPGAGD









LWTWRAARAQGAGDQHLSTE









CLREAARVEPHRGVFWHTLG









DRLQSQGDLHGALEAYTRCL









KTDTPNRWSHINCIRLSADL









GFYKKGLEHLRAAQAAWKEM









QPWREARTHLFMRWFDHAAH









HSYDRITQDDIRARTHPDAR









FLAFMNTFVPAVASIGIPAP









LTLARTDGPILILSGSGLSE









RTRWEASLRIAPEDARQVIV









FSREQVALFAESLPGASVAL









YHEVETDGLIVDTLLRAKAL









GVRNIYWAGPLGRDSTGEGP









DLSDLAWSDFLLSRDSRETG









RTLRSIHAATMCDDVVLTMP









SLITRFHDLGLRPRLGVSAL









MEALADMPRTTETAPGKIRI









FCSLTGRPVRVSTSDEDAYA









PRIGQKALLKALDTLLETYP









DVSLLVEGVDPALPLSIRNS









TRIERLGSELTSDQRLAALS









RSSIALDLRHVPRDQRSLAD









EATWSGIPCLVLSDNPALGS









ASTPGYAKWAQISEILKAWI









GQPQTLEDVTLAARTHFEEA









VSPTPVVWSPVRAVPTTKAR









PRILFANLFAPPQTTGGATR









VLSDNAGYMLAHAGDDYDFA









ILASDDENSHRGVTRVDSWK









GAPVFRIATPQEIDMDWRTY









NSEVDAQTRRIITLFKPDLV






GO_
GO_
Acetylornithine
H
F
Both
MIPALMPNYKRADLAFEQGE
22


2902
2902
aminotransferase



GVWLTATNGRRYLDFGAGIA





(EC



VTSLGHAHPKLVKTIAEQAA





2.6.1.11)



KVMHVSNLYRIPQAEKLAEL









LVQNTFADSVLFCNSGAEAN









EGMVKMIRRAQFENGHPERT









NILCFNGAFHGRTLAMISAT









GNPAYLKGFGPVVEGFDHAP









FNNTNTLRDAITPHTAGIVV









EPVQGESGIKPATREFMEGL









RAVCDEYGLYLGFDEVQTGV









GRTGKLFAHEWYGVRPDVIS









VAKGIGGGFPLGAVLATEEL









ARHLTPGSHGTTFGGNPLAC









AAGVTVLEEILSPGFLEHVR









SVGDAFGRMLEDVVSRSEGV









FDNVRGIGLMRGLHCVPPVA









DVMQAVLNQELLTVSAGDNV









LRLVPPLIVTETECREACER









LVKAADSLKVPATQENAS






GO_
GO_
Transcriptional
H
F
Both
MSQETNAPELHQLTAQIVTA
23


3260
3260
regulator



YVSNNDIPADALPALIRSVH









DSLATVNVPEEAPVEKPVPA









VSPRKSVFPDYIICLEDGKK









LKLLRRHLKTAYNMTPQEYR









ERWGLPPEYPMVAPNYANHR









SSLARKIGLGRRRED






GO_
GO_
UDP-glucose 4-
H
F
Both
MRYLVTGGAGFVGSHVVLAL
24


36
36
epimerase (EC



RDAGHDVVVLDNLSTGYREA





5.1.3.2)



VPAGVPFHKVDLLDYAATSA









VVAQGNWDGVLHFAALSLVG









DSMRDPFHYLRQNYLTALNL









VQICAGHGVRKIVFSSTAAL









FGGPERLDPIPETAPVQPGS









PYGESKFMIERVLHWADAIY









GLRSACLRYFNAAGADPQGR









AGEDHRPETHLIPLTIDAAL









GRRPALKLFGTDYPTRDGSC









VRDYIHVTDLADAHIRALAQ









IDQRSVTYNIGNGHGYSNLE









IIQSVERVSGRKVPWEPAPR









REGDPALLVADSTTLRNDTE









WAPRFGDIDSIVETALRWRE









SHPHGYGG






GO_
GO_
hypothetical
H
F
Both
MSPENDQDRNRPDPGDYARA
25


406
406
protein



PKQPAGPASGARPQARFDRE









RLSNDYDDEPPPRRRPAAAG









GASGAGRLTSVLGNDPATRK









LVGGAVGIGVVLLLAVGGWS









LMGSHHGGIPIIGPPPGPVK









DRPADPGGMQIMGGDDGDTD









MTGNGEAHLAPGPEQPDTKA









LARQYGVPPGTPAPETPKAD









APKADGAAPDNAPAAQTPAI









PPEAAAPADTGQMSPGTALP









ATVPEKPQDQAAAPAEAPKA









APPKEAPKKEEAPVHHAARP









AEKPLPAPVPEPENVGPPKA









AAPAAETSGGTHEVQLGALD









SEAAARKEWDSLRHQAPALF









AGHTPLFEKTIRGDHTFVRL









RIGGFADLKSARAYCVKLHA









QSVACTPAQF






GO_
GO_
Transcriptional
H
F
Both
MKKAVTLNSVAVEAGVSRAT
26


868
868
regulator, LacI



ASLVLRDSPLVSLETRDRVI





family



GAMDKLGYIYNRGAANLRGQ









KTGTIGLVLCDIGSPFYSQL









MLGVDEVIVDANIVAILVNS









AENPDRQLRQIRRLREHGVD









GLILCPAAGSSDALLSEIER









LHLPCVQVLRHVSQRNGNYV









GPDYADGTSLAVTHLVRHGR









RKIAFLGGKPVHSAARERLD









GFRKTLKKYKLEHDLIIPTQ









LENLSDLGSFPELLASSTPP









DAVVCYNDMLAQSVMGYLLA









RGKMPGRDFAVIGADDLPQS









AVSFPTLTTIVTDPVGVGRN









AARLLLDRIDNPATSSTRIL









VSGQLMIRQSCGGQLS






GO_
hemK
Peptide chain
H
F
Both
MMMAKDDLLREASQALEQAG
27


1937

release



IEDARREARLLLCWATGRDL





factor N(5)-



GGLLSLDGVEPAQKSRFAEA





glutaminemethyl



LKRRLEREPLAFITGETGFW





transferase (EC



TLDLETGRDTLIPRADSEAL





2.1.1.297)



IEALLDVCPDRNAPLSILDL









GTGTGCLLLAALSEYPQATG









VGVDLSPQAVALAQRNSVRT









GLEKRTAFLAGSWADALNAR









FDVVLSNPPYIETGDLAGLM









PEVLQYEPARALDGGTGGLD









AYRILCAALPALLVPGGYAI









LEMGIGQIDAVSALGVASGL









RDVAHKADLGGIERALVLQS









DG






GO_
ntrX
Nitrogen
H
F
Both
MEHEILIVDDEPDIRFLIEG
28


174

regulation



ILNDEGYKTRTAANSDQALE





protein NtrX



LFRAHCPSLAILDIWLQGSR









LDGIELLKIFQTEEPGLPTL









MISGHGTIETAVSSLKLGAY









DFIEKPFQSDRLLVVVRRAL









EAARLRRENAELRLRAGPET









TLSGDGAVISAVRAQIERVA









PTNSRVLISGPAGSGKEVAA









RMIHARSRRAEGPFIALNCA









TLAPNRFEEELFGLEGEDGQ









PMRRGVLERAHRGTLLLDEV









ADMPPETQGKIVRALQDQTF









ERLGGNTRVKVDIRVIATTN









RDLQSEIAAHRFREDLYYRL









AVVPLRIPSLRERREDIPGL









ARHFLERCAQSSGLPVRELS









VDALAALQSYEWPGNVRELR









NLMERLLIMMPGTGNDPIRA









DMLPATISQGAPSMTRLNSG









ADVMSLPLREARDLFETQYL









QVQLMRFGGNISRTASFVCM









ERSALHRKLKQLGVTTNEER









NTAPSTPVSG






GO_
paaD
PaaD-like
H
F
Both
MSEAMTDITPSEDTATAPAP
29


1871

protein



GTAPDQEAVIAAIATVYDPE





(DUF59)



IPVNIYELGLIYAIDLHDDG





involved in



RVHIEMTLTAPNCPSAQELP





Fe-Scluster



EMVRDAVSHVPGVSQATVEI





assembly



VWDPPWDMSRMSDDARLALN









MF






GO_
tps1
Trehalose-6-
H
F
Both
MIQVPFPPSRAALLLDFDGT
30


2181

phosphate



LVDIAPTPESVRVPQGLAAD





phosphatase (EC



LLRLRDMLDGALAIITGRPI





3.1.3.12)



AQIDHFLPDIPHAVAGEHGV









MMRHAPGQALRERKLPVVPG









EWIQAVEKAAADHPGASVEH









KKAGMVLHYRRAPEAESVFR









ELASVWPVENRGFHLQDAQM









AIELRPLGIDKGKALRELMA









EPPFAGRLPVFAGDDATDRD









GVRAARQMGGAGWLIPDDFP









DAATFRRWLHDLSEGHGWGA






GO_
mur
Manganese
H
F
Both
MVADTKIAERRAGPGNRKAP
31


3261

uptake



SSPVPDDSHIARLCVESGLK





regulation



MTGQRRVIAHVLSVADDHPD





protein



VEELYRRASEIDSRISVATV





MUR



YRTVRLLEEKGILERRDFGG









GRARYEASDSGNHYHLIDVD









SGRVIEFEDEEPVRLLAQLA









QRLGFDLVSHRIELFGRRAE









PDDRKKSPSENRNKSGS






GO_
GO_
Shikimate 5-
H
F
Both
MIDGHTKLAGVMGWPVEHSR
32


2463
2463
dehydrogenase I



SPLMHNHWCRVNGVNGAYVP





alpha (EC 1.1.1.25)



LPTRPEGFDQALRGLAAAGF









QGVNVTIPHKEAAMLACDEL









TPTAKRAGAVNTICFVAGRI









IGDCTDGTGFCDNLSAHDVE









ISGRAMVLGAGGAARAVAAA









LLDRGCEVVIANRTLERAEA









LVEALGGGEAVAWYEWPSLL









SGCSLLVNATSMGMGGKAGL









DWDAVLREAAPGLCVTDIVY









TPRETPLLLAAQARGLRTVD









GLGMLVHQARAGFRAWFGVD









PQADQTTFDLLAASLRTDA






GO_
cyoA
Cytochrome O
H
S
Up
MMKAGPMKKLWRYLPALPAL
33


2506

ubiquinol



MLSGCTVDLLQPRGPVAEMN





oxidase



RDVMVAEFVIMMLVVVPTCA





subunit II



ATLYFAWKYRASNKEAEYLP





(EC 1.10.3.—)



TWDHSTAIEYVIWGVPAILI









ALLGAISWWSTHAYDPYRPL









QTADNVKPLNVQVVSLDWKW









LFIYPDLGIATINQLDVPTN









TPLNFQITSDTVMTSFFIPR









LGSMIYSMPGEQTQLHLLAS









ESGDYLGEASQFSGRGFSDM









KFRTLAMDPAQFNDWVEKVK









SGSENLDDTTYPKYAAPQEA









APVQYFAHVQPDLFDGIVAK









YNNGMMVDKKTGKVMHMQSA









SNTAPSDTGMKE






GO_
cyoD
Cytochrome O
H
S
Up
MTQAPTTTMTGDSHGSYPSY
34


2503

ubiquinol



LIGFVLAVILTVASFAAVMS





oxidase



HALSPGMALAALTVLAVVQI





subunit IV



VVHLVFFLHMNTSTEQSWNL





(EC 1.10.3.—)



MCFIFAAASVIVIIGGTIFI









MHDTAINMMSR






GO_
lam
Lysine 2,3-
H
S
Up
MDDMVKTAPRHSTKRHTLRT
35


2812

aminomutase



PSDLIDAGLAPEADRATLEA





(EC



VGERFTMAIPPAFQDLITHP





5.4.3.2)



DDPIARQVIPDARELITLPH









EDADPIGDDALSPVPGIVHR









YADRALLKPLLVCPLYCRFC









FRREHVGPGGGLLSDAQLEA









ALDWVRQHPDIREIILTGGD









PLMLAPRRLKHIVQSLSDIP









HIETIRIHSRVPVADPGRMT









EELLDAMETDRSMWLVVHAN









HANELTPQAIKGIRAVLSRA









IPVLSQSVLLRGVNDTVESL









EALLRAFLKARVKPYYLHHL









DAAAGTGHFHVPVAEGQALL









RQLRGRVTGLAWPTYVLDIP









GGRGKVPIGPEYLDPASPGT









VSTPDGEACSFT






GO_
GO_
NADH
H
S
Up
MASRSEILIVGGGVAGLSLA
36


923
0923
dehydrogenase



TRLGKSMGKSGKARITLIDK





(EC



SFSHVWKPMLHCFASGTLSN





1.6.99.3)



ENDKVNFISQASGHHFEFWP









GEVASIDRENREVVLSPLLE









ADGTVILESRRMKYDTIVIA









IGSCANDFGTPGVKEHCMSI









DNLVEANAFNEKFRMELLRA









FGNNSELDIAIVGGGATGVQ









LAAELHKALEIVGPYNLHAF









GKAPPKLHVTLLQSGARILP









AFPESVSAAAQQELEHIGVT









VRTNARVAAADDHGFTLKDG









SYVPAKLRVWAAGVKAPEVT









TAYGGLTINRTGQILVNPNL









SSIDDEHIFALGDCSFIQDD









PLPATAQVARQQAKHLARYL









PAWIEHGQKVPSCIFHNKGA









IVALGKYNGWAALPGGTVWG









GGISHGFSARMAHLMLYRQH









QIELFGYYRGLMSFYSDWVE









TFVRPSVRLD






GO_
GO_
hypothetical
H
S
Up
MSGCSDPEGIFAPDSAAVRA
37


1060
1060
protein



FRARLDSQPSATAALQARCS









TPIRVIRLSVDRPVTEDILT









LLQVRETHQVMTRHVRLLCG









ETVLSDAWNWYVPERLSPAM









NTLLEQTDTPFGRVVRQTAF









RRQRLETRFPGRASGIVLEN









RALLLRGADNAPISLVVEDY









LPAAIRP






GO_
GO_
FIG00687856:
H
S
Up
MPDVLEQRLIGELTTPVDPG
38


1659
1659
Predicted



VVAFADALARACPVLPLGVL





nucleotidyl



FYGSLLRKADPDGILDFYII





transferases



TENAAGFAGGLVARTGNLVL









PPNVRYSEFRHGGRVLRAKI









AVLSRAQFEARTGLGALDTT









IWARFCQPVRLVWVRDPQSA









DVILSLIAGCVTTATCWAAL









LGDVSMTALEFWQTLFAHTY









ASELRVEKKGRGNSILEGQE









ARYAALLTLGWARGRLQFSA









HGDRLEPVIDAALRRKAARR









WALIQISGRPRNVSRLLKAA









FTFENGASYLAWKIQRHTGF









DMQLSPFESRHPLVMLPRLL









WRARGLLARSKA






GO_
GO_
AMP-binding
H
S
Up
MSGNPNGASPGLTEANQNPT
39


1662
1662
enzyme,



ANPVPTPSRSGLERRYGDFP





associated



SFAAALDYAAQGESGFNIYS





with



GRGQLLEALPYRLLREQARS





serinepalmitoyl



MACRLLGLGLVPGDRVAIVA





transferase



ESDGDFARIFFGCQYAGLVP









APLPLPVAFGGREGYVTTLR









GMIQSAAARAVVVPDVIGSW









TADIVDGLDLVFGGSPADLY









RHAEARVELPEISPTALSYL









QFSSGSTRFPMGVSVTQAAG









MANARAIARDGLHVYPAEDP









RDDRCVSWLPLYHDMGLVGF









FLTPLTCQLSVDLLPTREFA









RRPHVWLDLISRNRGTIAYS









PSFGYELCARRSGQADLDLS









CWRIAGIGGDMIRHHILEGF









AERFASNGFRATSFVASYGM









AEATLAISFAPLDTGIQTDT









IDLRRLEKDGIAEPSNDPSH









PLRTFVLCGEALPDHQIEVR









DAAGHDLADRQVGTVYVRGP









SLMCGYFRRPDETEAVLDAD









GWLNTGDLGYHLNGQIVVTG









RAKDLIIINGRNIWPQDLEW









SAESEVPSLRSRDVAVFSVD









GDEGEKIVALVQCRATEDES









RNQLRDEVTSLFRRQHGVDV









DVILVPPRTLPQTSSGKLTR









AKAKTMLLSGQFEQQPETTS









SVA






GO_
GO_
hypothetical
H
S
Up
MKVAFPLIGQRHQTLHALPI
40


1663
1663
protein



ALEVSARHPDVAVHVSCLTV









SHLELARSLATLYPEARVQF









DLLPISPKLRRRIELHGLRV









VDRLIGLFASRHYFRTFDAI









IVPEATSLQLRRMGVGRPKM









IWTGHGAGDRAIGFARHLGK









FDFLLVPGRKVEQRMLEKSI









IRPGAYHRGTYAKFDLVRRM









DAKRPKLFNNNRPTILYNPH









FLRRLSSWPEMGHQVLQFFA









TQDRYNLVFAPHFRLFDNHR









EEGEALRRQYGHLPHMLIDP









GSHRSIDMTYTMGADLYLGD









VSSQVAEFMIRPRPCLFLNA









HHVKWHGNPDYQFWTLGPVT









ENVSDLGSKIENAFETHPRF









LEAQRQYVLETFETLGDEPT









APAAADAIVDFLKRAA






GO_
GO_
Mannose-1-
H
S
Up
MSQKIVPVILSGGSGSRLWP
41


182
182
phosphate



VSRSSYPKQFWPLLSKYSLI





guanylyltransferase



QETALRGARAGLADPIVICN





(EC 2.7.7.13)/



AEHRFIVAEQLRDVGVENAR





Mannose-6-



IVLEPVGRNSAPAIAAAAFL





phosphate isomerase



VAETDPDAVLWIMAADAAIT





(EC 5.3.1.8)



DEAALYSALDHAVAAAGQGR









IVTFGMKPTRVETGYGYIES









GAPLSGLEGVCEVSRFVEKP









DAATAEAFFRDGRYLWNSGM









FVTQAGVFLSEIQTFEPALY









EHVGQAVRTRQSDLDFDRLD









DASFRQAPDISVDYAVAERT









KRAAVVPGTFGWSDIGSWDA









LWELTSKDEAGNATFGDVFL









DDARNCYVRSDGIVATVAGV









EDLIVVVTQDAVMVSHRDRA









QDVKHMVSRLKKAGRKEATA









HNRMYRPWGFYESLIQADRF









QVKRIVVEPGQKLSLQKHFH









RAEHWVVVGGTAVVTRDADQ









IMVRENESVYLPLGCVHRLE









NPGRIPLTLIEVQSGPYLGE









DDIVRIEDVYSRN






GO_
GO_
Sensory
H
S
Up
MTVTRSGSPDLNPRRWRRLW
42


1993
1993
transduction



YRRDALRSIRMFDTVGARVM





histidine kinase



TLIVATTLPLAIIASLLAWH









SYQQNVGNSAMRTERDTQLA









ISEITTDLDQTHTLLDMLAD









GDISSGNALREFALVQTVSQ









HHYCMLMLTDVSGRPSVVLP









PPSTQDAAICSSPELAAPAT









NSPTARTPVVGVDVLKGDRG









PLLKFVVPILSNNSVSGYII









AVRTLGWQRSHLPKGDSRLL









LGTDNNSRHFLAMPDGTLYS









LFPDRPVTAELPARAFARLK









RDISSLSLHDVFTSQGITYA









FQNAYGPVSLIVATERTAEE









SHALNIFLIRVSLIVGLLVL









ELMAVALGARLFLVDPLEKL









ALAVADWRKGAAFAPRISHS









IPLEIRHLERAFLRATRRLS









KHEQDLEQSARNQDMLIREI









HHRVKNNLQVVASLLNLQAS









RIRSHEAREEFRLVRDRVRA









LATLHRYLYSESGLSALDVQ









SFLEELCSILLSANGMNAQT









RIRLQLDIEHVLISPDQAVP









IALIVTEVVSNALRYAFPEN









RAGHIVINLHKVVSTDAEKE









GLVELKLGDDGIGINAGQAT









ESRTRREGIGMQLIRGFARQ









INADMTVSNENGTWYTLRFI









PERPSLTALAMARKAISYGE









DSGL






GO_
GO_
Dolichol-
H
S
Up
MAVLNEAENILPVCQELADT
43


2191
2191
phosphate



FGADPSAEILAIDDGSTDAT





mannosyltransferase



VKKLLEARQTLLPRLRIISH









PKRLGKSAALRTGITAAKGQ









WIATIDGDGQDDPSAILKML









DQATSASGAAPLVVGVRRKR









NDRLSRRIATRFANGLRRRL









LNDGCPDTGAPLKLFPRDLF









LKIPQFEGVHRFLPALLGHY









GAPLICIEVQHRARLHGSSK









YTNFNRALVGIRDLLGVMWL









QNRTHLPDHLTEH






GO_
GO_
Diaminopimelate
H
S
Up
MSAPLPSDPATDPSFSDMLE
44


2479
2479
decarboxylase



TRPSLKMDARDGLMFEGVPL





(EC



HVIAAAVGTPCWITGAETLR





4.1.1.20)



RRAKALRTAFEARNLPVNMH









FAMKSQDHQATLTILRQCGY









GVDIVSGGEMQRALHAGIQP









SGIVFSGVGKSDAELRAAVE









HDIAQVNVESVEELYRLDDI









ARACGRVARAALRVNPDVDA









DTHDKISTGRAGDKFGIEHR









RAVALYGEAASLKNVRLVGL









AVHLGSQMLTATPFREGYAR









LADMVREIRAAGHTVESVDC









GGGLGIRYRDEIAPSPDMLA









GVIAETLGDLDVRLSIEPGR









WLSAPTGILLTRVIETKAGN









PDFVVIDAAMNDLARPSLYE









SWHGIMPVAPSGLTSPTKLW









DIVGPVCESSDIFARDRALP









AETKRGDLIALLDTGAYGSV









MSSTYNTRPLAAQVLIDNGK









WEIIRQRQSVAELIAAETVP









EWLTAKDDHG






GO_
GO_
Mitochondrial
H
S
Up
MPDTIEVTRLDNGLTIITER
45


2557
2557
processing



MDRVETVSFGAYVSIGTRDE





peptidase-



TADNNGVSHFLEHMAFKGTE





like protein



RRSASRIAEEIENVGGYINA





(EC 3.4.24.64)



YTARETTAYYVKLLKNDLAL









GVDIIGDILTHSTFLDAEIE









RERGVILQEIGQANDTPDDI









IFDQFQERAFPEQPMGRPTL









GSEERVSTMTRDTLMSYMRE









HYTTHNITIAAAGNLHHQQV









VDLVKEHFRDLPTHQTPRPR









AASYEGGELRTPRELDQAHL









VMGFPSVSYMHPDHYAVMIL









STLLGGGMSSRLFQEIRERR









GLVYSVYSFASPFSDSGLFG









LYAGTGEEQTAELVPVMIDE









LKRLQDGLSAEELSRARAQL









KSSLLMSLESTGSRCEQLAR









QIQVHNRPVPTAETVGKIDA









VTEDDILRVARTIFSGTPTF









TAIGPIDNMPSLEDITARLA









A






GO_
GO_
NifU protein
H
S
Up
MSGRLERKDMTTMFIETEDT
46


3255
3255




PNPATLKFLPGRSVTGDARP









VDFGDADVAAGRSELATALF









DQPNVRRVFLGGDFVSVTKS









DDISWGDLKPVVLGTITTFF









ESGRPVLSGTQAAPEHDVSP









EDAEVVSRIQDLLDTRVRPA









VAGDGGDIAFRGYKDGVVYL









AMQGACSGCPSSRATLKHGV









ENMLRHYVPEVASVEQVED






GO_
kdtA
3-deoxy-D-manno-
H
S
Up
MTLFPRLLRLWLGTCLRTTR
47


2438

octulosonic acid



WQVSGSPRALETLTTPAQGT





transferase



VVAFWHRSLTLSPALWFWAR





(EC 2.4.99.12)(EC



TLEPRLELRVLISRNPDGML





2.4.99.13)



IADVVRPWGIIGIHGSSSKK









GKNKGGAAVLRTALKELEAG









SIVAITPDGPRGPAELVQPG









AVALSRLARCAVVPVGMAST









SLRLPSWDGLVFPLPFGRGA









LIMGEPLFQPDAALLQNALN









DVSLRAESVVRHRQSNLADR









LWRVAGTLMAPALTVMLRIR









LHRGRELPGRLRERMGLERT









GPRRGHRPPGQLLWIHAASV









GETLCALPLAEALLEALPEM









RILFTTATVTGSEIVARHPL









YGQRIIHRFIPHDVPRWLRR









FLNLWQPEGAIFVESELWPG









IIAACSRRDIPVMLVNGRLS









DRSARLWTRLGDPARRMMKR









LSWVAARGPEDAARFRALGA









LPVYEDGDLKQDAPPLAYDE









TEYARLESLIGERPVFVAAS









THPGEEELVLQAAERARRLQ









PDLLTIIVPRHPARGAELAA









RFDLPRRAAGQDPTPQTQIW









LADTLGELGLLYRLADRCFL









GNSLAGKGGGHNPFEPLRLG









IPTATGPKMENWREAIATVS









DTIHIVNDVECLTRWLESPL









PPVRTTGLQRSVVSVLRDRI









LKTVER






GO_
kup
Kup system
H
S
Up
MPEHDGDHASNPPHGVGIPN
48


1459

potassium



DSGEIVQTIEQARSEGHTHE





uptake



IGGEEDGSSHHRPAGMGALL





protein



AVLGVVYGDIGTSPLYALQS









SVSIVSSPKAPAQPWEIMGL









ASLTFWALMLIVTIKYVILI









MRADHDGEGGIIALMSLAQR









VCKSQHFRWLFGLVGIAGTC









LFFGDSIITPAISVLSAVEG









IETSVPSASHIIIPLAMVVL









VALFSVQVLGTGKIGKAFGP









IMVCWFSVLAILGIKGIFLY









PHILLALSPTFALEFIIMHG









YLSFIALGSVVLSVTGAEAL









YADMGHFGRAPIRKAWLFFV









LPSLTLNYFGQAALLIRDPH









ALSNPFYLLVPHWAQIPMLI









LATFATVIASQAGISGSFSL









CRQLIQLGYLPRTRIMHTNA









SEEAQIYLPSLNWILAFGAL









VLVLAFRSSSALAAAYGIAV









TGTFLCTCVLAMVVFRRVFK









WKSATVGIVFGFFFIVDSIF









FSANVLKIPDGGWVPLAIGI









ISTIIMTTWKRGRSLIAARQ









QADSMPMGSFLARLPQSRTI









RVPGLAVFLTANPDIVPNSL









LHNLKHNKVLHDHILFVTVE









NLDKPEAERGHRAIVQELAP









NIHRVIVRYGFMEMPNLPRA









LLELNALGVAFDAIQASYFT









SHELVVRSRVPKMQLWRMWI









FLLLLRNAASTTEFLRIPPD









RVVEFGVRIAI






GO_
mgdH
Glucose
H
S
Up
MSTTSRPGLWALITAAAFAL
49


2781

dehydrogenase,



CGAILTVGGAWVAAIGGPLY





PQQ-



YVILGLALLATAFLSFRRNP





dependent



AALYLFAVVVFGTVIWELTV





(EC 1.1.5.2)



VGLDIWALIPRSDIVIILGI









WLLLPFVSRQIGGTRTTVLP









LAGAVGVAVLALFASLFTDP









HDISGELPTQIANASPADPD









NVPASEWHAYGRTQAGDRWS









PLNQINASNVSNLKVAWHIH









TKDMMNSNDPGEATNEATPI









EFNNTLYMCSLHQKLFAVDG









ATGNVKWVYDPKLQINPGFQ









HLTCRGVSFHETPANATDSD









GNPAPTDCAKRIILPVNDGR









LVEVDADTGKACSGFGTNGE









IDLRVPNQPYTTPGQYEPTS









PPVITDKLIIANSAITDNGS









VKQASGATQAFDVYTGKRVW









VFDASNPDPNQLPDDSHPVF









HPNSPNSWIVSSYDRNLNLV









YIPMGVGTPDQWGGDRTKDS









ERFAPGIVALNADTGKLAWF









YQTVHHDLWDMDVPSQPSLV









DVTQKDGTLVPAIYAPTKTG









DIFVLDRRTGKEIVPAPETP









VPQGAAPGDHTSPTQPMSQL









TLRPKNPLNDSDIWGGTIFD









QMFCSIYFHTLRYEGPFTPP









SLKGSLIFPGDLGMFEWGGL









AVDPQRQVAFANPISLPFVS









QLVPRGPGNPLWPEKDAKGT









GGETGLQHNYGIPYAVNLHP









FLDPVLLPLGIKMPCRTPPW









GYVAGIDLKTNKVVWQHRNG









TLRDSMYGSSLPIPLPPIKI









GVPSLGGPLSTAGNLGFLTA









SMDYYIRAYNLTTGKVLWQD









RLPAGAQATPITYAINGKQY









IVTYAGGHNSFPTRMGDDII









AYALPDQK






GO_
mreC
Rod shape-
H
S
Up
MLSIHARQVLAKAVLPILIL
50


388

determining



LAVGLVLLGLVRRPAVDGVR





protein



LMATDFMAPAYHGLVWPQER





MreC



VKVWLTDLRGATDLAKENAR









LRDENRALRHWYDVAVALAA









ENGRLKKSLHWIPETVPQYV









TGRVTRDDGGPYSRAVLLDV









GSGHDVRIGDVALDAAGLLG









RVTEVGPHTVRVLMINDDAS









RIPVTLGSSHGDAIMAGDDT









ASPRLIFYPQDHHPVEGERV









ETRGQSTMPAGLPVGTVHYS









APNRPVVVPDADLDRLDIVR









VFDYGDDDSQAPDAPGRVRV









KKLPQNPLTGPLPFSWLPNL









PDMPGRGGQ






GO_
mreD
Rod shape-
H
S
Up
MVAENSTPHLHSAVEPKQTF
51


389

determining



RRALDMAARAAMPSLFIVFS





protein



AILLSAPFGIPGQAQLQFGI





MreD



AMCTVWFWAYSRPRSMPALA









VFLCGLVVEIFSFGPPGTVL









LSLLVIYGVAHHWRYGLSRL









GFIAGWLIFSVFAALASFFQ









WALVCLHAVALLSPAPGLFQ









AALTIGIYPSLTALFVWGRR









TFANPDQA






GO_
pqqC
Coenzyme PQQ
H
S
Up
MTLLTPDQLEAQLRQIGAER
52


2303

synthesis



YHNRHPFHRKLHDGKLDKAQ





protein C



VQAWALNRYYYQARIPAKDA









TLLARLPTAELRREWRRRIE









DHDGTEPGTGGVARWLMLTD









GLGLDRDYVESLEGLLPATR









FSVDAYVNFVRDQSILAAIA









SSLTELFSPTIISERVSGML









RHYDFVSEKTLAYFTPRLTQ









APRDSDFALAYVRENARTPE









QQKEVLGALEFKCSVLWTML









DALDYAYVEGHIPPGAFVP






GO_
pqqE
Coenzyme PQQ
H
S
Up
MTLPSPPMSLLAELTHRCPL
53


2305

synthesis



SCPYCSNPLELERKAAELDT





protein E



ATWTAVLEQAAELGVLQVHF









SGGEPMARPDLVELVSVAQK









LNLYSNLITSGVLLDEPKLE









ALDRAGLDHIQLSFQDVTEA









GAERIGGLKGAQARKIAAAR









LIRASGIPMTLNFVVHRENV









ARIPEMFALARELGAGRVEI









AHTQYYGWGLKNRDALLPSR









DQLEESTRAVEAERAKGGLS









IDYVTPDYHADRPKPCMGGW









GQRFVNVTPSGRVLPCHAAE









IIPDVAFPNVKDVTLSEIWN









LSPLFNMFRGTDWMPEPCRS









CERKERDWGGCRCQALALTG









NAANTDPVCSLSPFHNLVEK









AATGVPEKPELLYRRF






GO_
tldD
TldD protein,
H
S
Up
MSVAADALGGLATTDALFFG
54


2196

part of



RSDSKLTRDDARALVNRGLD





TldE/TldD



GVDDGELFLEYRENESISLD





proteolyticcomplex



DGTIRSASFNTSSGFGLRAV









LGTETAFAHADDISRDALER









AVSTVGAVRQGRSGIMAPGP









QATNQRLYGDSRPLEGTDFA









ARAAVLSEIDAYARGLDSRV









VQVSAVLSSEWQAVQIMRRA









DSGGDVADLRPLVRMNVSVV









VEKDGQRESGSCGLGGRYEL









DRLLAPETWRDAVDKALKQA









LITLEATPAPAGEMDVVLGP









GWPGILLHEAVGHGLEGDFN









RKGTSSFSGMIGKRVASPGV









TVVDDGTLPERRGSLSVDDE









GTPTSRTVLIEDGILTGYLQ









DRLNARLMGTKSTGNGRRES









YAHAPMPRMTNTLMLEGSAT









TDEMIRSMKRGLYAVNFGGG









QVDITSGKFVFAASEAYLVE









EGKIVRPVKGATLIGNGADA









MNQISMIGSDVALDPGIGTC









GKAGQGVPVGVGQPTLKISG









LTVGGTA






GO_
tldE
TldE protein,
H
S
Up
MTTTPVEALLAAARRHGADH
55


2558

part of



ADAILVRDESESALVRKGVP





TldE/TldD



EGIERSESVALGLRVFRGKR





proteolyticcomplex



AATVSTSVLNEAEFDRLAEQ









ACAMALVVPEDQYAGLAEAA









LQGRFDAVGLDLECSSAPSM









DDLLARAREAEDTALSFEGI









TNTNGASAGHGRTSVALGTS









AGFFGAYSRTGHSTSASVLA









GEGATMQRDYAYRSAVHLED









LESPAVIGREAAERVLARIN









PGRPRTGTYSVIYDPRVSST









LLGHLVGAINGAAIARGTSF









LKDSLGKQILSAGLTVHDDP









RRIRGAASRPFDAEGCAALP









LDLIADGVLQTWLLDSRSGR









QLNMPTNGRASRGVASPPSP









SVTNLHLAPGTLSSVALRSD









ISEGILITELMGSSVNMLTG









DYSRGASGFMIRNGEIAEPV









AELTVAGNLKDMFARMIPGS









DLMFRQSVNAPSIRIDGMNI









AGL






GO_
GO_
Tryptophan
H
S
Up
MTNTPSPLSSPLANSLRSGP
56


2863
2863
synthase



DDRGRFGIFGGRFVAETLMP





beta chain



LLLELDEAYRAAQADPEFRR





(EC



ELDYYLKDYVGRPSPLWFAQ





4.2.1.20)



HLTEELGGAKVYFKREELNH









TGSHKLNNVMGQILVARRMG









KTRIVAETGAGQHGVATATV









CALFGLKCTIYMGATDVERQ









KPNVFRMHLLGAEVKPVTAG









AGTLKDAMNEAMRDWVANVA









DTYFLVGTVAGPHPYPEMVR









DFQSVIGVEVKEQITQAEGR









LPDVIVAAIGGGSNAMGIFH









PFLDDASVRLIGVEAAGHGL









DSGKTAASISRGRPGVLHGN









RTYLLQDKHGQIEEAHSISA









GLDYPGIGPEHSWLNDIGRA









EYVGVTDEEALEAFQVCTRT









EGIIPALECAHGLAHVMKIA









PAMAKDQIIVLNVSGRGDKD









IFTVAHHLGVKL






GO_
atu4171
ATP-dependent
H

Up
MPFPDTHPALKRALEARGYE
57


673

RNA



QLTPVQEAVLQPGLDERDLL





helicase



VSAQTGSGKTVAFGLAIAPT





Atu4171



LLGDADRLPPSPQPMALVIA









PTRELALQVQSELKWLYAET









GARIASCIGGTDARSEAREL









NRGVHIVVGTPGRLCDHLSR









GSLDLSALRCVILDEADEML









DMGFRDELEKLLDAAPTERR









TLLFSATIAREIASLARRYQ









KNAERIDTVSGAKQHSDITY









RCVITQPQEIERSLVNVLRF









YESPTAMVFCNTRMMVNQVQ









ATLLERGFASVAISGEMGQN









ERSRAIESLRSGQARVCVAT









DVAARGIDVPALNLVIHASI









PTAAETLLHRSGRTGRAGRK









GTSVLMVPLNQRRRAERLLQ









MAKIQAEWEAVPTADAIAEQ









DKTRLMHDPILTNAVDDMSD









ELVNQLVETYDATKLAAALV









GLYRARLPKVEQIRPMSVEA









PRRTERGERAPREEHTMSGE









WFKMGVGRTERADPKWLIPL









ICRLGGVQKREIGSIRIDQE









QTYFQIADESVARFKSCLAG









AEADEVTIEPSEAPAGGMGP









RGRNPGEGKRFGGGGRSGGG









FKGGPRGGAGGGYKGRGGSG









YGRPKPAAGDGPRGDGSSRK









RRS






GO_
ccmA
ABC transporter
H

Up
MTSPSDFPPPPVPGRLLDVE
58


1481

involved in



DVTVFRGDRLVLDGLSLTLD





cytochrome



AGDAMILTGPNGAGKSTLLR





cbiogenesis,



TISGLRRPDSGEVIRYGDLA





ATPase



WLGHQDALKPGLTLAQNLAL





component CcmA



AEKLGTNSLPDALEALDLTH









LTDLPARLLSSGQKRRAAFA









RVMLSGAPLWLLDEPTVGLD









VASIERLGAVMAAHRAKGGA









MIVTTHVPLPLDNTRSHELP









SLAHVESFWLS






GO_
clpX
ATP-dependent Clp
H

Up
MSNKSGDSKNTLYCSFCGKS
59


1879

protease ATP-



QHEVRKLIAGPTVFICDECV





binding subunit



ELCMDIIREEHKTHLVKSRD





ClpX



GVPTPKEICKVLDDYVIGQF









EAKRALSVAVHNHYKRLAHA









AKSSDIEIAKSNILLIGPTG









SGKTLLAQTLARILDVPFTM









ADATTLTEAGYVGEDVENII









LKLLQSADYNVDRAQRGIVY









IDEIDKISRKSDNPSITRDV









SGEGVQQALLKLMEGTVASV









PPQGGRKHPQQEFLQVDTTN









MLFICGGAFAGLDKIISARG









KGSGIGFGADVRSDDERRLG









AILQSVEPEDLLKFGLIPEF









IGRLPVIAALNDLDESALIQ









ILSKPKNALIKQYGRLFEME









GVKLTFTEDALAAIAKRAIE









RKTGARGLRSILENILLGTM









FDLPGLEGVEEVVINREVAE









SKAQPVYVYGKGKSEPAEQS









A






GO_
cysG
Precorrin-2 oxidase
H

Up
MNTQPHHSSPDSPQDGGWFP
60


1671

(EC 1.3.1.76)



ISIRLSGARVLLVGGGEIAV





Sirohydrochlorin



NKGRLLLDHGAWIDVLAEKL





ferrochelatase



HPVVQGWVESGRVCHVGERA





activity of CysG



DDEVLRRLLPGCRLVYAATD





(EC 4.99.1.4)/



SRDTNRQVAALADELNIPVC





Uroporphyrinogen-III



AVDDPGPSSFITPAQVRRGM





methyltransferase



VRVAVSTEGAAPVLARRLRE





(EC 2.1.1.107)



QIETLLPEGTGRLAAYMQSR









RVLVSGRYPNVQDRKRIWED









FLDGPAAEAARSGDESRADA









RLEALLNGDRKPGEVWLVGA









GPGDPDLLTLKALHLMQNAD









SVLYDNLVSPALLDMVRRDA









ELVFVGKQRDRHALPQDEIN









REMVRRAQAGERVLRLKGGD









PFIFGRGGEEIEALVAAGVA









FRLVPGISAANGCAAYSGIP









LTHRDCAQACLFVTGHAKAD









GVLDLPWDDMADRRQTVVIY









MGISTLPQLAAGLLGKGLPA









DWPVAIVERGTQPGQRVFTG









TLATIAQQAAEAQVKSPALV









IVGQVVRHRVVSP






GO_
DbsA
Periplasmicthiol:
H

Up
MTRLSLSRRFFVSAAPALAV
61


1605

disulfide



AGTAAGTARAAGTGSTDARL





interchange



SPRIIGNPNAKVLVQEWFSL





protein



TCTHCAHFATEEFPKIKEQL





DsbA



IDTGKIRYQFHDFCGDRVGL









TAAMVARSLPEERYVPFLEA









LFSSQMQWAFAAGGDPMQRL









QQMSALAGVSAAQFDAISKD









NVFAEALFDQVKKDSDTYNI









QGTPYFRFNNTHYDQDPETY









EKFADLVAKAS






GO_
dusB
RNA-
H

Up
MTASAPSAAPDAPAAAPPNR
62


171

dihydrouridine



VLKPIDLGQGVVIEDPVILA





synthase



PLSGVTDLPFRQLARDLGAG





DusB



LVVSEMIASWAMIRENENTM









RMARMAERGPNAVQLAGCDP









EAMAQAAKISVDGGANLIDI









NFGCPVKKVAIGQMAGSALM









RDEVLAGKLLEATARAVNVP









VTLKMRMGWDHNSLNAPRLA









KIAEESGIRLVTVHGRTRQM









FYNGTADWRFVKTVKDAVSL









PVIVNGDINTIRDAREALHQ









SQADGVMIGRGCYGRPWFTA









QVAQSLRTGEDVLDPDLATE









KEIALRHYRMMLDHFGERPG









LRLARKHVSWYSAGLPGSAT









FRSTINGVESAAEAIALLTA









FYDRHIEAGVVRNREAGPTG









SLSRDGTREAA






GO_
envC
Murein hydrolase
H

Up
MKAPDPRPFLPLVLLLSPGW
63


2710

activator EnvC



AAAHHASHHHARHTEKPAVA









AASEGQKALARAQAARRTLE









KRQADEAAVLKAKQIASAQA









EAKARQDNARTLAFTAQTHT









AQSAVDTTQSRILALKASIA









ELMDKRTAVEADIRQQNAAL









QPLLPVAARLSIAPDAALLA









SPETASESVTALSVLGGFSR









LTQQRAQALQSREDELHAIG









IDLDSRQKELAELLAQQTRE









RNAAAARTRIAARQEAVADQ









GAQKARKAVADAMQAAADLS









AEIDALVRQEAQARAELEKE









AAALTRQHQLERARHARSQA









QALSSSGQGVSSGSGHAPVS









GRVAVRWGQTTEAGPATGIT









YAALSSTPVQAPCTGRVEFA









GPFRSFGQMLILDCGRNYRF









VLSGLGQLNVSGGQSIRKAA









TLGQMPAADGMLFVQLRHGT









QVVSPAPFL






GO_
ftsE
Cell-division-
H

Up
MIRLLNVSMMPPGVGQPVLR
64


2773

associated, ABC-



NLTLTVAQGEFRWLLGPSGA





transporter-



GKSSLLRLLTLETRPSAGQM





like



DLLGMSVSQASRATLRNLRR





signaling



RIGFVPQDYRLIGEWTVFDN





protein



VALPLRLRGASERDTRREAF





FtsE



AVLEWLDVAHLADKRPGTLS









GGEQQRAAIARALIGRPEIL









LADEPTNALEDAQARRLLAT









FQELVDMGTTVIVATHNEAL









VREAPAASIVLQDGTLADAD









TQDGIAARRSDRA







GO_
3-phosphoshikimate
H

Up
MQVSRPLTVSASPKGLSGRT
65



1058GO_
1-



RVPGDKSISHRSLMFAALAS




1058
carboxyvinyl



GRTYVTGLLEGEDVLRTADA





transferase



MRALGATITREGADWVIEGR





(EC 2.5.1.19)



GVGALTEPADVLDMGNSGTA









ARLLSGILSSHGFNSIMTGD









ASLRSRPMRRVTVPLAANGS









EFLTREGGRLPMAVRGTGEA









KPIEYRLPVASAQVKSAILL









AGLNAHGTTVVEEPVATRDH









TENMLRHFGVEVDVSRIDAG









GRRIALTGPVRMTARDVTVP









GDPSSAAFPIVAALLVPGSD









IWIEGVGLNPLRTGLFTTLI









EMGASLSIENERVEGGEPVG









DLHVRYSQLKGVDVPPERAP









SMIDEYPVLAVACAFAEGPS









RLRGLEELRVKESDRLASTV









ALLNVNGAETEVIGDDLIVK









GHHGPLGGGTVQTHMDHRLA









MSAVVLGLAAQKPVNVDDTA









FIETSFPGFVDLMNALGAGL









TP






GO_
GO_
Fructokinase (EC
H

Up
MSAPQHDLLCIGNAIVDVLA
66


1072
1072
2.7.1.4)



PVGQDLIDGLGAAAGSMTLI









DAPTAHAIESRVDIENVTGG









GSGANTAVVAARMGAKVAYL









GKVTADEAGDHFTRDIREQG









ITFPSEPLPAADGTPTARCI









VLVTPEGQRTMFTYLGACTE









FTPEDVHESVVADAAITYLE









GYLYDKPHAQEAFEHAARLA









RKAGRQVALTLSDTFCVERH









RAAFHELVAGHVDILFANEA









ELLALYEVTDFEEAITQVST









ETKLAVITRGEKGAVVIGDG









ERHDVPTTEVKVVDTTGAGD









AFAAGFLAGLSKKHDLVTCA









KLGNQAAGEIITRYGARPTE









TFTLTA






GO_
GO_
Fe-S oxidoreductase
H

Up
MMRTLFLQPPSFDGFDGGAG
67


1074
1074




SRYQAKREIKSFWYPTWLAQ









PAALVPGSRLIDAPPAKMGM









DPILEDVKNRDLVVMHTSTP









SFASDVRVAQMLKDANPRLM









IGMVGAKVAVQPMESMEKGG









PIDFVARNEFDFTIKEIAEG









KPLAEVDGITWRNEKGEIIA









NKDRAMIEDMDSLPFVTEVY









KRDLNINDYFIGYLKHPYIS









IYTGRGCKSRCTFCLWPQTV









GGHRYRTRSPEHVAAEVRLA









KQYFPEVQEFMFDDDTFTDD









LPRAEAIAREMGKLGVTWSC









NAKANVPYETLKVLKENGLR









LLLVGYESGNQQILHNIKKG









MRVETAKEFTRNCHKLGIKI









HGTFIVGLPGETKETIQETI









EFAKEINPHTLQVSLAAPYP









GTFLHKQATENGWLNEAEAE









LIDESGVQIAPLHYPHLSHT









EIFESVEEFYRKFYFRGSKI









ASIVNEMVRSPQMMKRRLRE









GVEFFQFLKDRHAA






GO_
GO_
Ceramide
H

Up
MPLPLTIAAGFCALVSAAGN
68


1075
1075
glucosyltransferase



LQALAGATLLARFRRTERKA





(EC 2.4.1.80)



DDALRLSDRIWPSVTVLKPL









HGNEPLLEDALESVFTQDYP









DFQIVFGVQDREDTALAVIE









RLRARHPRIPVSVVIDPQEH









GPNRKVGNLMNMYGEVRHDI









IVISDSDIHASPNYLRHVVT









SLEEQGTGLVTTLYAGRPAA









GTLVQQLGACQINHNFLPGV









MMSRFLGRQDCLGATMALRR









QTLEEIGGLEALVDHVADDA









ELGQLIRVRGENITIAPTLT









HTTVGEHSISDLLAHELRWG









RTVKNVAPVGYGLSAIQLPL









FWAVTAVLFRPNAWWTWFML









LLTWLVRAIGSRIMDRATEC









PLPAAIPLLVVRDWLSAAIM









VGSARGSRVAWRGRTVHIAR









RKRNSASCAPSLQAGATHRS









VRS






GO_
GO_
hypothetical
H

Up
MDGPWLSSLSRLRKVGKHEG
69


1077
1077
protein



PSSIRLTAYRPIVVFASMSG









CIIRIRAVANRAQMDLWMPE









LVTGNLIQCVMNLISTHGTV









YRTKARS






GO_
GO_
NADPH-
H

Up
MPDHQPTGPSAPGTDALSQL
70


1097
1097
dependent 7-



GRATTTPQSPEEAVLERVPS





cyano-7-



PHQGRQYVVRFTAPEFTSLC





deazaguanine



PVTGQPDFAHIVIDYIPGEW





reductase



IVESKSLKLFLTSFRNHGAF





(EC 1.7.1.13)



HEDCSIAIAERLVALLDPQW









LRIGAYWYPRGGIPIDVFWQ









TGEPPKGVWIPAQDVPGYRG









RG






GO_
GO_
Histidine
H

Up
MMDLVEGTEEASGALMLPPA
71


1106
1106
kinase/response



PAVGRASILCVHLLALAAAE





regulator



GGGEAALLLRDADGVRVLGG





hybridprotein



EGSAIAAEGAACLMDGQSLD









ACTVRLLPVRSGAVEVWLCV









RRNAPALEHVLALCALQVDD









LLRERAAAPQSGEHELVERM









QLRMQRMADTADVAFYRCDF









ATRVVTGDARFASLWGLPPE









RLAVGVPIDELLMFLHPDDR









LVYDGSLEDELRDEGCYELR









FRILVSSPSMPGSGQAQSRS









PRSSLLRHVLLRGWREDESR









PDSRRSVGLAMDVSSASMTA









EALRSSEAFTRLLLSSLPDC









IHILDCEGCIRFVNEGGIRS









MEMDSPIIMHGLPWVDLWRG









QPRRRAALAVQTALAGETAR









FQGYAMTMRGQRRFWDVAVT









PVFGEDGDVRRLLAIGRDLT









EANQSAERLQLALEAGAIAG









TWMWDDSTSRMTGDARLAQT









LGLDPARMREGVMPNVIYDS









VDPRDRFAVVQAVTAATRRG









GKCRFEFRVDTPEGQRWFEG









NGRCDLGDEGRVARFPGIVF









DIDRSKRQALRQAALVELGD









QLRALDDTSMMEEVAARIIC









RELDASGAGYGVVNDDWTGM









TVGGAPEVTRPLVGMRMFAD









YGEFRPILGRGEPVAIADVH









TDALTAGYDARYDAEGIVAI









LCVPIFKFGRFVGLMFVCHD









APHIWTDEEIVFTRAVADRT









HASMRQARTQQQIRDLNVML









EERILQRTRERDRLWNIARD









LFIIIDRRGYYVAVSPSWEE









TQGYRVDELAGLRLDALCHP









DDRRMVLDTFERLLAGTPWP









TAGLDVRMRRSDGTWRTYNW









NCNDEGDAIYAVGRDLTERN









ELEEQLRQAQKMEAVGQLTG









GLAHDFNNLLAGIGGGLELI









GLRLAQGRTDGLGRYIAASQ









DAVRRAASLTHRLLAFSRRQ









TLDPTPTDMNALVRGLESLL









RGTVGPGIELLFDLQPGLWL









TRVDANQLENAILNLCINAR









DAMHDRGTMLRLESANRVLT









ADVATDMSIRAGDYVVLTVQ









DEGCGMPPEIVQRAFDPFFT









TKPLGEGTGLGLSMIYGFTQ









QSGGQVEIHSTPGQGTVVSL









WLPRYQGQETIRPEPPLLPV









ASQPRLLEGQRVLVVDDEEA









VRMIVSDMVTDLGGIVLTAS









DGPSAEALAAEGVPPAVLIS









DIGMPGGMNGRELGEQMLKR









WPGLKVLFITGYAEQSVLGD









QALVPGCALLVKPFTVAAFS









RKLAVLLKGD






GO_
GO_
DNA protection
H

Up
MVSRTDRHVTQNNTADNTKN
72


1168
1168
during starvation



VSIETLNARLSDLIDLALIT





protein



KQAHWNLKGPQFIGVHEMLD









GFRSSIDGFSDTVAERAVQL









GGTALGTVQDVSKNSACKPY









PNNIYRVADHLAALIDRYAT









VANNMRESIKVTDEAGDDDT









ADVFTEVSRGLDKHLWFLEA









HVQEPTGQMRDGDHKGSRS






GO_
GO_
hypothetical
H

Up
MSFKRRLSALLSSRGKLEYA
73


1174
1174
protein



IHLTETGQAVQGFALLSRLA









ATGDAEAAFRVGRAYLDGLG









VPPSLEDGARWIYQAAEAGH









IEAAFVLATLYTVGLPEGFE









IRTAGEGLDLSHVPQVGPRH









PDFHLGLRWAKIAADAGSPD









AQALLGYILTNGPEDLRDLT









QARSWYDRSAAAGCSQGHLG









VALSILHEAHSDEDLSAAAR









HLIEATKGGLGTAFDILGRM









YESGSGVPRDLGKAASYFHQ









AAERNIVTAQARYGLMLLEG









TGTPRHYGRAETWLKRAAAN









GDTQSAALLGDLCANGGDLP









PNLMEASKWYRLAAEQKHAG









AARALGLLYLTGNGVHQDPD









VAAHWFRVASEAGDAHADAD









FGNLILAGASATPDEKQALH









ARFEKAAEKGDLVGAYNLGV









CFAEGVTGTKDGREAARWMQ









KAADGVVNAQYWYGRMLLEG









RGVQPDPTQALYWMEKAANA









GMAEAQVTVAGLLVDGSING









RQDHEKALTLYRKAAESGNV









DAMFSLAAMYGGGHDVPENR









PQAQLWFRKAAQRGNGLAQM









MLGRYLVRGLAGVTDPVEGR









IWLERAKAQNIRDAEVELAL









LDEAQPDDDD






GO_
GO_
Bacteriocin/
H

Up
MEHTQSLSGPDGRVSPTVIR
74


1176
1176
lantibiotic 



LYAVLAAARYHGLELDIRDF





efflux ABC



AAEPGEDSPSPATLARWLNE





transporter,



QGAVAKGMRLRWRYLVKIRN





permease/



SPPVVLMFKDGSAGLMVRAD





ATP-binding



AEKSVVWLRDPMGGEGDTPV





protein



PVDELRLMQVWTGDVLLVKR









RRDESEADAKFDLLWFAKMV









LREKKVMRDIAFASLILSIL









QIFPALIVMQVVDRVVNYHS









MATLVSLSGFVIILSFYEIL









LTYARRELSLILSTRLDARI









SLHAFNRLLALPLEFYEREQ









TGEILGRFMAVFKVRDFLTG









QLMSTLLDLFTLIVVLPVLF









VMSPTLAWMTLAAAGCIGLI









VVVFLPPVTRVIGRQVLAEM









KRGSILYETVAGIRTVKTLA









LETTRRELWDERTADVVRWK









LAAGRMASWPQTLVMPFEIF









INRGIILVGAYLILTNASSM









QAGALMGFMMLGGRVASPLV









NLAKLMEAFNEVSVSLSEAG









MVLNQPTETKALTTGMRPVV









KGALSFNHVDFSYPGSTTKA









LNDVTFDIPAGTMLGLVGRS









GSGKSTITRLLQGVSRNYTG









YLRLDGVDLREINLTHLRRS









FGVVLQDNFLFRGTIRDNIT









AGRPGLTIDDAIRAARLAGA









EEFIERMPAGYDTWIEEGST









NISGGQRQRLAIARAVISDP









KLMILDEATSALDPESEALV









NANLQRIGKGRTMVIVSHRL









SSLVNCHQIAVMDQGKLVDI









APHRILLERCEIYRMLWLQQ









NRHMTDNDVPGSAGQLTEGE






GO_
GO_
O-
H

Up
MSSENWRTATRLLHEAPNRT
75


1380
1380
succinylhomoserine



EFGETSEALFLTSGFVYDSA





sulfhydrylase



EQAAATFTGDVQHFQYSRFG









NPTVDTLQERLALLEGAEAC









VATATGMGAVSSAILSTVKA









GDRVVASRAIFGSCYWIVTN









LLPRYGIETELVDGTDYDAW









ERALSRPTAAVLIESPSNPM









LDVLDIARVAELTHKAGGLL









IVDNVFATPLGQSPLRLGAD









VIVYSCTKHIDGQGRVLGGA









VLGSSKWINETLQPFTRNTG









NALSPFNAWVLLKGLETLQL









RTDAMARNAAAVADALAELP









GIVQVRYPGRADHPQHELAK









AQMSNGGSMVAFVVDKDREG









AFAFMNAFKVIAISNNLGDA









RSLATHPATTTHMRVSEEER









ARLGITDGAIRLSVGLEDPA









DLIDDLKRGAAAVAALA






GO_
GO_
Large exoproteins
H

Up
MAVPDFPRPPRRRFRPFCPG
76


1389
1389
involved in heme



PHFPRHLHIARWAALACVTP





utilization



IALFAAAGSVFLWELAHGPV





oradhesion



DITRVSHLVEPVSIAAGKRP









GHPAGRLSWDTLRIQWQPAA









GGVPAGLVLMARGLKVTRFD









NLIAERADEADAVLSLSALF









EGVIAPRTLRLENATLALRR









LPDGDVDMDLPNQKRGGRGV









PTRLDRLRAIDVHNVSITLA









GLPQDRTAVIGPVEMQARRI









RVAPHSPDFVWTGTARTMVM









LDGLRTTLTAQARQVGNTGR









LHLDSTPFEPAELGVFSPLA









ADWHVPVSVGADAVFVPHGM









DEQPSELTLNLTLGDGQVFQ









KTAEPIHLHAGQASVHLRMD









RPGLDGGATVSVPSAGLDVA









DNAGALTHVHASASLRLDSL









RQPRVMDGDAEAGLDGVRFA









TLGSIWPASIIKGGRRWISR









NITDGTGRDLEVRAHLHGDH









GPDSILPVSVQGQLTGRGLT









VNWLRPVPPATGLDASLHFD









GPETLVIDLSRGVQPTGVKE









NVLLPDGEIRIGDLYAKDQT









GDISTHLTGPLAGFMSALAH









PRLHLLARHPLPFTHPEGMV









DAHVRLTLPLVAHIPDGALH









VWTQAMFSGVHLGNVLMGQP









VDGASGKMSATEDGLDLTGD









GRLAGIPTHVVLHENFQGGA









PSRVLQTIEARSVLDPQSTA









KARIAPGGLFDGHAVLNAHF









VQQANEMSDLKLSLDMAQAA









LTVPIWAKPMGEPATAMVHI









GFQKGRMSVLDGLQAHGTGL









SVAGRGVTRAGKLTGIVLEG









FRIGRTEGDARIALPQAVDQ









PIGVTVDADPLDLAPMFAPH









PPTAAAPVSQGSSGAKGASM









GDNWSISLNAPHVYYGPKAQ









VGGVVSQIELRNGHLTSGRF









ALDAPTRVRAVLADTGREHP









FVLDIDNLGTLLEGLGLYDR









IRGGQTHLDGVFTPDETTVR









KVPEGRNTKSAGLWGGLPPF









RGHVEMGPSQFLRPPLTLTA









VSDLSPLHWLTNHLDRFEIS









HLATRLSLAGNLLVLHDGVI









GNQALGATMEGPIDLTTSTL









NLNGTIVPLFGLNALPGRLP









VLGHLLSPEKGGGLLAATFD









LHGTVEKPDLSVNPLSMLLP









GVMRRILH






GO_
GO_
5-aminolevulinate
H

Up
MNYDAMFQSALDGLHADGSY
77


1418
1418
synthase (EC



RYFADLERRAGNFPKAFHHG





2.3.1.37)



LGRDVTVWCSNDYLGMGQHP









EVLTAMHKALDETGAGAGGT









RNISGTNHYHVELEKELASL









HGKESALLFNSGYLSNWVTL









GTIAGRLRNCVVLSDELNHA









SMIEGIRHSRAEKQIFRHND









IEDLERRLKELPADVPKIIA









FESVYSMDGDIAPIEAFCDL









ADKYGAMTYLDEVHAVGMYG









DHGAGVAEKLGLSHRLTVIE









GTLGKGYGVVGGYIAASAAL









CDFVRSFGSGFIFSTALPPM









IAAGALASVRYLRSSSAERE









GQQRAVAYLRQALDKAGIPH









VMNPSHIVPVMVGEAELCRS









LSDELLNRFGNYIQPINFPT









VPRGTERLRITPTPLHTNEM









IDELVEALATLWQERQLKTS









KSAAA






GO_
GO_
hypothetical
H

Up
MRFSPSVLTRIGRWAAVVLP
78


1436
1436
protein



LALTHVRVAGEADLDLLAVL









LLLHSGLTGRRQGGWDWFRE









PWVVATFCWWGWQMLCTLWV









SPGHGALVQSLLAIRFPLAA









AALGCWLLKDALWRRRVLWL









ACACGVYIAFQMLIQAVFGR









NLFGIPRFHDGTLTGPYEHP









RAAAPLSRLILPLLMVGCAA









VEGARSRLVRTLGLCTATVV









AVGIMVLAGQRMPLALSLLG









IGVCALLYRPMRPAALAAAA









MLPVLVLVARVFSPGSFFHL









VTLARQQLTHFGQSPYGEIY









THAIVMAQAHPWIGQGYDAY









RHFCSDPSTFHGISGLSEAV









PERGWLDLCVQHPHNHYLQA









LVNAGVPGLILFVLMIATWL









KAIWPGRNGAAISIGLFAAV









FIQEWPIASSSDFLNLPLSG









WGFLLLGLALAYRTFRGVDG









FQAGRDRPIS






GO_
GO_
GDP-mannose 4,6-
H

Up
MPTALITGITGQDGAYLSQL
79


1441
1441
dehydratase (EC



LLGKGYRVVGLLRRSASADV





4.2.1.47)



IGERLRWLGILDDVELLDGN









MTDLSSLIRIVETVKPDEIY









NLAAQSFVAASWQQPLLTGN









VTGMGAVNMLEAARIVKSDA









RFYQASSSEMYGLIQEPVQN









EKTPFYPRSPYAAAKLYAHW









MTVNYRESFGMHASSGILFN









HESPLRGIEFVTRKVTDGVA









RIKLGLAKELALGNLDATRD









WGHARDYVRAMYLMLQQEVP









DDYVIATGRTTSIRDLCRIA









FSSVGLNYEDHVVTNPAFLR









PAEVEVLLGDASKAKKTLAW









EPETTLEEMITEMVEADLAR









HSKRNGL






GO_
GO_
GDP-mannose 4,6-
H

Up
MRLLITGLRGFVGQHLQHQV
80


1442
1442
dehydratase (EC



RKRFPGSEIMAGIPDIRDAQ





4.2.1.47)



AVEKVIAAEKPDHCVHLAAV









STIGAARKSPDHAWDVNLRG









TLNVARAMLRHVPHSTFLFA









STAEAYGTTFQLGTALTEDA









PLAPGNTYAATKAAADLALS









AMAREGLRVVRMRPFNHTGP









GQSPDFVVPAFASQIARIAK









GLQKPEISVGNLDAQRDFLD









VRDVCDAYLDVLTAKKPLTP









GTILNVCSGETRSIRSILDD









LLAISGINAEIVTDPDRLRP









SDIPVARGDATLITSTLGWR









RQIAWEDTLRNVYEDCMRKT









TA






GO_
GO_
Lipopolysaccharide
H

Up
MTKEYTIWIDVEDIFRYFEN
81


1446
1446
N-acetylglucosaminyl



NTRPSGIQRLVFEILSVIRH





transferase I



QAAAKPDIGRIVLTRRNTGA









RAETGPLLSPVSFDALNTLF









STHTEETTPTQAGERSAAHA









PSHSLMRRLRHAVIRRIESL









PPELARPLLNLAVNQLRALQ









LLRRYARAKFQRATPSRNTV









QAPLSPTAPAATSVDVPKPG









DIFLILGAAWSEPDFGERLG









RMRRAYGIQPVLLLYDLIPA









VRPEWCAISLIRDFRHWLDT









TLPQCGRLLAISHATAETVE









DYARKQRLKLLAPVQTIPIG









SGFGPPHKVGNERPKGLPTK









GSYVLFVSTLEARKNHLLAF









RIWRRLVTELPRDQVPTLVF









AGRVGWLVSDLMQQLENTEW









LRGKIRLLRDPSDEELAHLY









DGCMFTIFPSLYEGWGLPVT









ESLVNGRPCIASNTTSIPEA









GGPLTRYFNPEDLDDAYRVV









RETIEDRAGLKKWQDEVREQ









FQPVPWERSADAILDACHSA









HLTGRMNGQTS






GO_
GO_
glycosyl transferase,
H

Up
MTLWIDIDDLLHHLLHHSRP
82


1447
1447
group 1



SGIQRVVFEIGSALRNLAGH









NVQFVRRGPGATDARDFRTV









DWTMVETVFREATNSSIKPG









SSSVNAPPLTVQALEEVAPE









DTLSAFLRTESRILKGLAGL









PRTFARLGLKALQTRLEARR









ARPELPTFSEGTQLADVARP









GDVFLTLGSPWHHASYSQTV









RWLRDDLRLSYALLMYDLVP









IRCPEWCNRGIITTFRAWHQ









DILPLADTLFAISHATAKDV









RAYLAEQDIGTDIPVHPIPL









GTGFGLSDGGMSAEALVREP









YVLFVSTIEARKNHALLFRV









WRRMLEEMPAERVPTLVFAG









REGWLVSDFMQQLENADWLK









GKIRFIRNPTDEDLRRLYAD









CSFTVFPSFFEGWGLPVTES









LSMGRPCVVSNTTSIPEAGG









PLGRYFSPYSLDEAYTVIRK









TIEDPEGLAAWTAKVRAEFR









PVPWEDSARAILDRVL






GO_
GO_
Radical SAM
H

Up
MTTAPPPGPLSLYIHWPFCL
83


1460
1460
family



AKCPYCDFNSHVREVIPQQR





enzyme,



FAAALRRELEHDAARLTRDG





similar



VKRPLRSIFFGGGTPSLMAP





tocoproporphyrinogen



ETVAALIEDAHRLFDAEDDL





III oxidase,



EITLEANPTSVEAGKFAAFR





oxygen-



QAGVNRVSLGVQSLRDDALH





independent,



KLGREHSATQAIRALETART





clustered



LFPRISFDLIYARPGQSDAD





with nucleoside-



WTDELTTALDLVADHLSLYQ





triphosphatase RdgB



LTIEPGTKFEAMHRRGELTL









PDEDTAARLYDLTGEIAARH









GLLPYEVSNYARPGAESRHN









LTYWRYADYIGIGPGAHGRL









TLDGELYATRRHRAPEPWAE









RVEKTGSGSTEETLLTPQEK









GREALLMGLRLSEGIDEARF









AARTDRTLMECVDPALLEAC









IEENYLERANGILRATGEGR









LRLEAILARLVT






GO_
GO_
7-carboxy-7-
H

Up
MSYAVKEMFVTLQGEGAQTG
84


1506
1506
deazaguanine



RASVFCRFAGCNLWSGREQD





synthase (EC



RATAACTFCDTDFIGTDGEG





4.3.99.3)



GGRFETAEALASTIEACWTD









TADDSGRRYVVFTGGEPLLQ









LDDALIAAVKAHGFEIAVET









NGTIVAPAGIDWVCVSPKPG









GALVQTEGAELKLVYPQPEL









SPELFEQLSFRHFWLQPMDG









PDRIANTQAAVAYCLHHPRW









RLSLQTHKLIGIP






GO_
GO_
Outer membrane
H

Up
MAFLVSGQALAAPATSFTPA
85


1516
1516
protein



QRAEIVGIMRDALQNDPSIL









TDAIRAIREKAEEQKQDSTL









AAVKAHQSELQSAPDFAIRG









NPHGRITVVEFYDPRCSYCR









SMMGEVDSFLSRHPDVRLVE









KVVPVLGNNSVLDTRAIFAA









SAQGKYEAMRRALMADTTKP









SMERIVELAQANGIDTKKLT









ADMSSPQTVALINTNLDQGR









AVGLDGTPTFIFGTAAVAPG









ALEADQMDAFLERARKA






GO_
GO_
ATP-dependent Clp
H

Up
MKMHAGSGNDMDITRMTPTR
86


1530
1530
protease



LDDEPDAPEPETREDDNKTL





proteolytic



NSPISELEGRLFDQRKVLIF





subunit(EC



GGINDKIARDVTGRLLALAG





3.4.21.92)



TSDKPIDVYVNSPGGHVESG









DTIHDMIRFVDSIAPINMIG









TGWVASAGALIYAAGRPERR









VCLPNTRFLLHQPMGGVRGP









ATDIDIEAREIIKMRERLNR









IFAKETGQTYEKVAKDTDRN









YWMSANEAIAYGLVNRIVHS









ATELK






GO_
GO_
Phosphoribosyl-ATP
H

Up
MGKPATKPAPKPSKQQDDKK
87


156
156
pyrophosphatase (EC



SDLQQELVLQRLYDTVQSRR





3.6.1.31)



GTDPSLSHSARLMARGRNKI









AQKFGEEAVECLIEAVNGNR









KELIGESADVLYHLIVMWVD









AGVSPEDVWTELKRREGTSG









IAEKAARPKEKLG






GO_
GO_
N-acetyltransferase
H

Up
MTITCERVVSPLPPEDLDAL
88


158
158
/Phosphoribosyl



IEATSAGILDGGGFGWLQPP





formimino-5-



GHQALARYFEGLLLVPERSF





aminoimidazole



YVVRENGVICGAGQLVRPPA





carboxamideribotide



SYEAHAATANLTGFFVAPYA





isomerase (EC



RGRGLGRALLEAMLKGAKAI





5.3.1.16)



GCKVVNCDIRETHVAAIGLF









RSFEFEHWGTHPYYARIGGQ









TVRGLFLSKLLANENEAARW









QSSIAMPDTSSAASDTMTDT









PTPAHDLTLYPAIDLKDGAC









VRLRRGEMEDATHYSDDPGA









QAKLFAEAGCRHLHVVDLNG









AFAGRSTNIPAIESIVKATN









LPVQLGGGIRDMAAIERWLE









AGVSRVILGSVAVKDPELVR









QAARAFPGRIVAGIDARQGR









VATEGWAEVSELEANDLALR









MEDAGVAAVIFTEITRDGML









AGLDLEQTADMARRLSIPVI









ASGGVGSLEHLKALRDVARD









VPGISGAIVGRALYDGRIAL









KDALDVLGSC






GO_
GO_
Citrate
H

Up
MSENRSVTFGLDGLSRQFPL
89


1600
1600
synthase (si)



LEGTIGPDVVDMRALSQKTG





(EC 2.3.3.1)



VFSFDPGLGSTATCTSAISY









IDGDKGVLLHRGYPIEDLAL









NASFTETAYLLLYGELPTAA









QYQAFRTDMNTHRLLNEQIR









NFFNGFRRDAHPMAILCGTV









GALSAFYHDGLDISEPKARD









LSARRLIAKVPTIAAWAYKY









SIGEPFIYPDEEMSFSENFL









HMLFARPGNHYRVNPVLARA









MDRILLLHADHEQNASTTTV









RLVGSTGANPYACIAAGIAA









LWGPAHGGANEAALGMLETI









GTREGIPAFLNEVKNRDSGV









RLMGFGHRVYKNFDPRAKIL









QATCHEVIEELGLKRDPLLD









LAMELERVATEDDYFVSRRL









YPNVDFYSGLILKALGIPKS









MFTVLFAVARTVGWVSQWKE









MIEEPSVRISRPRQLYIGAA









ERSFVPMSERR






GO_
GO_
Putative phosphatase
H

p
MTRIREHGIRVVGDVHGDFN
90


1603
1603




AFRHATATDRFVIQLGDLVD









HGPDSAGVMELMLELLEQQR









GLFILGNHDRKLGRALEGRR









LRRDPPLEETLRQISLPEYE









GLPERAYRAIDQAPTWLRIG









RSLFVHGGFHTAMLSHSPVP









GLGEMSAPLSRALFGETTGR









MQPDGYPERRLTWINRIPEG









MTVYVGHDRRSTDGRPWRRT









GRLGGTAVFTDLGAGKGGHL









AWIDLNEP






GO_
GO_
Acyl-CoA:
H

Up
MSHRDAKTPNGRRGHNRPVL
91


1612
1612
1-acyl-sn-



EGKPDFPASRPTTSTTLYSR





glycerol-3-



LRCAGRLSLVLIWAFWACSM





phosphate



QAILVRLPGRLKIMMPRIFW





acyltransferase



KGVCRILGIRIRVIGHSAGG





(EC 2.3.1.51)



VRTARDVREGKRPVVFVANH









CSWLDIAIIGSTLPVVFVAK









GEVGKWPLIGTASRLGRTIF









VSRNRRETGRELHDMAARLW









DGDDIVLFPEGTSSDGSRVL









PFLSSFFAVAKPGRLEQVGM









PKAPPVLIQPVSVVYDSLEG









LPVGRSRRNVFSWYGDMDLA









PHLWSFGQWRSMGASLMLHD









PITPDDFRSRKDLSRATFEA









VNNGAAELRRGQPKVTGP






GO_
GO_
Response regulator
H

Up
MAPSLTVLLIEDDFLIRTCL
92


1616
1616
receiver



AEFLLDSGLTVREADNCAEA









RAIIGAEPKLDALVADMTLP









DGDGMTLVQPARERWPDLPV









IYISGHGDLRRDETSGDPAR









DRFISKPYTLASILEALLDM









TSAASD






GO_
GO_
hypothetical
H

Up
MKRLHFSNMDQAVVFFASRT
93


1618
1618
protein



GSLALATQETLSVMCFQSRF









QTCIHKER






GO_
GO_
FIG00688344:
H

Up
MTLPVLVLAGSRDGENDVLA
94


1653
1653
hypothetical



KLGQVSHKALLPVAGQPMLA





protein



RVLDTIARTPGLGPVTISIE









NPDCIRDLAGDATILRSAPS









PSESVAEAIARIGTPCLVTT









ADHALLRPEWIQEFLAKAQG









CDLAAAVALRATVERDVPGT









KRTYIHLSDMSFSGCNLFLI









GTPKGRNVIELWKRLQQNRK









RPLRMALTLGIGTLLRAVTR









TLDPTALYRRIRTLTGANVR









LVTLSDGRAAVDVDKPSDLT









LAEKILAQTTP






GO_
GO_
Sphingolipid (S)-
H

Up
MSNFKAPWRNMSAIRTGRSF
95


1654
1654
alpha-hydroxylase



DLGKMNLQQLWFAYLTYPTI





(no EC)



LLYFALIAVSTWAALHFSTA









LWATLIPVPVVIVVYPLAWY









AIHRFILHGRWLYRNHWTAS









LWKRIHFDHHQDPHLLDVLF









GSPLNTVPTMAIITMPIGGL









IAGWSGAFCALSTALVMTCI









YEFFHCIQHLAYKPRWKWVA









DIKQLHVLHHFHDEDGNYGI









TNYVPDRLFSSFYREARDRP









RSKHVFNLGYDIEEAHRYPW









VMDLTGSPPRDRPDGARPAS









ARAAADRNRAA






GO_
GO_
Lipopolysaccharide
H

Up
MKQRAHILDRYLLTQMAPPF
96


1656
1656
export system



AIALLAMLVALLLERLLSLF





permease



DYLASAGSSLGTCIALLTDL





proteinLptF



LPHYFGIALPAALCIAVFLT









IRSMSDNNEIDALQAGRVSL









MRISRPFMIVGLLLGAASVF









LYGYIQPVARYDYRAGFYFA









EHTGWAPHLQAGMFASTSSK









AVMTADSVSHAGTRLRRVFI









REVNANGVAHIITARTGALT









ISEKTRSTRLDLWNGEIVDD









PFQATKPHKPTVTHFEHVVR









VIDRPNKETSFRSRGADERE









LTLFELAHDLRYGLPGIEYR









TLRAEMDFRMARAIAIPFIP









PLAVALAISARRRKSVWGLI









AVAVILIGFDQTLMFGHSLA









STGRLPIWLAIWVPEVVFCV









GCLAALLRRSRGSWRRRKFT









RAPA






GO_

Serine
H

Up
MTDIFAKHHGLREAYEGLTA
97


1660GO_

palmitoyltransferase



ASPRNPFEVVIERPISASVG



1660

(EC 2.3.1.50)



IIEGRETLLFGTNNYLGLSQ









SKKAIGAAVETAETMGVGTT









GSRIANGTFGLHRKLEAKLA









EFFRRKHCMVFSTGYQANLG









TISALVNKDDVLLLDADSHA









SIYDGAKLSGAQVIRFRHND









PVDLEKRLARLKDHPGAKLI









VAEGIYSMTGNVAPLDKFVD









IKTRHGAYLMADEAHSFGVL









GAHGRGVAEMQGCEDGIDFV









VGTFSKSLGTVGGYCVTNHD









GVDLMRLCSRPYMFTASLPP









EIIAATMAALEDMQARPELR









TKLQENAARLHAGLQKVGLK









TGEHVSPVVAVTLETVDQAV









GFWNALLENGVYVNLSLPPA









TPDNRPLLRCSVMAAHSPEE









IDRAVAVFGEVARHFGL






GO_
GO_
Homoserine O-
H

Up
MDISASPSIADGPVYTHQTV
98


1749
1749
acetyltransferase



RLDSGLDLECGVHLAPLEVA





(EC



YCTYGTLSPARDNAILVCHA





2.3.1.31)



LTGDQYLAERNPLTGKPGWW









SRMVGPGLPIDTDRYFVVCS









NVLGGCMGTTGPRSICAETG









KAWDSEFPPITMHDIVAAQA









KLIDHLGVDRLFAVIGGSMG









GMQALTWAADFPDRVFAAMP









IATSPFHSAQNIAFNEVSRQ









AIFADPDWHDGHYRDFGAIP









ARGLGVARMMAHITYLSEEA









LSRKFGRRVRHDAATAVPAS









SSPSLFGEMFEVESYLRHQG









SSFVRRFDANSYLTITRAMD









YFDLAAEHDGDLANPFRKSQ









TRFCVVSFSSDWLFPTSQSR









LLVRALNRAGANVSFVEIES









DRGHDAFLLEEPDFDRTIRG









FIAGAAEHAALKVGER






GO_
GO_
UDP-N-
H

Up
MSGFPSHLLAGERYAVCGLG
99


1794
1794
acetylmuramoyl



RNGTAVVQALLRMGAEVQAW





alanine--D-



DDRNANLPAQPNLTVAPLTD





glutamate



LSGMTALILSPGIPHLLPKA





ligase(EC 6.3.2.9)



HPVADLARAQNVQILSDAEI









LYRAARKSGSKAAFVAVTGT









NGKSTTTALIAHLFTTAGRP









CAAGGNLGTASLALPLLPDD









GVYVIEMSSYMLERLDRFHA









NAACLLNLTPDHLDRHGDMA









GYAAAKAHIFDNMGPDDLAV









IGTDDDWCRSIASQVASRGV









QVAELDADTLPPYDGPALPG









RHNAQNVGAALAIARHLGLD









DAVIRTGLRSFPGLEHRLQK









VAECDGVSFINDSKATNAEA









VSKALAAYDNVMWIAGGVAK









AGGIESLAPFFAHIAQAFLI









GQDADVLAATLETHGVPFQQ









CGTLEKAVPAAFEAARNENI









PVVLLSPACASFDQFRSFED









RGSHFLQICDNIVKSGHSGT









NPMQKQED






GO_
GO_
FIG00688361:
H

Up
MDAESKSEGAATGGIAADRL
100


1806
1806
hypothetical



RSIIERVERLEEERKALAGD





protein



IKDIFSEAKSAGFDVKVIKQ









IIRLRKQEPAEIEEQETLLD









IYRRALGM






GO_
GO_
Transcriptional
H

Up
MGKKDEDRRIGERGENQMDW
101


1836
1836
regulator, LysR



DKLRIFHAVAEAGSFTHAGD





family



RLGLSQSAVSRQISALEDVL









RVPLFHRHARGLILTEQGDV









LNRTVREVFSKLALTQAFLS









ESKERAAGKIKITTTTGFGL









SWLSPRLNRFLELHPDIEVT









LLLEDADLDLGMREADVAIR









LHPPTQPDLVQRHLANFPMP









IYASAEYLERNGTPHSLEDL









ANHQIISFAGWHLPLPNVNW









LLDLLRQEGVARQGSRRLAI









NNISAVANAIAAGTGIGSLP









LYAATGYPELVRILPNQQVP









LVEAYFVYPEELRTSKRIAV









FRDFLLSEISNLKGHE






GO_
GO_
Integration
H

Up
MSTVTRANLVEHLYSRVGLS
102


1854
1854
host



RHDSSMILESLLGVISDRLE





factor alpha



AGESVKLSGFGTFSVRQKGE





subunit



RIGRNPKTGVEVPILPRAVL









VFRPSQLLRDRMNGSENGAA









DEASSHDR






GO_
GO_
Uncharacterized
H

Up
MTDFSPPPSPDTITVEASAS
103


1856
1856
UPF0118 membrane



TGTIQRRARGFLALFFVAIG





protein



LYTLKGFLPALLWGCVFAIS









IWPLYRRAELRFGRSDWLPM









VFTLAVALIFLVPVSLVGVK









VADEARSALEWIDDVRNNGI









PMPEWVPHLPFLSAQATNWW









QNHMTSPQRLSHLLHSVDVG









HGMQMTKQVGSQLARRGTLF









AFSLLTLFFLLKDGDSVIRK









CLLGSQRLFGEQGESLAKQM









ISSVHGTLAGLVLVGLGEGA









IMGIVYMATGAPQPLLFAMV









TAVAAMIPFLAWPTVGLVAL









LLLAKSSMIGAIVVLAIGSV









VIFIADHFIRPALIGGSTKM









PFLWVLLGILGGAETWGLLG









LFLGPAIMAALHLLWTLWTE









VNPRKGVYAEDKGS






GO_
GO_
Putative outer
H

Up
MRSRLTFSIGATAVLALSST
104


1909
1909
membrane protein



AMATPLQDPYGTWTVQGEND









AISTLKGTSDQYYTSGLRIN









WTSGTDNLPRPIAKLNHILM









GDGVQRISIGLQQIIDTPRD









TQADNPPQGDRPYAGLLLGT









VNLINDTDLSRTVMGIQFGM









LGPSGLGRQVQNGFHKAISD









TPSTGWSHQLANQPIFQVQA









GRIWRVPVLNVYGIHADVLP









AISGAAGDYRTYADVATTFR









IGQGLDSDFGNATIGPGLDG









TDAFRATRPFAWYFYGGVEG









QAVGYDVTLQGSTVRPNAPH









VEKVWDVGEIHAGVAVMWHG









VRLSYSQNWQTAQFETQKAG









LFNYGSLKLSVKF






GO_
GO_
UTP--glucose-1-
H

Up
MIKPLKKAVLPVAGLGTRFL
105


1922
1922
phosphate



PATKAMPKEMLPVVDKPLIQ





uridylyl



YAIDEAREAGIEEFCLVTGR





transferase



GKDSLIDYFDIAYELEATLK





(EC 2.7.7.9)



ERGKKSALEALAPSSVQAGS









LVAVRQQEPLGLGHAIWCAR









SFIGDDPFAILLPDDIVKGR









SCIGQLVEAYNQTGGNVVAV









TEVPPEHTNRYGILDVGSDD









GKLVEVKGLVEKPAPEDAPS









NLSIIGRYVLTPDVMKYLAK









LERGAGNEVQLTDAMAKTIG









EVPFHGLRYEGTRYDCGDKA









GFLEAQIAFSIDREDLGASV









KAFLKKYKQYVDAP






GO_
GO_
UTP--glucose-1-
H

Up
MPFRHDFDPTSLREYDIRGI
106


1923
1923
phosphate



VGKTLHPADAFAIGRTFASM





uridylyltransferase



VIRAGGKRIVVGYDGRLSSP





(EC 2.7.7.9)/



ALAEALVRGAVESGAEVTRI





Phosphomannomutase



GCGPTPMLYFASVADGADGA





(EC 5.4.2.8)



VMVTGSHNPPDYNGFKMMMG









GKPFYGDQIRELGRLSASGD









VLPATNGTAARIDISGRYID









RLVQDYDGIRPLRVVWDNGN









SAAGAVLSRLVERLPGEHTV









LFGEIDGHFPNHHPDPTVEK









NLQDLIRVVDEKQADLGIAF









DGDADRIGIVDNRGQIFWGD









QMLVLLAQDVLSRHPGATII









ADVKASQILFDEIAKAGGQP









LMWKTGHSLIKTKMAETGSP









LAGEMSGHIFFADKWYGFDD









ALYAAVRVLGIVSRLPGPLS









DFRDSLPVTVTTPELRFNCD









DKRKFEVITEVAERLRKEGS









DVSEIDGVRVNTADGWWLLR









ASNTQAVLVARAEARDEAGL









DRLKAALAAQLEASGLDAPD









FSGENAGH






GO_
GO_
hypothetical
H

Up
MSPPSSNRPFSQPSDQPSVG
107


1932
1932
protein



TVLRARREELGWRLEDVAEW









LRIRPKLLAALEADDLSKLP









GVAYAVGFLRTYAHAMQLDA









DALVERFRRDTRGAVTRKPE









LVFPQPEGDRGLPVGVLVGA









GLVVVVAAYVGWYRFTEHDN









PAQRQVPAVAELMPGAATPA









MTSPQVASVMPGRAPTPEPH









APVTASSVPATPAPVPTQNA









PAPELPAAPAGAQSTPPSAA









PSVAPPASDDDSETTPPAGE









AAPTQQTDTQQTGAIGRPAT









DLPPAVPEGAVVLRALAPVW









TQVRDRDGHVLMSRVMQPGE









SWQGDPAGAPFRMSFGNAGG









IVLTTAGATSAPLGKEGQVR









RNVEVTADAIRSGAFGSGVA









LPVQPNAPVSVPGAASAPLA









VAPAPVPPRAPSVSVPRKAP









TAPEVSADDLNARQLEHQPL









EQSSPPH






GO_
GO_
hypothetical
H

Up
MIAIGPAMASQPAWLKAATI
108


1945
1945
protein



IVGTFILEDVATVLSAIAAR









AGEVSIPLALGALYFGVAVG









DMGLYGLGAAGARWPYLKRF









LTLPKRERTQDWFSTNVIRV









VAISRFVPGARLPLYTACGF









FRAPFLPFAMTAVLATLVWT









TCLFLLAMRVGGWLLAHQGG









WRWAGLAGFVLCIVVVGRLI









ARLQTVSQ






GO_
GO_
Hypothetical
H

Up
MTLPDRTDIPAPHDDLVVRP
109


1984
1984
protein



VTTRADLKLFMTLPRRIYAG





associated



MAGFVPAFDMEQDDLLNPKK





with



APIFRHASIRYFLAWRGNTA





Serinepalmitoyl



VGRIAAIVDHRAIEHWGMKI





transferase



GCFGALDAVPEGSVVSALLE









MARNWLRLQGMQTMRGPVTL









SGNGESGLMVEGQDQPLMVA









MPWHPRLLGKLVEDAGYKPV









EDLLSYKLDLDDQTESRFKV









PGDLKIGEGRLGAIAIRRLS









KKQIAQQGEILRQLYNDAWS









DKFNFVPLQDYEMKAMIKQL









GPVLRPEHYVQIDQNGEPVA









MALVVPNIYDIAGDLGGAPS









PLGWVKLVARLTTHRFHSAR









VILLGVTQRLRGTVLGALLP









SLAIAELMRRRKSLPYSWVE









LGWIQASDSNMRNLAESIVP









EPYKRYRLYERPIDDPA






GO_
GO_
Oxidoreductase,
H

Up
MNTAQQLRVGIVGAGHFGRF
110


1999
1999
Gfo/Idh/MocA



HALKSAANPAEQLVALYDPD





family



PARAAIVAREARCGIATSYE









NLLEQVDAVIIAAPAEYHFR









LTSQALRAGRHALVEKPIAA









TLDEAHALADLARETGKVLQ









VGHLLRYSAEHQAITERIKA









PLYIEATRIAPYKPRGTDVS









VILDLMIHDLDLVLAIVDSP









IAEIDALGAAVSSAHEDIAN









ARVRFENGCVATITASRISL









KTERRMRLFSQDGYLSADFM









ERKLSFIGRERGMPLPGTGG









FRREAISWKDHDNLAVEHEA









FAASCLHGTPVLVDAQAGIR









ALDAAIRVTDSIRKSRQIME









LSGLIPASDKN






GO_
GO_
LSU ribosomal
H

Up
MKSGIHPDYHEITVIMTDGT
111


2004
2004
protein



EYKTHSCYGEPGATLRLDVD





L31pprotein



PKSHPAWTGVQRMMDTGGQV





L31p, zinc-



AKFNKRFAGIGTRTK





independent










GO_
GO_
hypothetical
H

Up
MTLPLMPKATAVWLIEKTGL
112


2006
2006
protein



TFTQIAEFCGMHPLEVQAIA









DGEVAAGINGYDPIKNHQLA









EAEIKRCEADTNARLKIMPT









SSPVKRRAKGARYTPVAKRN









DRPDAIAFVLRQFPQLSEAQ









IVKLLGTTKDTITKVRDRQH









WNSANIKPRDPVILGLCTQT









DLNAAVTAANDRLAREGHAL









PVVEAYVPDSDSHA






GO_
GO_
Phosphoribosylamin
H

Up
MARRRQLYEGKAKVLFEGPE
113


2062
2062
oimidazole-



PGTLVQYFKDDATAGNGAKS





succinocarboxamides



GIITGKGVLNNRISEYLMLK





ynthase



LHEINIPTHFIRRLNMREQL





(EC 6.3.2.6)



IREVEIIPLEVVVRNVAAGS









LSKRLGIPEGTRLPRTIIEY









YYKNDALGDPMVSEEHIAAF









NWAAPQDMDDMNQLALRIND









FLMGMFTAVGITLVDFKLEF









GRIWEGEEMRILLADEISPD









NCRLWDSKTNEKMDKDRFRR









DMGRVEEAYQEVAKRLGILP









ESGNGDLKGPEAVQ






GO_
GO_
Anthranilate
H

Up
MTVSADFTSLLHKAALGRHL
114


2075
2075
phosphoribosyl



DSHEAETAFHAIMAGEVDPI





transferase



QLAAFLTALKLRGETFAELT





(EC 2.4.2.18)



GAVQAVRHHMTVLPDVPAGA









IDVCGTGGDGLKTLNVSTAV









AFVLAGLGVPVAKHGNRALS









SATGATDVLEVLGIPPTDDL









ALQGRRLREDGLVFLAAPQH









HPAMRHAAPVRKALGFRTLF









NLLGPLCNPAQVRHQLIGVF









DGRWCEPVARALGALGSLSV









WVVHGSTEEGGSDELTLAGP









SQVSAWQDDTLFSFGIEPDM









AGLAAAPISAIRGGDAQTNA









AALLALLDGAGGAYRDTVLL









NAAAALHVAGRGDIVKAGAI









DVPAFRRNVGMAADSIDRGL









ARAALEAARMSAHSIAPKDA









GRS






GO_
GO_
LSU ribosomal
H

Up
MGKSNVIQIRLVSSAETGYF
115


2086
2086
protein



YVTKKNARSATGKMEVRKYD





L33pprotein



PVARKHVVFREAKIK





L33p, zinc-









independent










GO_
hpnB
Hopene-associated
H

Up
MLFGTALTSLGAWIYLSLFH
116


2109

glycosyltransferase



GKFWQKGPILAQKPTPVCAP





HpnB



DVAVVVPARDEADSIRECLT









SLLEQDYDGKLSVILVDDES









ADGTGDIARALPDPHHRLTV









ISGQKRPAGWSGKLWAVHQG









EQEALTRIGPYGYILLTDAD









IMHAPGHLASLVAKAREDDL









DLVSEMVALNCESTAERFLV









PAFVYFFAMLYPFSRIASEH









SRIAGAAGGTILLRRRALER









IGGISALRGALIDDCTLAAH









VKRSGGRLYLGHSALAWSVR









PYRGMKDVWHMIARTAYVQL









RYSPVLLIATIIGMATIWLL









PVALALFGKGRERRVGLLTY









LLSCLTFVPTLRRFGLPLWR









AIPLPLVAAFYMAATIGSAF









DHHRGVGVRWKNRSYTDETS






GO_
GO_
Predicted integral
H

Up
MSKRYVTKTLKKTLPVLLSL
117


2111
2111
membrane protein



LGVALFTFIAAKAGIHPVME









ALSKVGVGGFLLLAACQLLI









DMGLGVAWHAAVPLLSVRRL









MGARLVRDSAGACLPFSQLG









GMVIGVRATLAGVDPRTVKG









EELHWPEGVAANLVDITTEV









LGQIAFVLIALLCLIGHHGA









SRFVWPLIGGMVLLSLGIAG









FIWTQQRGGVMVRKAAAFLG









KHIAAEWRDSLIGNTETFQL









RLESLWSRPDRISLGAFCHL









LCWMGSAAMTWLALQLLGAH









VGFFSSVAIEGVVCGIMSAG









FLVPGALGVQEAAYVALGMI









FGIDAEISLSLSLLRRGRDI









LIGIPVLLAWQIVEMRRLRH









APPSEASKSTPAPSPASARK









TVIPPAVTALAGNIKKEATS









RDGKKTEDTPFATAPRVL






GO_
GO_
UDP-N-
H

Up
MKVLVTGVAGFIGFHVAHAL
118


2144
2144
acetylglucosamine 4-



LKQGMEVVGVDTLNAYYDPA





epimerase



LKAARLEQLEPYPGFSFLKV









DVASPAAMQDLVARHPDLEG









VIHLAAQAGVRHSMVDPYSY









VTSNVMGQVALLEACRHLKK









LTHVVYASSSSVYGRNQSVP









FRETDRVERPSSVYAVTKRA









AELMSESYAYLHGIPQTGLR









FFTVYGPWGRPDMAYYGFAK









AISEGRPVTLYEGKHLSRDF









TYIDDIVRGVQRVLGRPPEA









GMSRVLNLGGDKPERVTRMI









ELLEQNLGKKAFVERRPRPV









ADMESTWASLENVREFCGWK









PVVSFEEGMKEFCLWFRKFH









GI






GO_
GO_
hypothetical
H

Up
MRVLCCALVAALGMSAGVAK
119


2145
2145
protein



AEDPITQAQARLPTAPLTIT









TRDGQKHEFTVELAKTYRQQ









EVGEMFRKHLPENEGMLFMW









ATPQVSDMWMRNTLVPLDIV









FIDSTNHIHAIAENAVPLSE









AILRSDGVVANTLELAGGVT









AKLGIRVGDAVTSSALKH






GO_
GO_
hypothetical
H

Up
MKHKSCRKTFFSALALSAIA
120


2148
2148
protein



FFSGQAQARHSSGHHGRTVF









HSHRSSSHRHSYAHVIQCVA









YAKTASEVVLHGNARDWWYN









AAGVYARGSAPQAGSVLNFR









AIRRMPLGHVAVVRSVEDSR









TIYIDQSHWASNGIAHNVRV









VDVSPNNDWSAVRVALNDRS









GRLGSIYPTYGFIYPHSDNG









DRNPAPHVVMARASTVSGFR









HRAVLNGSDALSHPMNSTEV









AEAPDDAFTSDAPDRSIR






GO_
GO_
Ribonucleotide
H

Up
MTDPDDSALRSVTLPAAWDD
121


2185
2185
reductase of



EAAQALAQITLNGGPVRLAA





class II



EAARWVDTIDACPPLPGTPA





(coenzymeB12-



NTPSPGRSLSYLLLMQQMAP





dependent) (EC



NTALWQCQPDQTPGFTIRLS





1.17.4.1)



SFVQEAGFAAEHFVACLRLA









CDALRRLHAATRIERTGELP









LFDLPAQPEDEAAGLILLTD









LDACLAALGLDYDSDDARTA









ACAMAALATTVARAGTKLSP









PSIPESPLPGLRTIASSVCA









TEEGRHFCPIETGFSSPAAT









EGLLGVETCGLAPAFSPLRE









DGHLRASTLARLACRGLTPE









SALALALAGETPLPPVRPQA









QAAMHAAVKNVVDFLPAVPE









PDLADLQARLARGVRRPLPM









RQTGFTQRAAVGGHSLFMRT









SEFEDGTLGEISLTPPRESP









MARGLMDCLGHAVSIGLQYG









APLEAFVERFAYTRFGPAGT









VEGDPSTAYATSMLDYAFRT









LSEAYLGEHMPDAPRVEPSS









EDPAPMLPFGRGSGESPEWK









DRGRRLKLVS






GO_
GO_
Uncharacterized
H

Up
MTLNLRHYALLGLLAFLLAL
122


2192
2192
integral



PGRMTLPPLDRDEPRYMEAS





membrane,



EQMLLSHNFIDVRFQDKPRY





glycosyltransferase



LQPAGIYWLEAASTAAAEKI









FGPSVLRKTWPYRIPSLLAA









TIIVPLTAWIGATLFGGATG









LMAAGLLMVSTLFVAESHMA









TIDTVLLLDILCIEAALLCA









LTDRQKSRPTHLRVAVAYWL









ALGVGLMLKGPVVLIPGFGT









PLALWFLEKDRSWWPRLRPR









WGWMLMIAVVVPWCVAIEVI









SGGDFFARAVGRNFLGKVTH









GQEAHGLPPGFHLLVFGLAF









WPGSLFAALAIPSVWKNRKL









PQVRFLLSWIVPHWLVFELI









ATKLPHYVLPTYPAIAILTA









ASLMAWRPLTLSRWAKALLG









VYGVLWAVIGIAFCLAGSIA









LYKLEHTFSLSALIALGGSL









PLMLGAIMMLLKQQRRQAAF









CAMGAAVIAHAGLFLSVIPN









LQTIRLSPRIADLFEDVRPC









NDSVLISSSYSEPSLVFLVG









PNTQLIGPEAAAAYLHDHPQ









CSLALIDIKDKNIFMSTLKK









FGINVVEYNKIEGLNYSNGH









HLNLELFAPL






GO_
GO_
S-
H

Up
MNALAQLGMVSELPRDIQNG
123


2210
2210
adenosylmethionine



AAHLVEEERKDYFIERDGER





decarboxylase



YAGNHLLIDFWDARNLDDPM





proenzyme



RIDETLCEAAVAAGATILHS





(EC 4.1.1.50),



HFHHFTPNGGVSGVIVLAES





prokaryotic



HISIHTWPERNYAAVDVFMC





class 1B



GACDPNLSIPVMQRLFQAGR









IEVDAVRRGRVQDKAVKAA






GO_
GO_
tRNA
H

Up
MNAPKTTEAKTAIIVAGPTC
124


2214
2214
dimethylallyl



SGKSALALDLARTFGGTVIN





transferase



ADSMQVYRDLRILTARPDAA





(EC 2.5.1.75)



DEAAVPHRLYGVLDAAVPGS









VAWWRAEALREMDAAWAEGR









MPVLCGGTGMYLRALTDGLV









EVPDPGDAARTEARGLAEEI









GPEGLHARLMQVDPETASGL









RPNDTQRISRAWEVWTGTGR









GLAWWRSQPGLPPAPCRFVS









VRLDPERDGLRRAIDSRFAQ









MLDAGAIEEVSHLLERGLDP









VLPAMRAHGVPELASVLRGD









VTLEEARKSAVLAIGRYTRR









QATWFRHHALGEAEDSMVSL









RRYTHSAQESESHYEKIENF









ISERVDAAALSS






GO_
GO_
hypothetical
H

Up
MLVHYGYGVVGIIVMFESMG
125


2262
2262
protein



LPLPAESVIIAASLYAGSTH









HLEIRWIALAAVLGAIMGDN









IGYLIGHHFGYGILKKHGYK









VGMTEERLMLGRYLFRKHGG









IVVFLGRFIAVLRVFVALLA









GANRMPWHSFLFFNAMGGIC









WAGGYAFVTYELGKQIEKIS









GPVGVVMAILGVSCLIGALV









FLKKNEKRLTEEALREAEAD









EKRDEARADTKPS






GO_
GO_
Histidinol
H

Up
MKRLDTSAAGFSEDFAKLLA
126


2297
2297
dehydrogenase



ARGSDERSVAEPVRAILADV





(EC 1.1.1.23)



RSRGDEALCDYTARFDRLTL









PAEKLRISTEEIASEAARVP









ADLMDALRTAARRIETFHAA









QMPKDLDFTDEDGIRLGMRW









TPLDAVGLYVPGGKAAYPSS









VLMNALPARVAGVKRLAMCV









PSPGGVLNPLVLAAAQLCGV









EEIYRIGGAQAVGAMAFGTD









LIALVDRIVGPGNAYVAEAK









RQVFGHVGIDSIAGPSEVVV









VADGQNDPRLVALDLLAQAE









HDEQAQAILITTDAAFADRA









AEAVRKELETLPRTTIASKS









WDDHGAIIVVRSLEEAAEIV









NALAPEHLEVMLDAPRDFSA









MIRHAGAIFMGRYCPEAVGD









YVGGPNHVLPTSRTARFASG









LSVFDFIKRTTTIETDEAGL









RRIGPAGVALATAEGLDAHA









LSLSVRLEKN






GO_
GO_
hypothetical
H

Up
MPRHHSYRNRSLLALMVLEI
127


2348
2348
protein



CVPRMAVAASPASAATPVTQ









APLIQASVTQAPVTQTEEWI









HVPSTERPPIQNYPHAGVVA









QPRRVVASQNHAPQGRQGQW









GAFSYGNGESAGFGPVGRYG









VAPWAEDWSFLRDKSRRDDP









FDPLKFIALNDAKTIWLSFS









GETRLRNWYEETPFLGKKGG









SNSGRFGVRNLYGADLHLGE









HVRLFGQLINADAAGWKGFG









YNTTYRKRLDLQQAFIEFKG









KLAGAQTGFMFGRQQFLDAP









SYVLYNRETPNVPLSWNGGR









IYAIWPNIRVDAFDFVQTKT









DATLMFHDTEDYGTRLYGGD









ITALVPQFSIGGETVHSFLD









VFYYGYRYGGSLSVVPLASG









SLKGTSSRGNVGFRWYGTAA









SFEYSFGGLYQDGTFQKSGS









EHKSGVQAYSINTIVGYRHT









PSPLHPFIGVQADLYSGGAN









GTNGPVRTYMAPFNPQTNYL









DTTTYIQPSNLVSLSPVLSV









TPWKGFASIQFKVPFMWREN









ADGAIWNSSGPYTFSKTYHG









GYIGVVPQASLKLQLNRHLT









WQIYGARFMASNGLHAAGGK









SGSYAQSNVVFRF






GO_
GO_
hypothetical
H

Up
MRQPLPARLALIALLGCGLA
128


2355
2355
protein



ALPDSARAEPAIMPPPPPAP









PAPPSLQAPLTASGTLVIPA









TCLDRLSIVGGENAHIVSGS









GSLEKHGDRLTFTTSPQDCA









TQDSAVVMVPALTSIDIQLP









HSRLTTYRITGVNGDVTAIS









GRGNIDIDQASGLTLTMQST









GNVSVGHVTGRLSVQNLSSG









DLHIGDLAASSASITAMSSG









DIRVEQGTVDVLTVRDYGSS









TITLNAEARDADITLLGSGD









ITLRKVSEALKKRPIGSGTL









SIGDATSSRITSVNTPDGAA









ILSDATRKILDRLDIQLDSP









DHVSRTTDHNRHHSGGYGVI









GVLLKIALIVWAVRLFRRYR









RTGVLPFRKTLDKAAAGYAE









GVQSWSRHRAAWRDTPGASA









TAVVRDTMAGFRRQQPDPAE









DFSRSVAPGHPLARLQDRLV









RMERRLGLMEQFVTSPDFSL









ERQFRDLERADGRRA






GO_
GO_
Creatinine
H

Up
MLFLRRLSCRVALLCVGMGL
129


2373
2373
amidohydrolase



SVPAVRAQGVLEAPPHCSGL





(EC 3.5.2.10)



ALQAEFACRSWTEVAQDVKA









GTDTVIIPVGGTEQSGPYMA









VGKHNVRAQVLADAIAVQAG









HTLVAPVVAYVPEGSTSPRT









SHMKFPGTISIPPAVFEGLL









KGAAESFRVQGFRRIVLLGD









HGGYQSFMAQVAQELNRAWK









GQAAVLYLRDYYEVVPHQYA









EALRAQGHAAEVGLHAELSD









TSLMLAVDPSLVRQDALRAA









PKPGVAEGVYGGDPRRASAG









LGRIGTEMQIRTAVAAIQSF









QRSHP






GO_
GO_
hypothetical
H

Up
MTFKTPLLVAMTLLGAAAAH
130


2374
2374
protein



AQEYSPSAPMVPVPADASAP









VAAPVAPSGIQTIPGMPPVI









DPKNIYSETTPSHISPAIAH









DPARVYVPNLRGDSVSVIDP









ASFQVVDTFRVGHSPQHVVP









SWDLRMLWVINNSEGRPDGS









LTPINPATAKPGPSIAVDDP









YNMYFTPDGKYAITVAEAHK









RLDFRDPHTMELKGSVETPE









CKGVNHADFSIDGKYAIFTC









EFGGYVAKVDTVNLKMIGML









KLSKGGMPQDILTAPDGHKF









YVADMMADGVFVVDGDSFTE









TGFIPTGIGTHGLYPSRDGK









LMYVANRGSHRIHGPKHGPG









GVSIIDFATDKVIKTWMIPG









GGSPDMGNVSADGKLLWLSG









RFDDVVYAIDTDTGAMRKIP









VGAEPHGLTVWPQPGRYSVG









HTGILR






GO_
GO_
5-hydroxyisourate
H

Up
MSSLSTHVLDTVSGKPAAGV
131


2388
2388
hydrolase



SLRLLQGDRVLFEGQTNTDG





(EC 3.5.2.17)



RCPELRDVAVSKGIYCLEFQ









IGDYFRKGGQVLSDPPFLDV









VPIVFGLAAEAHAHVPLLAA









PFGYSTYRGS






GO_
GO_
Pyridoxamine
H

Up
MSDIPLIDLKADPFALFAAW
132


2435
2435
5′-phosphate



MSDAEKSEPNDPNAMAVATA





oxidase



TPDGRPSVRMLLLKGVDERG





(EC 1.4.3.5)



FVFYTNLESRKGRELLSNPH









VALLFHWKSLRRQIRIEGPV









EAVSTTEADAYFASRSRMSR









LGAIASDQSRPLDDRSTFEE









RLKAVDGKYGDGPIPRPANW









SGFRVLPEAIEFWQDRPYRL









HDRAVWTRDGNGWNVTRLYP






GO_
GO_
hypothetical
H

Up
MLIDIKNILLPLNGSGDLEA
133


2436
2436
protein



VMSVALDFARRFDAHLSAVV









VGSDPSEVATLAGEGISAGM









VNEMIDTATTEAQRRAISIR









KAFDAFIHEHGIRRVEPSKI









GSSAGDGVSASLDVLNGTEH









DSLTWRSRLADMTLVPNLAK









DGDPRASETLHAILFDSGRP









LVIAPPAPPKTVGKRIAIAW









NGTPEASLALRCILPWAHKA









EGVQVLTCQDYQRRGPGADE









VVTYLRMHGISATSREFEAV









NRDIGAGLLKAATEFNADML









GMGAYSHSRLRQMILGGVTR









HILEQAQLTVLMSR






GO_
GO_
Polyphosphate
H

Up
MRSVFLCVPEDPIVTTEDSR
134


2485
2485
kinase



PAPRRRSPRKPRNAVTPAQN





(EC 2.7.4.1)



RGRRRQTAAARAEDYAHMLT









SPERFLNRELSWLDFNQRVI









DEAENPRNPLLERVRFLSIS









SSNLDEFYSVRVAGLVGQVR









EGTVVRSPDGLTPAQQLVQV









RQKARHLLAEQQRVWHLLEG









ELKEAGIVILPTDSLDETDL









AQLSTLFDERVFPVLTPMAV









DPSHPLPFIPNMGLALHMRL









KDAASSAHVMDGLILLPAQV









PRFLRLPARLKEGQETPDQI









RFVLLEDLITLFAGRLFPGL









VIGAAGVLRVIRDTDVEFED









EAEDLVRSYETALKQRRRGV









CIHLALDRKLPDTLGREMGE









ELGVGEEDVVVLPSFVGVTD









LKQLIVDDRPDLVFPPYTPR









FPERVLDYDGDCFAAIRAKD









MLVHHPFESFDVVVQFLRQA









ALDPNVLAIKQTLYRTSRDS









PIVHALIEAAEAGKSVTAMV









ELRARFDEEANIRLSRALEA









AGVQVVFGFAHLKTHAKLSL









VVRRENGSLRSYAHFGTGNY









HPITARIYTDLSFFTCDPKL









ASDSARLFNYMTGYAIPAKM









DALAFSPITIRSTLEQLIQD









EIDHAKAGRPGRIWLKMNSL









VDAELIDRLYKASQAGVKII









GIIRGICCLRPGVPGLSDNI









EIKSIVGRFLEHARVFAFGN









GHRMPSHKAKVFISSADWMV









RNMDWRVEAMVPITNPTVHA









QILGQIMTMNIKDNLQSWTL









TRDGYWHRVSPGAHPFSAHE









YFMNNPSLSGRGSAAREKVL









PEAHRPRERPDRILED






GO_
GO_
UDP-N-
H

Up
MPARRIALNVVLDGVVSAAA
135


2496
2496
acetylglucosamine



APVARWLADPAGGWLHPLWF





4,6-dehydratase



IAGGGITLLVGGLPFRIPQQ





(EC



YWRFSGVADLFNIACASVLS





4.2.1.135)



ALLFAELLHVAGYPLPTPTF









PIIHALVLLVFLGAIRMMWR









LAARRRSLALDGERILLLGA









DHEADLFIRAMERDSGNNRR









VVGLLTGGAQQAGRRIHDCP









ILGTISETPAILERLFAAGK









LPDALVITAGEIKGRELAQI









LEAARVYDIDVQRTPSLTAL









QPADRVELRPIAIEDLLNRP









PVALDSQGMARLICGRVIAV









TGAGGSIGSELARQIASFQP









AMLLLIESSEYALWQINLDI









SERFADVKRQQIIADVRDRR









RIAEVFGMYRPHLVFHAAAL









KHVPIVEDNPVEGVLTNVIG









TRIVADEAERAGAQAMVMIS









TDKAVNPSSLMGASKRCAEV









YGQALDMRARAGQGGMRCVT









VRFGNVLGSTGSVVPLFRRQ









LEHGGPLTVTHPDMTRYFMT









VPEAVGLVLQAAVRGTHERA









QNDATDLRLRQGGIFVLDMG









DPVRIMDLAFQMIRLAGLRP









ETDIEIRFTGLRPGEKLFEE









LFHGREAPVPTDAPGLRMAS









PRTVDFKVAAAAMDELETAC









HASDLGAIMSILYRLVPEFL









HNRDGGMPVAMSHPDPEMIA









P






GO_
GO_
Putative
H

Up
MGMPGDNRPQDVQVSSVMEE
136


2511
2511
transmembrane



ERLSVDVGAAGGTCVETGQR





protein



KRRWQVFMSRAPALVGLVLL









VAAVVVIWRELQHLSLHDIT









ASLSAIPDSALLAGGAATVL









SYFILSFYDRLACLHVRAKV









SYQRSAFAAFCSYVLSHNLG









CAAISGAAVRFRLYRSWGVA









PGAIAQIIAFCSATYLLGTM









ALIGGILIIEPHAVPVLSHL









PEFLLRLAGLALWGVLLAYV









LVARVRRHVRIWKYEIELPG









PGIAIAQIAVSAADMAATAL









IAYCVLPPLPPEAHFGFGTF









LAIYLASYTAGLMASVPGGL









GVEDGAMLLALQAYLPASQI









MGAILVFRLFYYIIPLLLAG









LMFAGHELFLRGEQALVSAG









QTPRRVRPSQVIRESEADFS









VAVATSVQAVVGILLVLYAL









VADLPPLQTSLGAAVSQIAD









LLLTVAGVGLVALSWGLSQR









VALAWKFSLGMLGSAALLLM









LRHAPWEGPVVIVLVMLLLL









PFRNCYYRRAHLLAAPLTPS









MLAPLSLWGLGLLGVGWVAV









QRHLGPIWWRSMIYDAHTAV









GRWFLGFSALCGFYVLWRGM









RRTRIRFEAWTAENAHRYHS









LAHALPQLGARRPTGLLLDE









AGRAAIPFLRTGQFIIGLGD









PAGSERNCVAAIWRLRDLAL









QEGCKLAFIQVGQSLMAVYN









DLGLTVCPDRTAGTVCCFSE









DYRMLRAFLKGEERLARKRQ









PQTASGLTGS






GO_
GO_
Glycerol-3-
H

Up
MTTRPHIAVIGAGAWGTALA
137


2544
2544
phosphate



CATAATGADVTLWMRNPVPP





dehydrogenase



GTRTLPRLPDITLPDNVTIT





[NAD(P)+](EC



GDFPRTADIALLVTPVQTAR





1.1.1.94)



DVSTRLQTVLDPAVPVVTCC









KGLEQATSLLPLDVLAETMP









GRPTGVLSGPNFAIEVAKGL









PAAATLACTDLALAQKLTAL









LNTSSFRLYASDDAAGVQLA









GAAKNVIAIGAGITIGAGLG









ENARAALITRAVAEIGRLAE









ATGGRASTLAGLAGMGDLIL









TCTGRGSRNYSVGLELGEGR









PLTDILASRTTVAEGVLTAP









AMLALARQHNVRVPIIETVT









RLLNDGVSIEEARHLLLDRP









PTRE






GO_
GO_
Heat shock
H

Up
MSGRLFTSPMFLGFDHLEQM
138


2589
2589
protein,



LERAAKSTSDGYPPYNIEQL





Hsp20 family



SSTALRITLAVAGFVMDDLQ









ITQEDNQLVIRGRQADDSQG









RIFLHRGIAARQFHKAFVLA









EGIEIGGAWLDNGLLHIDLL









RPEPEVRVKRIAISQGRRST









APGPAVHHEVVPPVVKARRT









TRPARDIDDE






GO_
GO_
tRNA
H

Up
MSDTQAAEPIAEPAIEPTGL
139


2592
2592
pseudouridine



NRWALRIEYDGTGYLGWQKQ





(38-40)



NDGTSIQGLIEAAASKLVRN





synthase



RPVPSITAGRTDAGVHAAGM





(EC



VIHLDFPDDAPIDARQIRDG





5.4.99.12)



MGYHLKPHRVVVLETAKVGP









EWNARFSATWRSYRYTILNR









PARPGLMENRVWHIKRPLDV









DLMQQAANHLLGPHDFTSFR









AVACQARSPIRTLDVLNIHR









DGELVVIDTKARSFLHHQVR









NMAGTLMMIGSRQWPVEKII









EILEAKDRCAAGQTAPPEGL









CLMDVGYPDDPFNRF






GO_
GO_
UDP-3-O-[3-
H

Up
MSDMTASESRPGDSRFFQRS
140


2607
2607
hydroxymyristoyl]



GPFGLERLAEVSGSEIIPAA





glucosamineN-



SGKGLSEFRGVAPLHVAGPD





acyltransferase



EISFLDNRRYLPLLAETKAG





(EC 2.3.1.191)



AVILSPAFTDKLPPDTAGLA









CKAPYLAWARVATLFHPAPA









STGVRHPSAWIAEDAEIGEN









VEIGPFAVIGSGVRIGRDSI









VASHVSIGQSVEIGERCRIG









AHAAISHARIGDRVTLYPGV









RIGQDGFGFAVGPEGFETVP









QLGLVVLEDGVEVGANSTID









RGSMRDTLIGAGTRIDNLVQ









IGHNARLGRCCIVVSQAGIS









GSTELGDFVTIAAQAGLIGH









IKIGSKARIGAQCGVMSDVD









AGADVIGSPAMPFREFFRNV









ATLRKLSRKSGD






GO_
GO_
Periplasmic
H

Up
MTLNSLMRTVSAGALLAATI
141


2608
2608
chaperone



LVSAPGAHAQASGGNGGWFV





of outer



PKAAHPDAPPPRPVQRRVPE





membrane



AAPDEEEDSAPAEQQQAPPI





proteins



LPLPPIPAPPSIAKASPPPA





Skp @ Outer



AVIGVINVQAVMQISSAWQE





membrane



IQQVLGARRDRLAQAVQREE





protein H



AAWRGEQQKLQAQARSLTSD





precursor



QIQLRERHLQERRAKDQHDF









GNQARIIQEAAQVAMHQIER









ELEEPNGIIAAVAAAHNMNL









ILHAEQVVLHVGGQDITEEV









GTQLNKTLPHVFIPDDGVDP









EQLARSGKMPTTADEQRQAQ









GPQAPGQQQAPASAPSESVL









RQHH






GO_
GO_
hypothetical
H

Up
MLLRQNERTALFIDGASLHH
142


2622
2622
protein



AARNLGFEVDFRSLRNLFES









QCLFQRAFYYAAMPETDDYS









PLRPLTDWLAYNGYHLVLKN









AREFTDHSGRRRIKGNMDVE









LTVDLLEQAGRLDHAVIVSG









DSDLRRAVEAVQARGVRVTV









ISSMRSTPPMIGDDLRRQAD









LFVELADIAPSFTRRQAEPR









NPSRQGPVRHPADINSDETS









DS






GO_
GO_
Glutathione
H

Up
MRILHHLPLSPQCRLVRLAL
143


2643
2643
S-transferase



SEKRLPFEPVIERVWEQREE





family



FLHLNPAGEVPVLVEENGLA





protein



VPGGRVICEYLEDAYPDTPL









LGRTFADRVETRRLVDWFDT









RFAQEVTRNLLGEKVDKRQF









GRGHPDGNALRAGYANMRFH









LDYIGWLAETRSWLAGPALS









LADFAAAAHLSALDFIGDVN









WSKAPAAKDWYARVKSRPCF









RGLLSDKVSGITPPAHYANL









DF“






GO_
czcA/cus
Cobalt-zinc-
H

Up
MNAIVVTALKRPYTFVVLSI
144


2649
A
cadmium



MILIFGVRAIVSTPTDVFPS





resistance



IKIPIVAVIWSYTGLMPDDM





protein



SGRIVYYYERALTATVSNIE





CzcA;



HIESSSYYGRGIVKIFFQPG





Cation efflux



TNTAVAQTQITSVSQTVIKQ





system protein



LPNGATPPLILAMDASSVPV





CusA



LTLQVNNPTMSGSEIYNMAS









NLIRPELISVPGAAIPNPYG









GLAPDIMVDIDPIKLLAHRL









SPEDVAAALNLQNIVLPAGD









QRIGQLDWMVKTNSTPLDLA









VFNKMPVKQVGNSVIYLRDV









AWVHRGGPPQINAVLVKGQQ









AVLIVILKSGDASTLSVVSG









IKKLLPQVQATLPAGTTVSI









LTDASSFVKESVVDVVREMI









TAAILTSLTVMLFLGSWRST









VIVATSIPLAMLCSIIGLSI









AGQSINVMTLGGLALAVGIL









VDDATVMIENIDAHLETGKE









LEDAIIDAANQIVIPTFVST









TCICIVWLPLFELTGISGWL









FMPMAEAIIFAMIASFILSR









TLVPTMANWMLAAQVRMHRD









PEWHNRKLSIFGRFQRGFEA









RFTSFREHYKTILETLISIR









GRFVTLFLLAAVSSMALLLF









IGQDFFPEIKSGTLQMHMRA









PIGSRLEETGKIAGLAERRI









RSLLPGQVVNVVNNCGLPFS









QLNQAMIPSPTVGSQDCDIT









IQLRNSESPIAEYRRTLRKG









LTNDFPGTIFTFQPGDLTAK









ILNFGLPSPIDVQVVGRDLS









DNFRFATQLAKKLRHIPGIT









DVSIQEPMTQPTIMVNNRRS









FALGTGITERDVALNALVTL









SGSGQVGQTYYLNAQGTSQL









IDVQAPANYLQTMNDLEILP









IDKGDGNPTNQTPQLLGGLS









ALVQTGTPSEIAHYNIMPVF









DIYAAPEDMDLGTVSRAVNR









IVNHERKLLPHGSSMVVRGQ









AVTMNDAYVQLIGGLALSIV









LVYLIIVVNFQSWLDPFVII









TALPGALGGISWSLFLTHTA









MSVPALTGAIMCMGTATANA









ILVVSFARERMDHHGDAITA









ALEAGYERIRPVLMTALAMM









IGMIPMSVSNSDNAPLGKAV









IGGLLVATVATLLFVPCVFA









LIHYKRPAGPEGDRA






GO_
GO_
Membrane-
H

Up
MSHSADQGQVPPTNHPARTG
145


2650
2650
fusion



SGTRGKLVLLVVILLAIALA





protein



AWGIVQRGAHYHSLTGATED









AAIPPVTLIAPQPGPKTRQV









DLPANLAAWYEAPIYAQVSG









YVKMWYKDYGAHVKRGDVLA









EISTPSIDAQFEAAKAHYNV









ILARYNLALITTKRWTALKG









TQAVSRQEVDVQAANAAAQK









AELEAARHDVDRFQALEDFK









KIVAPFDGIVTSRLVNVGDY









VNAGGGNLNSRGTASELFSV









ADVHRMRVFVSVPQDFASVI









SPKIEAELTVPQYPGSHFRA









TFLATANAFNAATRTVTTEL









TLDNSDNLLWPNSYATAHIS









APGNPNILILPEGAIIFRAE









GTQVAKVINNHAHLVNVTVG









INFGTTVQVLSGITKDDRVV









ANPTADLLEGDEVKIVPTTP









GYNTPSKAQQDADQQPVRQH









DANPEEAGSR






GO_
GO_
Efflux
H

Up
MKPECSQSSPLQSSPSATAS
146


2651
2651
transport



SRRNRSRWRITTALAGVFSI





system,



GLASCDLSPEYHPQKFLYPE





outer



GWEGKGLMVNAQPADGVVRS





membrane



DWWTMFNDPILDGLEKRMLA





factor



VNPDLQAAAEAFTQARDVAR





(OMF)



ETESRLYPQVTGAAHMSDNK





lipoprotein



GSIGRLYNNPATSSSLVYES









NQAYSGAATWEPDFWNSIRN









TTRMQKNLAQASAGQYALAR









LSLEAELASDYIALRGLDAQ









NAVYDDSIRYFRAAVEITEL









RQAGSIGAGLDVSRAETQLY









SAQAGKSNLIARRNVMEHAI









AVLLNTAPAGFHIAPVKDVK









MHFGVVKINAGLPASLLERR









PDIAIAERQMAASARAIGVS









RAAFYPHITFSAEGGFEDGG









FDLASISRAFWKIAVQAVEP









AFTGGLRRAALQRSWSQYRS









MVDNYRSVVLSAFQDVEDGL









TQTRQFKIAQDQQQKAVDAA









LRTQSMTMALYTGGLSNYLD









ALVAQQDALQARLAEVEVQT









AQVQSSVRLVRALGGGWSAS









DLPGIKQIDPFGPLQYKDLR









TPKPVNGIDSHASPLDNDLR









GDRVSENVP






GO_
GO_
DNA-directed
H

Up
MNELMKILGQTGQSVTFDQI
147


2657
2657
RNA



KIQLASSEQVRSWSYGEIKK





polymerase



PETINYRTFKPERDGLFCAR





beta′



IFGPIKDYECLCGKYKRMKF





subunit (EC



RGIVCEKCGVEVTLAKVRRE





2.7.7.6)



RMGHIELASPVAHIWFLKSL









PSRIATMLDLPLKDVEPVLY









FEKFLVLDKGVCESDQIDSY









KNGKKRDQYLLDEIRCEDLL









DEYPDAGIDVGIGAEAIKRA









LSSYDWGIPNDQERDLSLAA









KEKGLPDPFDYDADVMEGDS









EKTMMRKKLRKATSEAARKK









LVKRLKLVEAFVESGSRPDW









MIMDIVPVIPPELRPLVPLD









GGRFATSDLNDLYRRVINRN









NRLKRLIELRAPDIIVRNEK









RMLQEAVDALFDNGRRGRAI









TGANKRPLKSLSDMLKGKQG









RFRQNLLGKRVDYSGRSVIV









VGPELKLHQCGLPKKMALEL









FKPFIYSKLEKYGHATTIKA









AKRMVEKERPEVWDILEEVI









REHPVMLNRAPTLHRLGIQA









FEPTLIEGKAIQLHPLVCTA









FNADFDGDQMAVHVPLSLEA









QLEARVLMMSTNNILSPANG









KPIIVPSQDIVLGLYYLSLE









VPEYRETPDEAVIKDGKIVT









AAPPAYSDVAEIESAMLSGS









LKLHDKIRLRLPTIDADGKS









VRQTIVTTPGRALIAQILPK









HQAIPFSLINKQLTKKNVSD









VIDTVYRHCGQKEAVIFCDR









LMGLGFRHAARAGISFGKDD









MIIPEAKATLVGKTSEEVKE









FEQQYQDGLITAGERYNKVV









DAWSRCTDEVQAAMLKEISK









QVIGKPTNSVWMMSHSGARG









SPAQMKQLAGMRGLMVKPSG









EIIEQPIIANFKEGLSVLDY









FTSSHGARKGLADTALKTAN









SGYLTRRLVDVAQDCIIVEP









DCGTERGLTVRAVMDSGEVV









ASLSERILGRTLSKDVIHPV









TQDVILPRNTLIEEAEAELI









EKAGVESVDIRSVLTCDSRV









GICAHCYGRDLARGTPVNIG









EAVGVIAAQSIGEPGTQLTM









RTFHIGGAATRGAEQSMVEA









SRDGIVTIKNRNVVENSQKV









LVVMSRNCEILLTDENGVER









ARYRVPYGARLMVSEGEAVT









RTQKMAEWDPYTLPIITEQA









GTVEYLDLIDSITLVERMDE









VTGLSSKVVVDYKQAAKGVD









LRPRLQLKDASGNVVKLANG









NDARYFLSPDSILSVENGAE









VNAGDVLARIPREGSKTRDI









TGGLPRVAELFEARRPKDHA









IIAEGEGRIEFGKDYKSKRC









VIVKNDDTGEETQYLIPKGK









HVSVQEGDFVQKGDPLVDGP









RVPHDILKVMGVEALSDYLV









NEIQDVYRLQGVKINDKHIE









VIVRQMLQKVEILEPGDSTY









LIGETVDRIEYEGENQRLME









NGDTPAKAMPVLQGITKASL









QTQSFISAASFQETTRVLTD









AATSGKVDTLNGLKENVIVG









RLIPAGTGSVMNRLRGIAAS









QDRQRVGGTSPKAVEDAAE






GO_
GO_
hypothetical
H

Up
MDADLEQYLEAGVGRLQDDA
148


2689
2689
protein



STCSRMKGLEKKVSSAARET









EALVSDLMVDQPLFWLLTSF









FIGILLGKGLFRKS






GO_
GO_
FIG139612:
H

Up
MKSPSDTLRSLFRRNRDAAS
149


2702
2702
Possible



SAPAVQAESLALPALVLEAE





conserved



KIAASLQSGVHGRRRSGAGE





membrane



DFWQFRPYHAGEPATSIDWR





protein



QSARSPVEDTFWVREREREN









AQSLMLWCDPSPSMQWRSSD









VLPTKAERAQLCTLALASAS









LRGGEHAGLLTGIEAGRALA









GRQVLPRLAASLLRPDADEP









EFPRMALVPARSDLVVISDF









LWDEDRIDTFLKTCASRPVR









THLLCVLDPAERELKRSGRI









RFEGLEGGVLTLPAMESLGP









AYEQAMNAHLAALKQSAASL









HADCIMHDTSQNPLPALLAL









HMALGGGR






GO_
GO_
DNA polymerase
H

Up
MDVGFYHLTRTPLEEALPAL
150


2752
2752
III



LGRTLDAGERALVRCPDAAA





chi subunit (EC



VMALDAALWACRDPVWLPHG





2.7.7.7)



TAKSGHADRQPIWLTEGEDV









PNGARFLFRVDGAGSDEFAP









FTRIFDLFDGGNPQSVQRAR









QRWVAMKSSGHNLVYWKQEE









RGWKKAG






GO_
GO_
hypothetical
H

Up
MRSVSTSCPDRALHILASLF
151


2755
2755
protein



HVDPVSLCLALLVIPACVQA









MQPGRPGRAVVLCLATLAAV









LGLSPAVQAVALGVIAAQDR









EACPAVWSVPALLLSALFPA









QTFVVLAVLPVLFWSALVRR









SDGEQEGGPFPAVMGILGVS









LVWHAPAAVSAELVAGLGAA









VIGLLGRSVLGACRPGDLGL









LRPVLLMVLVVAAQAEGLAV









CARIALEAILLDLSLLVLTA









ALGRVFPVLSVLRLPFPPLP









GLVVLWLGIHAALGMAAGIE









GWSVLGVAVALLLGLLGLSD









ILVVGRVFSAWQGRVSGVSV









LLVGAGSLLLPALVFGVVSP









VLHFMGGEWVWPVWRMGGGD









GASLRLPAFVLTGAVLWCVL









VRPWRVAGGIVQAASTLLPA









LGNLLSVGDGLFEEAPSLGW









KIRCVIVAGRRRFMAVRGVK









APVLPDLRQGAVGLWLVLLG









LVLAVLGVMA






GO_
GO_
Hydrogenase-4
H

Up
MIGMGRMIRSGERVALSHYH
152


2759
2759
component G



LDAEQWSAMLSAPGTTLPLI









SCWADDARAYVLLLEGDRPL









VASTAVEERRYLAPSSRFAG









AEWGERVAYDLYGVEAMDAR









GNGAPALDEGGWTSTWPLSS









RPGPAAGGLRPLAGRHLLRP









EQTGLSGPLELSFEVLKGKV









RSVEVCAGGAHRGVMSRLLG









RTPEEAMPLVSRMTAGGFVA









HPLAFARAVAQARGLVPGPG









IRDVWMLLLEIERMSLHLFD









MARTARGVDAELFATHCDHA









REAIARACAEQGVSRRLMDM









VACDGFREGLEIVPLAQAVH









AAMQPRLAALEELHRVFAPR









LDGFAVLDVRLAERFAVGGV









TGRASGRSMDMRRREAGMRL









EALRATGSSQGDARAREGLR









LAEIRDSLKLLERILGSIGL









EDDEPAPDRTDEGIGVAEGA









RGDVWYWVRLKDGRIESLHV









RDPGVSLLPVLGAMLRGYPV









SRVPAALGSIGISPAGIAL






GO_
GO_
SAM-dependent
H

Up
MLTSLARIRSDDAATFYESR
153


2764
2764
methyltransferase 2,



QGQRTALLLNGRLQSIMPPM





in cluster



RGRRILGIGYTAPYLPESAE





with



FAVSGRLLHPQTQRTTRPTR





Hydroxyacyl



SQTRNISWADCIVSSGRLPF





glutathione



DDLSMNAVLVVHGLEFTRFA





hydrolase



PDFLRAIWRTLSDDGILTLV









VPNRSGYWAHTDATPFGHGI









PYSSGQLTRLLDQALFRIEH









HSTALMTPPAALSVTHGRLM









ERAGRTLRLPCGGVHVVTAR









KNVYAGTPLIDEKLCVPLPR









QVAEPA






GO_
GO_
Hydroxyacyl
H

Up
MPLDIKPIPVLSDNYAWLLT
154


2765
2765
glutathione



AMEGQRAVVDPGEAGPIMDE





hydrolase (EC



IGEGRLDMILLTHHHADHTA





3.1.2.6)



GTDALRERYGAKVYGPRQKR









EWLPRLDHDVEDGDSFSLGS









AQIRVLSTPGHAVGHVSYVV









PGVPALFCGDVLFSLGCGRL









LEGTAQELFDSLHRYDSLPD









RTLVCAGHEYTRSNLAFALH









VDPDNEALKARAAEVEQLLE









AGRPTLPVSLGVERKTNPFL









LAPDVATFARLRREKDTF






GO_
ftsX
Cell-division-
H

Up
MSAPVSPGLRSGSLPLLVAL
155


2772

associated,



MTLLAGLSLAGLTGVQTLAE





ABC-



GWAGAARNATTIEIPSDTPQ





transporter-



LEDRTRALIQTLHKTPDITT





like



VRELSPQQVQTLLAPWLGQV





signaling



SDSGHLPGLSLPVVLIVAHT





protein



GTPDLGRVVHEALPEAVVEE





FtsX



DRRWGERLNGLGSSLVACAW









LAVSLIAAIAVLSVGMTVRR









SVMAQRKAVEIVHFLGAGDV









TISSRIAGRAALLSLAGGLA









GLFSLSPVITMLARKLAPFS









HDAGSAALPATTWQTMLASW









WNTLHVLPRLLLEELGALPL









IAACLGWLTAQTVVLVWLRR









LP






GO_
GO_
hypothetical
H

Up
MRIECPHCHAVFEVPEALAK
156


2774
2774
protein



GVKRLRCANCGDSWELGAAA









VSKSEEAPDGAVAAPEVFEV









PEEGVAAAPAVADSPVSGTE









GTFRATGAMASRSNARRSAV









LHSRSAGDVQVPTDTAGPSM









IGSTGAWIAAWGASLVLAGG









GVAALWYCKGAGVFGFLPGA









GHFS






GO_
GO_
Translation
H

Up
MTVLSADPGRIAERLPLLER
157


2813
2813
elongation



RTQMVRSVRTFFEERGYLEV





factor



ETPFAVPVPGEEVHLRCFRT





PLys34--(R)-



ELERPDGSREARFLHTSPEF





beta-



AMKRIVAATGRPVFQMARVW





lysine ligase



RNGEASNTHAPEFTMLEWYR









PGADLSSLMDETEAFLRALL









PPVVHRGMDVIDLSLPFERL









TMQAAFARYVGADLLGTAGN









AEALAAQAHVGLRNGENWED









LFFRLLLERIEPVIGRERPT









FLTHWPAEQAALARRDPEDG









RAALRFELYVGGLELANAFE









ELTDPVEQRERFATDRKRRV









ELSPDQDWGLDEDFLAALPD









LPPCSGIALGFDRLVMLATG









APRISDILWLA






GO_
GO_
hypothetical
H

Up
MGQVSIRLNGYVYNVGCQDG
158


2819
2819
protein



EEAHLYDMARHVEGWLQRAR









TLGGAASESKTLMMAALLMA









DEIFELKRRQISPQAETQIQ









QAEQLLRLEGARQERLARLA









GQAELLAAELERAS






GO_
GO_
hypothetical
H

Up
MKPWRIGRLFRTSLPADHHI
159


2828
2828
protein



RQGNAHNSDRNWAQAARAYQ









AALAVDPGLAHIWIQLGHAL









KEQGDLSQAEHAYRQATLLS









PHDPDGWLQLGHLLSLAGNV









RDSITALEEGQRISGDPLFA









AQDIAALRERQKQPQRSWRQ









PEWVTPDITGLWTSEGFCPA









GMELFDPWAYWQINPEVRQM









FDIPVALDLVQHFCTFGVSI









CLPFSLIESFDPDFYRRFCL









NGIAFTDAGAYRHWLTTGIA









QHVPANEKRWIQSLLGDRIT









KLEDVDPLLSSAFRDENAAT









HTQRTLVEGFISDLLTDPQR









PVTPTPRNAPLLHAIACRGE









KGTELHQEGARRLREKIYLH









VPTYRENTRALTRTMTTQGL









DIAAHPLLKDLARHPDEPAE









TLIALANCENRLGSLDAAVT









TLRTATGKKPGRPDLRLCHD









LQEDRNYHHAWNAALALART









GQLEAGQRHLRAYLDSLPFM









LPDHRPLRPRSGAVAIVGKL









NLLQCRLYRVEQRRDHLLAA









GYTVEIFDVDTDLDVFTAKI









AAFESVIFYRLPAWPAVIRA









IHLARSLGLTTFYDIDDPLF









DADLYPEPFETYGGTISRET









YYGLALGVPLFAKALSLCEY









AIASTEPLAEQMRHHHIGEV









FVQPNGLGEAHAIAMRRHGS









QSPSPDQPVTIFYGSNTKAN









RSEIVSVLEPALMRILKKHG









QRVRLCIVGDLPEDSVLRNL









RENITLLPPLPDVQAYWSLL









SSADINLAILGQSPTTDTKS









GIKWLEAAMFGIPSVLSDTA









GYRDVARENETALFATDTDS









WVRALDQLVTDPALRTRIGK









AAYTHALTTYSATPLASHAK









AFMERTAPPDTTARHRILGV









NVFYPPQAIGGATRVFHDNL









SDLSTPEDRRFLFEVFTSQV









EPDSKKLRVYAQDGILVTSI









APLDVDDKDRIAEDPNMVAQ









FRKVVERFRPHLVHFHCIQR









LTAGIIDVLLELDIPYCITL









HDAWWISDRQFVIDELGQPR









LYNYSSPLETLERCGAKAVA









RMESLRDRLFGAKAVLAVSE









AFAELYRTAGVHQVQTIENG









VSVLTPRPRLREESGRIRLG









FIGGLARHKGWDLIQIALRA









GSFHNLELLAIDHAMSPGDE









RTDVFGQTPVVFRGKMSQNE









VADLYASIDVLLAPSIWPES









FGLVTREATLCGCWVVASDR









GAIGDTISDDINGFRIDVSS









AADLRRVLTLIDESPARFRQ









PAPELKISRTARDQAQDLGV









LYEKLLQPGET






GO_
GO_
hypothetical
H

Up
MIFPFKSAPRLRDLARNADT
160


2830
2830
protein



ARDAKQWPEAALAYRNLLTR









YPDRVDMWIQYGHALKESGY









LVDAELAYRQAIQRSPTQAE









GYIQLGHALKLQNRREEAAA









AYREALRHDPDATVATVELA









ALGF






GO_
GO_
L-lactate
H

Up
MNHHGIAALHRRADRVLPRI
161


2845
2845
dehydrogenase



FRDYVNGGSHSERTVRANRR









AFDRWAVVPKCLVDVSECDL









SGSFLGATHRLPFMFAPLGF









GGLMYPDGEIRAARVAAASG









LPMAVSTFAIQSLETLSRVP









GVTLAAQIYVFRDRGITRDM









LRRAESCGIRNIILTVDTPI









TPLRLRDVRNGFRNLTRPSL









RHVLSMAAHPRWTAGMLRNG









MPKIGNLAPYGMGDNLMEQA









RNAASQIDPTLTWKDLDWLR









SVWPGQLAIKGIMDAGDALA









CQKAGAQTVIVSNHGGRQMD









PAPSSLSVLPDIVEALKGET









DVILDGGVRWGGDVVTALAL









GAKAVGIGRPWAWALAAGGE









RGVRSLVDGLGGEIRDVLRL









GGMVDLASLRAQGAAALRPV









S






GO_
GO_
hypothetical
H

Up
MMMPRFFRCLPLALLVVLTA
162


2905
2905
protein



CGNRYEYSRASFNGPLQCAP









YARERTGLKLSGSAASWWGQ









SVGRYAHTHTPRPGEVLVFR









ATSRVPSGHVSIVRRQVSDR









TILVDHANWEPGRIDRAVPV









TDVSARNDWTLVRVWWAPVH









SLGKRAYPTYGFISSHDSDD









SS






GO_
GO_
Paraquat-
H

Up
MSDSRNNRGEPTVSPKEAPV
163


2970
2970
inducible



RRTRFSLILLIPVVAILIAG





protein B



WLAWEHFATRGPVITITFET









ADGLTPGQTQVKNKAVTLGT









VQDITLSDDMKHVDVTVQMN









ANSAHILTDHTRFWVVRPRI









NGASITGLDTLFSGAYIALD









PGSDDGHYQKFFKGLESPPG









VRSDQPGETFWLVSPSLGSL









GPGSPVFFRDLQVGEVLGYT









MPPGGKGPIVIQAFVKEPYD









HYLRTDSRFWNVSGVQVGLG









AGGLKVQLKSLQALFSGGIA









FGLPERRRNIDLPDAPANSV









FKLYASEADADNARYHKRLR









VVTYINSSVKGLINGSQVTM









FGLQIGTVTDVRLLLEGPTK









LPRVRVDMELEPERMLSNWD









DRIENSKEPPVEKYLQAFVA









DGMRASVQSASFLTGESMIA









LQFVKNAPVTTLTYEGDVAV









LPSQAGGMDGIMESVSTITD









KIAAMPLTEIGGHVNDLLAH









ADGRLNSPEVTQSLAALRDS









LQNLSRLTKTANQNLPALMK









GLQGTLANAQSVLGAYGGDT









DFHRSLQNMITQLTQMSRSL









RFLTDYLDHHPSALITGRRN






GO_
GO_
Outer membrane
H

Up
MIPGFLQSPYGPPSFGAPYG
164


300
300
low



TTHALGDWWGAQPWLQKHGL





permeability



YVAIDDYESLSGNPIGGKRQ





porin,



SETDTGQTAVTLDVDFQRLL





OprBfamily



EMGTWSKNFWLHMLVLNGHG









RNLSQIFGDNGNQVQQIYGA









RGNVVAHLVWAYFEKSWLQN









RIDWSVGWIPTGTFFNNSPW









VCSFMNVWMCGNITPTKYLT









GGRDWPSGNIGTVLRLMPTS









HFYIMGGLFAVSPHSYNGGI









SGWAWGQDGLGKLSTEAELG









WIPEFGKDHLIGHYKVGAMY









DNSKYDDLYDDRYGHAWIVS









GLAPRKQSGQISAWVLADQM









LLRHGEGATNGLILAGAYSY









AQGQTSAMNHHLIAALMDTG









HMWGRSLDSIGIAFQWANFS









RSATLAQEAALTAGQPFQSS









NFGTPYGIQGHENIYEFFYT









YHVMTGMTLQPDFQYINHIG









GTTVFKDAVVFSLAFNVSL






GO_
GO_
hypothetical
H

Up
MRALLFLAVLTGSGLALTDV
165


3148
3148
protein



SAGAQELRRDGLSAHAVLTD









EVSQSGVDHRMLECRTDPRL









LHTVWDGRPSPHPEPHVCTG









GANRLGAGYVRYLATSRMVK









AHKPLRG






GO_
GO_
hypothetical
H

Up
MPNHPYFRATLMAALAVESA
166


3172
3172
protein



TGLSACGPMGPGKLRNDQLE









YSRALGDTQKHEMLLNIVRL









RYADPPTFLDTTQVIAGYSV









SKSISGGFYAYPATAVGNYL









FGTGTMSLGESPTFTYQPVT









GQQYAENVVRPISPTVIMPL









SLGGLPIDTLLRLTAQSIDG









LSNVRGLGAGPSGGGSVRFY









LLLHDLRQLQIQGAMTIRIT









SETPPPPDSKKNGGKSDSNG









NGGSSTGTERSYLVLTSTSD









SNLLAIQAEVRRLLHLDPGA









EEAEIVYGPYPKHPGKQIAI









LTRSMLAMLTQLAYEVEVPE









DDIKSGRTPPTIGQVGIENR









PEVVIHSSREEPDSRYAAVS









YNNTWFWISDRDFQSKLAFT









MVQVLAALAATNHTAGAVVT









IPAG






GO_

hypothetical
H

Up
MKIAFIYIAEPYQCYHTASV
167


3238GO_

protein



ASALAAIPGHDVVEYYSFPE



3238





TVEHLSRIRQALDVPALPLK









AFPKSLKARLLKRARRLDQE









RLVVLRENIAELNRYDAVVA









TEYTAGVLKEMGLSSPKLIL









LMHGAGDRYVNDEHLVREFD









LTLVPGPKVEGYFQDRGLLR









PETTRVVGYPKFDVFEAVQR









EKTISFANGRPFALYNPHYQ









RKLTSASGWMMPLIRGFKAQ









SDYNLVVAPHIKTFHRGFGI









RERQLKRQRSPEVMVDTGSS









AMLDMTYTSQAALYIGDVSS









QVYEFLGIPRPCVFLNPRKL









PWQDDPYFLHWTLGEVVEDL









DDLMPAIARAQERHALYRPA









QEKLFRETFGEPLLGASQRA









ADAIAQFMSVA






GO_
GO_
Putative
H

Up
MTTKPAGTPLSVPDDATVAS
168


3262
3262
hemolysin



VSTPASTPAPHTLASSEETL









RQMETLSTLSLNREGGFQEL









RGGTLGVRIAETAEERDAAQ









ALRYRVFFEELGARPDERAF









RTKRDVDEFDEAADHLLVID









HAKGPGAAGVVGTYRLLRSD









AAEKIGRFYTSSEYDISTLT









EFPGRLLEVGRSCVAKEYRG









RSAMQLLWRGIASYIFLHRI









DVLFGCGSLPGTDPDALADQ









LTYMHHNHLAPPALRIRALP









DRYVEMQRTDPHVLDYRACL









NKLPPLIKGYLRLGGYVGDG









AVVDEQFNTTDVAVLVKSEL









LADKYYRHYERRLRDALD






GO_
GO_
Acetyltransferase
H

Up
MLGREIRTARLVLTPVNWPD
169


3278
3278




LEDMVALKGDAGAFARMLGG









VRNRTTTEEEMAEDVSFWAR









RGVGIFAIRENGRFVGITGV









HERPDGRGLGLRFALFPWAA









GRGIAREAAAAALRYVLDCG









EKRIVAVAREDNLASRTVLG









SLGLHHTQTFDRNGDTMLLY









EITAD






GO_
GO_
Biotin carboxyl
H

Up
MIPDLKILDALMARMQALGI
170


350
350
carrier



TELDYSRDGEHIRLVRDAQD





protein of



SSPQPTSPAPAAAASTLPVF





acetyl-CoA



ETASTPPKAETTIDAPMHGQ





carboxylase



FYASPTPDAPPFVKPGDIVA









EGQPLYILEVMKTLSRIEAE









FPCRIVAVLAANADAVSPGT









PLFTVEPLDA






GO_
GO_
DNA polymerase I
H

Up
MPPEKPDLGKADLEKPHLVL
171


373
373
(EC 2.7.7.7)



IDGSGFIFRAFHALPPMSSP









QGVPVNAVYGFTNMLARLLR









DHVGTHLAVIFDAGRTTFRN









EIYPQYKAHRPEAPEDLRPQ









FGLIRDATAAFNVPSIELAG









WEADDLLAAYAKAAVEAGGC









CTIISSDKDLMQLVRPGVEL









MDPMKQKPIREAEVEAKFGV









RPDQVVDVQALMGDSTDNVP









GVPGIGPKGAAQLVNEYGTL









EQILEAAPGMKASKRRDNLI









EHADAARMSRRLVLLDDNAP









MPQPISELGCREPVRETLRD









WLEEMGFHSTIQRMGLGLAA









KPRPFTRQIVRPEDKAAARD









EVAAVTIPDAPYGPYETVTD









MDALDRWIADARTAGVVAVD









TETDSLNARQANMVGLSLSV









APGKACYVPFLHETIRDLLE









EDSTGEAFVRQLDRTEALER









LKPLLQDASVLKVFQNAKYD









LTVFRGAGIPEISPIDDTML









ISYAQSAGEHGQGMDELSEL









HLGHTPVTYDSVTGTGRKRI









PFAQVAIDTATAYAAEDADV









TLRLWQVLRPQLRTRHALAL









YEEIERPLIQILTDMEEVGI









KVDATELRRMSADFAERMAT









IEQEIHEQVGRSFNVGSPKQ









LGEILFDEMGLPGGKRTKSG









SWGTDSGVLESLAEQGHELP









QKILSWRQLAKLKSTYADAL









VQQMDQDTQRVHTSFQMAIT









TTGRLSSNEPNLQNIPIRTE









EGARIRKAFVAAPGCVLLSA









DYSQIELRLLAHVAKIEPLL









EAFRLGQDIHARTASEVFGI









PLEGMDPLTRRRAKAINFGI









IYGISAFGLAQQLQISPGEA









RSYIDAYFARYPGIRAYMER









TKEEAKRHGYVTTPFGRRCY









VPGITEKNGARRAYAERQAI









NAPLQGGAADIIKRAMVHLA









RRLPAMGLKAKMVLQVHDEL









LFEVEEQDAKALADFVRTEM









EGAARLDVALEVETGIGPSW









ADAH






GO_
GO_
ABC transporter,
H

Up
MKRGAALLAASLLLGAGAFP
172


375
375
substrate-binding



ALAQEQTPPDWNGITLGSPH





protein



RGGTLHLTADGPGGTLDPQI





(cluster 5,



NYGTQYMQVFVNMYDPLLTF





nickel/



RLARGKAGLEVVPDLADAMP





peptides/opines)



QISPDGLTWRLHLRSGLHFS









DGAPVRVEDVVASFRRIYRA









GSPTAASFYGGIAGAGECLE









TPDRCTLSGVEGHPETGEIV









FHLTKPDGEFLYKLAFPHAV









ILPASTPVHDMGGTTVPGTG









PYRITQYDPGHGMVLERNPY









FHVWNPQAQTDGFVDRIEYD









FGLSDEAQVTAVEQGRYDWM









LDAKPADRLGELGANYTSQV









HIEPLLGLYYLAMNTHEKPF









TDVRVRRAVSMAVNRHAMTI









LFGGSAISEPLCQMVPHGIP









GADLGLDCPQDMEGARRLIH









EADADGASVTLVVPNRAMEL









GMGTYLRNALQSAGLNVQLR









PITAGLAESYEQNTANHVQI









ALSYWFADYPSASTFLDDLF









GCDNYHPNSAVSPNYTGFCD









QHVQSLFDQAKAQTDPAKAA









PIWQEAGHVIMEQMPGAPMI









QMRTVDFVSKRLGNYYATLL









SHMLLSHVWVQ






GO_
GO_
N-acetylmuramoy1-
H

Up
MIAPSFTAGHWGQGMLTRRT
173


382
382
L-alanine



LVSGLSGLPLLSPVAAFGRH





amidase



PLHKKLPAPAVHRGAVPPKP





(EC 3.5.1.28)



LVMLDPGHGGKDPGAIGISG









TYEKHIAEAAASELSRQLLA









SGQYRVAMTRSEDRFIPLEG









RVELAQRHQAHLFISMHADA









LHDRDVRGASVYTLSSGASD









AQTASLARTENSADRFAGPA









FHGMSPDVQQILASLVSEET









RRGSAHMAASVVNSFRNRIG









LLTHPSRHAAFVVLKSSEIP









SVLVEMGFMSNRLDEAALRQ









AVHRTQVASAMKTAIDRYFA









THAGVMTG






GO_
GO_
Outer membrane
H

Up
MRLRTALLAMTSMVAAPSLA
174


441
441
protein



MASTITGPYVNIGGGYNLVQ









QQHGSFSPTTQADGTSSNAA









SSSRYRHHDGFTGFGAFGWG









FGNGLRVEVEGLYNYSQINH









RRPTAVNGMTHGSDQAYGGL









VNVLYDIDLANFGLNVPVTP









FVGVGAGYLWQHYNPTTTNY









VNGAVDRMGGTQGSFAYQGI









VGAAYDIPNVPGLAVTTEYR









FIGQDFVNGPYRSTAYNASG









VHKGNVNFDQRFSHQFILGL









RYAFDTAPPPPPPAPVVVPP









APTPARTYLVFFDWDKSDLT









GRAREIVAQAAQASTHVQTT









RIEVNGYTDNSAAHPGPRGE









KYNLGLSNRRASSVKAELIR









DGVPAAAIDIHGYGESKPLV









PTGPNTREPQNRRVEIILK






GO_
GO_
ABC transporter,
H

Up
MKTVFILLTVLAVGFPASHL
175


541
541
substrate-binding



PGTARAADARDTLSIGLAIE





protein



PPGLDPTRGSSEAIGMVTYG





(cluster 5,



NIYEGLMRLDEQGALTPLLA





nickel/



QDWHISPDGLTYDFTLHDGV





peptides/opines)



RFHDGTPLTCDSVKFSLLRA









GAADSTNPHRAIFSQITNIS









CPDSQHVSIRLQHPYGSFLY









QLAWNDAAILSPASVDQNIS









HPVGTGPFMFGEWRRGDHLT









LTRNPDYWGASPALRSVTFR









FMPDPLSASNALLAGELDAY









PSFPSREILSRFTGNTQLQV









VRGSFPFKAILALNNARRPF









SDIRVRQAIAQAIDRKALIQ









AVADGDGTLLQSHIAPDDPD









YVPLPDRYPYDPEHARALLK









EAGVAPGMHLTLTFPPIGYA









RDSSELIAAYLEQVGLIVTL









QPVEWPTWLGQVYGQGQFDM









TVIAHTEPHDIAIYDRTPVY









FHYHSPVFHGLAEQYEATAD









TVRRHQLSVQMQEQLAQDEP









NVFLFAIPRETVMNRRLKGL









WTNQPIAGCPVAGVSWAP






GO_
GO_
ABC transporter,
H

Up
MSSLLHVRNLGVQSPDRPIL
176


544
544
ATP-binding



HDVSFTLEPGQILAVTGESG





protein



SGKSTLALSLMGLLPPGFQA





(cluster 5,



HGSIRLEDTELSTLSEQDWC





nickel/



RIRGKRLGMVFQEPMTALNP





peptides/opines)



TRRIGTQIGDTFRLHTTLSR









HEIDTEMRMLLEQVGLSEAG









VSERAYPHQLSGGQRQRVLL









AMALACQPELLIADEFTTPL









DARTQATMMALVTRRCETQG









MAVLMISHDLGLVRHHADHV









LVMKDGACVEQGATASVFDA









PRHPYTQALLAMSLHGAART









PLTPLPIFTAPS






GO_
GO_
5-
H

Up
MKTLLPTSTAGSLPKPSWLA
177


584
584
methyltetra



KPETLWSPWKLQGEELVEGK





hydropteroyl



QDALRLTLDDQDRAGIDIVS





triglutamate--



DGEQTRQHFVTTFIEHLGGV





homocysteine



DFEKRQTVKIRNRYDASVPS





methyltransferase



VVGAVTREKPVFVEDAKYLR





(EC 2.1.1.14)



TLTKKPIKWALPGPMTMIDT









LYDGHYKSREKLAWEFAKIL









NQEARELEAAGVDIIQFDEP









AFNVFFDEVNDWGIATLEKA









VEGLKCETAVHICYGYGIKA









NIDWKNALGAEWRQYEEIFP









KLQKSSIDLISLECONSRVP









MDLIELVRGKKVMVGAIDVA









TNTIETPEDVASTLRKALKF









VDADKLYPSTNCGMAPLSRR









VARGKLNALGAGAEIVRKEL









SA






GO_
GO_
hypothetical
H

Up
MSVEFTFNIKKIPFNEDYTP
178


585
585
protein



SDSTRLTTNFANLARGEHRQ









ENLRNVLCMIDNRFNSLAHW









DNPNGDRYSVGVDIISAEMT









IRSEGKNESFPLIEVLNTSI









FDKKDDKRIPGIVGNNFSSY









VRDYDFSVLLLKHNKDQSEF









RTPDRFGDLHGNLFKCFINS









ECYKTHFRKMPVICLSVSSN









RTYYRTRNHHPVLGVEYEQR









EFSLTDQYFGKMGMKVRYFM









PENASAPLAFYFFGDLLFDY









SNMELISTISTMESFQKIYR









PEIYNSNSPAADCYQPSLKH









QDHSVTRIIYDREERSQLAI









AQGRFTEESFIKPYQDVLEQ









WSAHYSV






GO_
GO_
probable
H

Up
MPRPVFPFRTTVRTLSLIRA
179


634
634
transglycosylase



GAAFGLVGLLAACAGNNADM









GGGSELPVSQEAANYRAHAK









SYYAPPGPPSDPWGPYIQEA









SNRFDVPEAWIRAVMQQESG









GHLFDHNGNFITSVPGAMGL









LQLMPPTYDDMRQQYGLGED









PYDPHDNILAGTAYLRQMYD









IYGSPGFLAAYNDGPGSLDR









YLRRGRALPRETRRYVAAIG









PHIAGITPHNRSAADLLVAQ









HDPNSQVMLAQNTPSADIAP









VTSASERQAVSAAWNHRETA









DTSSDDSDSDTPAATPQTAP









VQVASAAGSEAPASISAAWA









ARGFTPTPARPAVRQASVPD









DEVADNRVTAQEIPIGHHLQ









PQPIMAVMPASRVQPRISLP









AISTSSRAATGNWAIQVGAF









ANAKQASIATSAAHSKGGVV









VASARSQVESVKGGRSHLYR









ARLTGLTHENAVAACRRLSH









GSPCVVVPPGAY






GO_
GO_
Queuine tRNA-
H

Up
MSDHKTDHATKMTWTPEATC
180


657
657
ribosyltransferase



GMARAGHLHTRHGTVPTPTF





(EC 2.4.2.29)



MPVGTVGTVKGMTMDAVRST









GAGIVLGNTYHLMLRPTADR









VQKLGGLHRMMDWPGPILTD









SGGFQVMSLGALRKLDEDGV









TFRSHIDGSKHRLTPEISTD









IQFKLDATITMAFDECPALP









ATPEVLRKSMEMSMRWAARS









REAFVAREGYGQFGIVQGGT









ERDLREYSIKALTDIGFEGY









AIGGLAVGEGQELMFSTLDF









TTPMLPQDKARYLMGVGTPD









DLLGAVMRGVDMFDCVMPSR









AGRTARAYTERGTINLRNAR









FADDTRPLTPHDDTPVAGRY









SRAYLHHLFRANEMLGPMLL









TWHNLAYYQRLMRQIRAAIV









DGTLDALAVKLRADWAKGDW









TEDEWPMPDLTL






GO_
GO_
Heparinase II/III
H

Up
MTGSRWLQGLRLSLARLPFG
181


68
68
family protein



GPASEGPVHAFRDPWKGDPD









QGARLIGGHFRFDRQDYPLP









NGNWERGPWPEPVREWLHGF









SWLRDLRTLGSDRARLTARG









LVSDWLAHPPTDPLVRDACV









TGSRLAAWLSNHEFCLASAD









PRLQQRLMERMLVEGRTIAA









LLPLPPQGVRGLMAFRGLLA









AAMAMPEQTGFMSRFLRYLP









GELERLVLADGTVAERSPEA









QFLVTRELAEMSVMFRTAHA









SVPPFIDRALDRVCPVLRAM









RHGDGGLAVFNGTNERHSAA









VEDVLAQGSRQKLIAPAMPQ









GKFTRLALGKSLLLVDSGPP









APAGFDSMAHAGTLSFEFSH









QRHRLFVNCGSAVVGAWRDA









MRCSAAHTVLVADGLSSADF









GPDGGMTRRPVTVSCDHQTD









GAAHWLDLSHDGYHAPLGAK









WTRRLYFGSDGEDLRGQEII









DGERNIDFAIRFHIHPDVKV









TQDDEDIILQVGGTIWRFRQ









RDGVVRLENDVYLGRGKREI









CQQIIITPRALPDAAPQEGE









AAPADEKTDAGKAVRRTHQS









VTWLLERIPE






GO_
GO_
None (90 bp
H

Up
MKHIRADKSNLSDIVTVAAG
182


721
721
upstream



HPFRGKIEPIEGAETAVVQM





from hypothetical



RDTSPSGMDWTSCVRTEVAG





protein GO_



RREPDWLRPGDILFPARGNV





721)



SLAVLINESIGSLQAVAAPH









FFLLRVSRSDVLPAYMAWWL









NQEPAQRHLEQQAQSSTLVR









NIARPVLEDTPVILPPLPRQ









RQIVELANAMQREEDLLRRL









RQTNQQIMTGLARDLLAG






GO_
GO_
Two-component
H

Up
MAADSLSRHLADRKTPWPHF
183


78
78
system sensor



NQYLVAYLSYLLFYPVPWLL





histidine



GYHRPTLAGVLFSTAAMLVF





kinase



LLVYFAPYRKDRYYGYGEII









LTDLIGYACAWTHGDWEVYC









IFAAGMCARLPGKRQSVTMV









ILLQVVLIISGHFRHKTTLE









VIPGAFFSIITYMGTLVQWQ









LGIRNFELREAQNEIRTLAT









TAERERIARDLHDLLGHSLT









VISVKAELAERLFTSDTSRA









RHEVTEISQIARTSLREVRE









AVSGMNGASLQRELDRARKA









LNTAGITLVLNGPGPSTDQP









QNSVLALALREAVTNVIRHS









DARTCTLTFQHTAEGHIHTF









TLEDDGPLQTTQSAPAIIEG









NGLRGMRARLAASGGTLTVS









PRPQGFKLTATTLP






GO_
hfq
RNA-binding
H

Up
MTSEPSSSAGSRAVQEVFLD
184


175

protein



HLRRTEASVTVFLVNGVKLQ





Hfq



GIVAQSDAHTLLLRRDGHVQ









LVYKHAVSTIMPVAAMSHFV









EEEL






GO_
hisH
Imidazole
H

Up
MRVVVIDYNGGNLASAAQAA
185


159

glycerol



RKAAIRKGIEADVVISRDAS





phosphate



DILNADRLILPGQGAFADCA





synthaseamido



QGLGPELRNMLETATANGTP





transferase



FLGICVGMQLMCEYGLEHGR





subunit (EC



TEGLGWISGNIRRMDEAANA





2.4.2. )



GLRLPHMGWNTLDFTPGAHL









LTDGLTPGNHGYFVHSYALH









DGTDSDLVATAQYGTQVPAI









VARGNRCGTQFHVEKSQDVG









LTILGNFLRWTS






GO_
hpnA
Hopanoid-
H

Up
MNDVTLVTGATGFVGSAVAR
186


2110

associated



VLEERGHRLRLLVRPTSDRS





sugar epimerase



NIAELNAELAVGDLSDPDTL





HpnA



APALKGVKILFHVAADYRLW









VPDPETMMKANVEGTRNLML









AALEAGVEKIIYCSSVAALG









LRSDGVPADETTPVSESQVI









GIYKLSKYRAEQEVLRLVRE









KNLPAIIVNPSTPVGPRDIK









PTPTGQMILDCASGNMPAYV









ETGLNIVHVDDVAEGHALAL









ERGKIGEKYILGGENIMLGD









LFRMVSQIAGVKPPSVKLKQ









SWLYPVALVSEWLARGFGIE









PRVTRETLAMSKKLMFFSSD









KAKKELGYAPRPARDAVTDA









IVWFRQHGRMK






GO_
hpnN
Hopanoid-
H

Up
MSGWGRETLPVLLRVGPMFS
187


2346

associated



DLTGRLNAVCARRAPLVLAL





RND transporter,



FALLCAGCVALSVTRISVTT





HpnN



DTSKMFANTLPWKKRSMELT









RLFPQDSNQLVAIIDSRIPE









QGRMAARQLAATLSQDHTHF









KTVSLPGDNAFYNSHGFLFL









DTKDLEPLLDSIVSAQPFLG









TLAADPSARGLFGALGLIGE









GIKAGQGIPSGFDGALDGFA









NSLTAAANGHPQDMSWQNLL









IGKLAELGSQYEFVVTQPKL









DYSSFQPGEGATTAMRQAIN









NLEFVKTKQASGIITGEVKL









SDEEFSTVAHGMVLGLVISL









VLVAVWLILAVHSPRVIIPI









LLTLISGLLLTTGFAALAVG









ELNLISVAFAILFVGIAVDF









AIQYSVRLRGQRNPDGSHPS









LHDAIILTGQESGAQILVAA









LATAAGFLAFYPTSFIGVAQ









LGLIAGFGMLIAFFCTMTLL









PALLSIFHAKLGNGTPGFAF









MAPADAFLRHKRHKVVGVFA









LLGIVGLALMPLLKFDADPL









HTKDPNTEGMRALHLLEANP









LTTPYSAQVLTPNLTEAARQ









AAAFSKLPSVHDVLWLGALV









PDDQKTKLAMIEDTASILLP









TITIANPAPAPDAAAIRAAA









VTAAQKLDAVKDQLPAPLEK









IRQALHTLSTAQDSTLLQAS









TSLTRFLPDELSMLRTALQP









TPVTMESIPQDVRQDYVLPD









GRARLTIHPKGQMSETPVLH









RFVRELRSVNPDVAGPAMEI









TESANTIVHAFTVAAICALI









MIAIILLVVLRRLLDAALVM









APLLMSALLTVILVVTVPET









LNYANIIALPLLLGVGVSFN









IYFVMNWREGVKGPLTSPTA









RAVLFSALTTATAFGSLARS









GHPGTASMGRLLLMSLGCTL









LCTMVFVPALLPKRPIDEA






GO_
lexA
SOS-response
H

Up
MAFILHLVFRPASAEAHGSA
188


2087

repressor and



CMLTRKQHOLLLYIDDHLRR





protease LexA



TGYSPSFDEMKDALELRSKS





(EC 3.4.21.88)



GIHRLISALEERGFLRRHHH









RARALEVLRLPHMGTEAPVA









TGTGTAFVPAVLNQGQTGLQ









GAFSEDSVANDRQTVSIPLY









GRIAAGLPIEAMQDDSDRID









VPVSLLGTGEHYALTVAGDS









MIEAGILDGDIAIIRRRETA









ENGQIIVALIDEQEVTLKKL









RRRGSMIALEAANRDYETRI









FPAERVHIQGRLVALFRQY






GO_
1ptG
Lipopolysaccharide
H

Up
MNDSTHAMPRHVLIKALNRA
189


1655

export



LLGRFLLCGAVLVSLLEILA





system



LLEKTTPILNRHLGVRGILT





permease



FAFLHLPALSIDILPLAFMV





proteinLptG



GALFLLTQMTLSSEISALRA









AGLSTPALYRLLLPAVLIAG









IGGTCAQYWLVPACENALTT









WWNRTDPLAGQDGQPEDNIL









WFRAGPTLVRIGQIAQGGTF









LRDVTIYHRDSTGLLTGTEH









TNVLTYRDGQWHPDGAQDLS









LSDDKSYVNVTKGDSTFVIP









ATPSVIMTLSQNGATVTPGQ









VSAILHKGAPASLPRATYRM









ALFSGMILPVEIAVMLLLTL









PVIYIPPRAGLRNPLPVYVL









AAGMGFVILQGMISALGNAG









TLPAPLAVSVGPLLGTLLGL









TWLLRMEER






GO_
LuxR
Two-component
H

Up
MRILLVEDDPTVRAFVLKGL
190


3200

transcriptional



REAGHVVDEADNGKDGLFLA





response



VSENYDVVILDRMLPGGIDG





regulator, LuxR



LRILETLRGQKNATPVLLLS





family



ALADVDERVAGLKAGGDDYM









TKPFAFSELLARVEALGRRG









RPESAPQTRLVVGDLEMDLL









SRTVKRGGEKIDLQPREFRL









LEFLIRHAGQVVTRTMLLER









VWDYHFDPQTNVIDVHVSRL









RQKVDKPFDKPMIHTIRNAG









YILRAD






GO_
metR
Transcriptional
H

Up
MSVLQRNHLMIIQEVAREGS
191


581

activator MetR



LTAASARLNLTQPALSHAVR









KIEMQLGVKIWRREGRSLIL









TQAGQWLLSLANRLLPQFSL









AEERLEQFANGERGTLRIGM









ECHPCYQWLLNVVSPYLERW









PKVDVDVRQKFQFGGIGAIL









SNEIDILVTPDPLYKPGLNF









TPVFDYELVLVVGSGHRLYG









VDRVTPEQLADETLITYPVP









SERLDIYTQFLQPAGIAPRQ









QKQIETTDIMLVMVAHGRGV









AALPRWLVDEYASRFDLHSV









RLGENGIAKQIFLGRRETDA









DVQYLTDFIAFAADPKD






GO_
metX
Homoserine O-
H

Up
MRVDQRLIAEMIAPRARVLD
192


1750

acetyltransferase



VGSGDGTLIDYLYRTRSCDA





(EC



RGIEIDMQNVTQSVAHGLPV





2.3.1.31)



MHGDADHDLADYPDDTFDYV









VLQRTLQAVERPREVLRQML









RIGRHAIVSFPNFGHWRLRL









QLLTTGRMPMTPVWNTPWYS









TPNIHPCTIRDFLLLCEEEG









YVIQQWLAIDEDGARAPWRR









SIRLANLFGEQAMFLLKRAG









H






GO_
minC
Septum site-
H

Up
MPDPVSATTSNTPMRIRARG
193


2642

determining



RSFLALVLSPEAPLPLWLEG





protein



LDYQIARSGGLFTGKPVILD





MinC



LGLLSETTPGLATLLDDIRR









RGVRIIGIEGGSRHWSAVAH









WDWPETLDGGRPAGEVEIPE









DPSASAAGPVSGGGTLIIEQ









TVRSGQSIQHMQGDVIILGS









VSSGAEIVAAGSIHVYGTLR









GRAIAGVGGQSQSRIFASRM









LAELLALDGYYAVTEDIDPA









ILGQAAQATLDEDRVRVLPL









TT






GO_
minD
Septum site-
H

Up
MAKVLVVTSGKGGVGKTTST
194


2641

determining



AALGAALAQSGQNVVVVDFD





protein



VGLRNLDLVMGAERRVVFDL





MinD



INVVQGDARLSQALIRDKRC









ETLSILPASQTRDKDALTSE









GVARVMDELREKFDWVICDS









PAGIERGAQLAMYHADMAVI









VTNPEVSSVRDSDRIIGLLD









SKTKKAEQGEKVDKHLLLTR









YDPARAARKEMLSVEDVLEI









LSIPLLGIVPESEDVLKSSN









VGAPVTLAAPTSLPARAYFE









AARRLSGEKLEVSVPVEKRG









FFDWLFKRDA






GO_
mlaD
Phospholipid ABC
H

Up
MQSTLSGRGGAILASGLVLA
195


1943

transporter



IAGTFLVYGNALRKGPDFQG





substrate-



EILHAAFNSANGLHTGANVD





bindingprotein



LAGVPVGRVVSITLDPRTQM





MlaD



ADVAFTVDQRLHLPVDTAVG









IGAPTMTADNALQIQPGHSR









TTLSGEGKITDTRDQLSLEQ









QVSNYIFGGGKLGQ






GO_
mlaE
Phospholipid ABC
H

Up
MNAVLDPIAALGRAALGLIK
196


2354

transporter



QAGALALFALEALSHLVRPP





permease



FYWRIFFSSLIETGFFSLPV





proteinMlaE



VALTALFSGAVIALQSYVGF









GQYHVQSAIAGIVVLAVTRE









LGPVLAGLMVAGRVGAAMSA









QIGTMRVTDQIDALTTLSTN









PMKYLVTPRLLAGTLALPCL









VLVADILGVMGGFTVSVAKL









GFSPSTYITATLDSLKTMDV









VVGLVKAAVFGFLIALLGCY









NGYNSRGGAEGVGSATTAAV









VGASILLLLFDYLLTDLFFS









Q






GO_
mnmE
tRNA-5-
H

Up
MTRSSLPDAPDNTPQVIFAL
197


2236

carboxymethylamino



ATGPSRAAIAIMRASGSGSD





methy1-2-



TILKALCNGRLPEPRRVSLR





thiouridine(34)



TLRHDGEVLDHAVALWLPGP





synthesis protein



NSYTGEDGFELHLHAGPAII





MnmE



ARVADALTDLGARPAEPGEF









TRRAVQKGRLDLLQAEAIAD









LVDAETESQRKQALRQADGA









LSRLYDDWAQRLRLVLAHQE









ALIDFPDEELPQDVEDGLVA









ELSKLQIEMSAHLQDNRGEL









MRQGLTVVIAGAPNVGKSSL









LNALSGTDAAIVTHRAGTTR









DAIALDWVLDGVRLRLIDTA









GLRETEDEIEAEGIRRALFH









VKQADVVLHLIGPNESLESL









SGQEIPVRTKIDIAPTPPGM









LGISTQSGEGLAALRQVLSE









RVAELMAGSAAPPLTRARHR









AGIQEAATHLERARTATWPE









LRGEELRLSMLALGRLTGRV









DVESLLDAIFGQFCIGK






GO_
mnmG
tRNA-5-
H

Up
MVIGGGHAGCEAAAAAARFG
198


2237

carboxymethylamino



ARTLLLTHRLETIGAMSCNP





methyl-2-



AIGGIGKGHLVREIDALDGL





thiouridine(34)



MGKAADRAGIHFKLLNRSKG





synthesis



PAVHGPRAQADRSLYRAAIQ





protein



DLLAATLNLTILEGAAGDLI





MnmG



EENGRITGVICEDGREFRCG









AVVLTTGTFLRGVIHVGHTQ









TEAGRIGEAPAKRLGERLYA









LGLQMGRLKTGTPPRLAKNS









IDWENLPADPGDAEPEAFSP









MTAAITNPQVVCRISHTTAE









THRIINENLHRSAMYGGAIA









GRGPRYCPSIEDKVVRFAER









TSHQVFLEPEALPGNPGGDL









VYPNGISTSLPADVQAAMIA









TMPGLEKARIVTAGYAVEYD









YVDPRELLPSLQLRRLPGLY









LAGQINGTTGYEEAGAQGLL









AGLNAARATAGNEALTLDRS









DAYLGVMIDDLTLHGISEPY









RMFTSRAEYRLTLRADNADL









RLTPKGIAAGCVLSERAAAF









TAQKAELDTAMTRAAETTFL









PQTLRDVGFEVSLDGRRRTV









LDVLASNGDHTKLDTLAPWF









AELPLRVRRHVETEARYGGY









LHRQDREIRQLASESAIALP









ADLDYSAIGGLSSEMRERFS









QARPTSFAAAQRVRGVTPAA









LVALLAHVRTLS






GO_
mntR
Mn-dependent
H

Up
MERKRRLRDIAPKETLPDVE
199


1674

transcriptional



THSEGFRANREARRNVLVED





regulator MntR



YVELISDLLSEGQEARQVDI









AGRLGVSQPTVAKMLARLAT









EGYVTQKPYRGVFLTPAGQD









MADRARHRHRIVEAFLLALG









VSEENARVDAEGVEHYVGSE









TLTLFEKALRGNLKQFMQAL









PDA″






GO_
mrdA
Peptidoglycan
H

Up
MRSGRGVFTRRALLVMAVQA
200


390

D,D-



GVLGVLGRRLYTLQVVDGGH





transpeptidase



LRQLAERNRTSKRLLAPARG





MrdA



TIHDRFGVALADNKVSWRAL





(EC 3.4.16.4)



LMPEETTDIPAVIERFSQIV









PLDEHDRARIERDLRHVHKY









VPVTLHEFLSWDDMARIELN









APSLPGVLVDVGSTRLYPFR









DLTAHIVGYVAPPNEEDVAK









DTTLSLPGMRVGRAGIEQTQ









EAVLRGEPGSVEMEVNAVGR









VIGEIDRVEGQQGEDVRLTL









DSVLQQQVLNRLEDRVASAV









VMDCRNGEVMAMVSTPSFDP









SLFDSGVSHAQWNEWANDPR









TPLVDKAVSGLYPPGSTFKP









AVALAALKSGSVTAQDRFNC









PGYYDLGGVRFHCWNRWGHG









LINMREGLKYSCDVYFYEVA









RRCGMDPIQAVGNAMGLGVK









LGIELPHVRSGVIPTPEWRQ









KHGFHWNGGDTVNAGIGQGF









VQVTPLALATYVSRIASGRD









VQPHLLRATNDQMSAMASVD









DVAKVDLPPEYLDVVRGGMF









AVVNDPHGTAPKARLDLPGI









QMAGKTGSAQVRRVSRALRE









SGHFNSMNLPWEYRPHALFI









CFAPYDNPKYAVSVVVEHGN









AGADEAAPLAKLIMTDTLLR









DPASDVRPPAPSVAQTPSPV









ADGTAPAPTVPVLPDPAPAA









PSEQTDPGAAQ






GO_
mreB
Rod shape-
H

Up
MFSRLLGLMSADMAIDLGTA
201


387

determining



NTLVYVKGRGIVLDEPSVVA





protein



IAEVRGKKQVLAVGNEAKQM





MreB



VGRTPGNITAIRPLRDGVIA









DFEVAEEMIKHFIRKVHNRR









AFASPQIIICVPSGATAVER









RAIQESAESAGARKVMLIEE









PMAAAIGAGLPVTEPSGSMI









VDIGGGTTEVAVISLGGIVY









ARSARVGGDKMDEAIISYIR









KTYNLLVGESSAERIKIELG









SAMMPDDPANPDGPLTEIKG









RDLINGVPREVIVSQAQIAE









SLAEPVMQIVDAVTTALENT









PPELAADIVDKGIVLSGGGA









LLYRLDEVLRLYTGLPVTVA









ENALSCVALGTGRALEEMRR









LRSVLSSMY






GO_
ntrY
Nitrogen
H

Up
MRFPALRRLFARLTSANGAV
202


173

regulation



LLTVMALVLAFATFVVLSGG





protein NtrY



MSLAHRPQVQAIVFLLDFIM





(EC 2.7.3. )



LMLIAAAAVVQIGRMLAERR









LGLAGARLHVRLITLFGIVA









VAPTIVVGAVATLFFHYGVE









IWFSNRVNDALNEARSVAVG









YLQEHNDNARTEAFALANTL









ITVQNDELFSRGTDLFHDPA









RLQEFLDDEVTERGLTDAEV









FDPLTYKVLAVGGLLGSDAD









MTTAPPLPPKSVVELARHGE









AVILDRPDQRRVRAVVALGG









NSGLMLVITRPVDPDVVEHM









RRTDTLVADYQRLITNRGKT









QVLFAVIFALMGLLVLAVGM









LTGLALANRIANPLGLLILA









AQRISKGDLGVRVPVPDDAG









QDKDDEVTGLSRAFNSMTDQ









LESQRSELMQAYDQINERRR









FTETVLAGVSAGVIGLDRMQ









VIELPNRAASSVLQRDLQPA









IGMKLTDRVPEFSGLLEAAR









MAPERVHTAEIQVDTEGAQR









PGGPGEGAGAGAGRTLLVRV









VAELRGQEVAGYVVTFDDIT









DLQSAQRKAAWADVARRVAH









EIKNPLTPIQLAAERLKRRF









LKEIHSDPETYTQLVDTIVR









QVGDIGRMVDEFSAFARMPQ









PVMQPEDFSRLCREALVLQR









NAHPEIVFETTGLPPSGPIV









RCDRRLIGQALTNLLQNAAD









AISMAGRGKPGENASGQPVQ









PIGHIVVGLHIRSGHVLLDI









EDDGIGLPTVERHRLTEPYV









THKAKGTGLGLAIVKKIMED









HSGMLQLTDRAPDQSRGASP









GQRGTRVTLSLPLWEQESHV









PGGTDLQTMRTADGT






GO_
oprB
Outer membrane
H

Up
MPVLASFARTSSRIRSEHLR
203


630

low



SVLMGLFSVSMLSAAVDSAQ





permeability



AQSDPDPNSARHRVSRAAAL





porin,



SSPAPQNSETPANGGSNTPI





OprBfamily



MQNTVSGFAQTEGDPGPYFS









APMGSQHFLGDWGGVQPWLL









KRGIHLMAAINEEFAGNFTG









GKERAYSDAGQFGIELDIDW









DKLAGVRNFWTHTLIVNGHG









QSVSRNFGDSIAGVQQIYGA









RGNVVAHMVAMYGEMSFVHN









RIDVSAGWIPVGSFFAASPL









FCDFMNVAMCGNPAPNKYTE









GNRDWPSGNLGAVVRAMPTM









DTYIMAGLFAVSPHSYNGGI









SGWSWAQSGLGKFSTPVEIG









WTPRFGHNQLQGHYVIGYSY









DNSRYLNLYEDIHGNSWQLT









GQPRRYEAGRNSAWLILDQM









LVRNGPGNTNGLIAMAGAMY









SDGKTVAMRDHEWAGLVDTG









SAWGRPLDTVGAMYQHFDMS









HTAALQQESSLALGLPYQDN









QWGAVYGPQSHENVYELFYS









AHIARAMALQPDFQYIQRPS









ATTTFHDAAVLGVQFTVVL






GO_
pa2737
Transcriptional
H

Up
MTDNSTSQAVMVSPNDDFAS
204


1855

regulator



APEKVRKAPEAYRTISEVAE





PA2737,



ELHIPQHRLRSWETIYPGVK





MerR family



PFRGESGRRYYSPEHIETLR









LISDLLYVQGYKGQGVLRVL









RERRAEKARAAQKAVPETAP









ETVPEVSAVSAEAVHVPLVM









VEATEENPAPVVDATPVTEP









VENEDSPVTLTEASVDDIVF









PEVPAAAHEVVVTETVDSTA









ENESPEAEAEAEAEAEAEAE









AEAEAEAEAEAEAEAPDSAL









LVTLRDENELLENTLEKTEA









ENSLLRSELREILEELRNLR









NLLPV






GO_
pemT
Phosphatidyl
H

Up
MSSTLSPRSALDAEAVKTAY
205


2563

ethanolamine N-



RRWARVYDTVFGGISGYGRK





methyltransferase



RAVAAVNALPGERVLEVGVG





(EC 2.1.1.17)



TGLALPSYSRDKRITGIDLS









EDMLERARIRVLQDHLTNVD









DLLEMDAEATTFEDDSFDIA









VAMFVASVVPHPDRLLAELK









RVVKPGGHILFVNHFLATGG









LRLSVERGMARASRSLGWHP









DFAIESLLPPEDLRRATLTP









VPPAGLFTLVTLPQCESKSD









AAALVA






GO_
plsY
Acyl-
H

Up
MSGFQAQLILLSLISYVIGS
206


2931

phosphate:



IPFGLLLTALGGGGDIRKIG





glycerol-3-



SGNIGATNVLRTGRRGLAAA





phosphateO-



TLLLDALKGAMAVLIARFFF





acyltransferase



PGASETTMAVAAVAVVIGHC





PlsY



FPVWLGFRGGKGVATGLGTI





(EC 2.3.1.n3)



WVLSWPVGLACCVVWLLVAR









LSRISSAGALAAFFIAPVLM









VLLSGRTLHSPIPVATLLVS









LLIWVRHSSNIARLLTGREP









RVNVDPASRR






GO_
pqqB
None (82 bp
H

Up
MIDVIVLGAAAGGGFPQWNS
207


2302

upstream from



AAPGCVAARTRQGAKARTQA





Coenzyme PQQ



SIAVSADGKRWFILNASPDL





synthesis



RQQIIDTPALHHQGSLRGTP





protein B)



IQGVVLTCGEIDAVTGLLTL









REREPFTLMGSDSTLQQLAD









NPIFGALDPEIVPRVPLLLD









EATSLMNKDGIPSGLLLTAF









AVPGKAPLYAEAAGSRPDET









LGLSITDGCKTMLFIPGCAQ









ITAEIVERVAAADLVFFDGT









LWRDDEMIRAGLSPKSGQRM









GHVSVNDAGGPVECFTTCEK









PRKVLIHINNSNPILFEDSP









ERKDVERAGWTVAEDGMTFR









LDTP






GO_
priA
Helicase PriA
H

Up
MASNSLSKPAPWRKPSSAGT
208


1198

essential for



RVSVLVPLPFPGPLDYLAPM





oriC/DnaA-



PLEPGELVTVPLGRRETVGC





independentDNA



VWETDRTLPADFALPVGREV





replication



PLARLRPVAGKLDVRPLPQS









LRRFIDWVAAYTLTPPGLVL









AMATRIHLKDAPRPTLGWVR









TEMPEGDLRITPARRSVLNF









ASSTPMTTAELGSRSGASAA









VIRGLATAGLLREAVIAVAA









PFATPDPSHGAPKLSEEQAE









VAQELCGPVEAGRFQVTLLE









GVTGSGKTEVYFEAVAACLA









KGKQVLVLLPEIALSAQWTD









RFIRRFGAEPAVWHSDLGAK









RRRETWRAVAEGSARVVVGA









RSALFLPFSDLGLVVVDEEH









ESAFKQEEGVMYHGRDMAVV









RARLADAPAILVSATPSLET









LANVESGRYRHELLTARHGG









ATLPDVSLVDMRADPPERGL









FLSPKLCTAIDETLEKGEQA









MLFLNRRGYAPLTLCRACGH









RMQCPNCSAWLVEHRARGIL









TCHHCGHTERIPKDCPECHA









ENSLVPIGPGIERITEEAKL









RFPDAKLLVMSSDTLGSPAA









TAEAVRKISDGEVNLIIGTQ









IVAKGWHFPKLTLVGVVDAD









LGLGGGDLRAAERTVQLLHQ









VAGRAGRAEHRGRVLLQSYV









GEHPVMTALVSNDFQTFMEQ









EAEQRRPSFWPPYGRLAALI









VSAPSAEAADALAREIALSA









PEREGVQVLGPAPAPLAVLR









GRHRRRLLLRTMRGIAVQPI









LRQWLGDIKPTGGAKVDIDI









DPISFL






GO_
proX
Glycine
H

Up
MTQMTIGHLYTSLHAGCASA
209


1638

betaine/L-



VARVLEAYEVEVEYVDLDPD





proline



DIEDALEGAEVDLLVSAWFP





transportsubstrate-



RDEKFAGPGRRVLGDLYQPV





binding



VSFAALLPLAAVGTLTSADV





protein ProX



DRIIVSDDSRQALEDALKQL





(TC 3.A.1.12.1)



PALSVLPIESIGEGALIERL









EKARDAGEKPLVVATQPHAV









FHTDLLTVIEDPAHLLGGEM









SARMIMREDVARQADSDLLD









ELSEMMLGNRVMSALDYVIS









VEGQDPEGAAEAWQRGRLIG









R






GO_
putR
Predicted
H

Up
MSEAEPIFTPVDTKSGSASL
210


548

regulator



EIAEALRRAITNGILTDGQP





PutR for



MRQSELARNFGVSTIPVREA





prolineutilization,



LKQLEAEGLIAFLPHRGAVV





GntR family



TGLSEADILEYSDIRASLES









MAAGLAMTSLTRVDLARIED









AYEAFVSGTGGTHGMEQSGR









LNWEFHGAIYAAAQRPRLYG









MIHDLHSRLDRYIRAHLELP









GRKTATDAEHFQILQACRAR









DGEELGRLTKQHILEAASLS









LDVIRNRTTP






GO_
rarA
Replication-
H

Up
MTDMTDLFGGAPEANRAPGH
211


1388

associated



ASARGPSRAPESMRQQRPIE





recombination



APQVQRRPPSRTQPLADRLR





proteinRarA



PRRLEDVRGQDHLLGPEGTL









TRMLERGTLSSLILWGGPGC









GKTTIARLLAGRAGLFYSQI









SAVFSGVADLRRAFEEADQK









QAATGKGTLLFVDEIHRFNR









AQQDGFLPYVERGTVVLVGA









TTENPSFALNAALLSRCQVL









VLNRLDDASLESLLLHAEEE









VGRPLPLDPEARASLRAMAD









GDGRYLLNMVEQLVALDPSK









VLTPRDLAAILSRRAILYDR









DREEHYNLISALHKSLRGSD









PDAALYWFARMLEGGEDPRY









IARRLTRFAAEDVGQADPSA









LPMAVAGWQTYERLGSPEGE









LALAQVVVHLATAPKSNAVY









TAYKAARALARDTGSLMPPS









HILNAPTSLMKDIGYGKGYE









YDHDSEDAFSGQNYFPDGMP









RASLYHPTDRGHEGRIRKLL









DMRAAKRASREP






GO_
rbfA
Ribosome-
H

Up
MKGPAGVSAHGPSTRQLRVA
212


1471

binding



EEVRRVLAELFARTEFRDPE





factor A



LLDVRITVTEVRISPDFRHA









TAFVTRLGRSDVEVLLPALK









RVAPFLRTGLSKALNLRTVP









EIHFQPDTALDNAMELDEIM









RSPEVQRDLNSKPE






GO_
reck
Regulatory
H

Up
MEDRPAPLPVPDAASLREAA
213


2904

protein



LAHLARFATTEQGLRQVLDR





RecX



RLRRWGVCASRAGLPNEDIE









STIAAVSPAIDGIVASMTDL









GAVDDAGYARNRAVSLTRTG









RSRRAVEAHLANKGVDQNTT









REALNDSLGERSDSSAQEAE









LAAALVLARKRRLGPFQRPD









REEEDPLKALGVFARNGFSR









DVAQSVLDMDSDEAEDRIIA









FRSL






GO_
rfbD
O-antigen
H

Up
MSVSSPASDVARNDAPHRQV
214


635

export



SRDALRGSPAARAWADWKET





system permease



RRLWRLGVRLGWLDIRLRYR





protein RfbD



GSALGPFWLTITSALMVASM









GVLYSKLFHMQLASYLPFLS









LSLTLWSVGFSSLIQESCTC









FLDAEDMVRSVRLPFLLYAV









RVVVRNAIVFAHNIVVPLGV









FALYHLWPGMDALLAIPALL









LWGLDGFAACMLFGSLCARF









RDVAPIIGALLQIVFYVTPV









IWMPQQLGPRAAYLLYNPFY









PLLEIVREPLLGHVPSLQIW









GIALATSAVFWLIAVRSFIR









VRSRLVFWI






GO_
rneE
Ribonuclease
H

Up
MRSDCTVPSTPHNLTFRLAK
215


380

E (EC 3.1.26.12)



AAIVERRGVQFSMTKRMLID









TTHAEETRVVVMDGDRVEDY









DVETSTKKQLKGNIYLAKVI









RVEPSLQAAFVEYGGNRHGF









LAFSEIHPDYFQIPVADREK









LIALQEEEIAERGDAADDGE









TETVSEEATDSEDGENQDRR









APETVGGEHDTGEESASSRR









TARFLRNYKIQEVIRRRQVL









LVQVVKEERGNKGAALTTYI









SLAGRYCVLMPNALRGGGVS









RKITSDSDRRRLRDVIAELD









LPKSMAMIVRTAGAGRPAQE









VTRDCEYLLQLWDDIRSHAL









SSVAPTLVYEEASLIKRVIR









DLYSKDIEDILVDGEAAWKS









AREFMRLLMPSNANKVKLWQ









NRGQSLFARYNVEGHLDAMF









SPTARLPSGGYLVINQTEAL









VAIDVNSGKSTSQRNIEETA









LRTNLEAAEEVGRQLRLRDL









AGLVVIDFIDMESRRHNAQV









EKRLKEALRSDRARIQVGHI









SHFGLLEMSRQRLRPSIAES









VLTPCPHCQGTGFIRGTESS









ALHVLRAIDEEGARQRSSEI









EVHVGSDIALYILNHKRSWL









ADIERHHRMQVIFRTEENLA









AADMRIERLQAQTPAPAQVR









APERAPEHVRTIEIIEEEAP









VVVRTETPVVDAEIIEDVAT









SESEEESNGGRRRRRRRRRG









GRREQNGDVPAAENSQEQDA









PKAETREIAAPEAADENGII









PGRRRTRFKRVVKDTEGSED









TAAQPVSEVRDVAPTRPAAT









TRSSAPAPTRTPRRREDREE









RPAPRRYTGPTPADPFGGSF









DIFDVIEQAELEGTTEALQT









GISTPTEIVIEHVPAAETTI









VVEEPVAEEAPKPRRGRGRR









PARAKAVEAAPAETVAEEAP









AAEAAPAPEEPVAEEPPKPR









RTRTRRTPKAQAVEAEAPAE









PTAEVAASPAETVSEEAVKP









KRTRARRTPKAKPVEAQTTE









EGNILQPVNVDEVAPTKRRA









GWWKR






GO_
rodA
Rod shape-
H

Up
MRRNGMNTFGFLKSDRRLLR
216


391

determining



AEPDFRPMARLLQVNWLYVL





protein



LVCLLAGVGYIALYSAGGGS





RodA



AKPFAGPQMVRFGFGLVMMI









AVSLVSPRILRMASVPIYLL









SVTLLALVLRMGHVGKGAER









WINLAGMQFQPSEFAKIGLV









LMLATWFHRIGNERMGNPLR









LIPPALLTLLPVLLVLKEPN









LGTATIIGVIGATMFFAAGM









RLWQILLLVAPLPFMGKLIY









SHLHDYQKARIDTFLHPEHD









PLGAGYNIIQSKIALGSGGM









WGEGYLHGSQGQLNFLPEKQ









TDFIFTMIGEEWGFVGGIAV









ITLLGTLVMGGMLIAIRSRN









QFGRLLGLGIAMDFFLYCAV









NLSMVMGAIPVGGVPLPLIS









YGGSAMLTMMFGFGLLMSAW









VHRNERDPGEDEDEDD






GO_
slp
SSU ribosomal
H

Up
MDIRSAKGTGIREYSIYMAS
217


1056

protein Slp



ATQTPTANHGTEDFAALLEE









TLGRDTGFDGSVVTGRVVRL









TDEFAIVDVGLKSEGRVSLK









EFGPAGVAPDVKPGDVVELY









VERYEDRDGSIVLSREKARR









EEAWTALERAFANNQRVNGT









IYGRVKGGFTVDLGGAMAFL









PGSQVDIRPVRDVGPLMGQP









QPFQILKMDRARGNIVVSRR









AVLEETRAEQRSELIQGLKE









GMILDGVVKNITDYGAFVDL









GGVDGLLHVTDIAWKRINHP









SEALQIGQPVRVQVIRFNPD









TQRISLGMKQLEADPWENVA









IKYPAGARFTGRVTNITDYG









AFVELEPGVEGLVHVSEMSW









TKKNVHPGKIVATSQEVDVM









VLDVDSAKRRISLGLKQVQR









NPWEQFEEEHKVGSIIEGEI









RNITEFGLFVGLSADIDGMV









HMSDLSWDEPGEAAMAHYEK









GQVVKAKVLDVDPEKERISL









GIKQLQEDPAADTLSRVQKG









AVVTCVVTAVQSNGIEVKVD









DVLTGFIRRAELARDKAEQR









PERFAVGEKVDAKVVSVDRA









SRKLALTIRGREVEEDKQAI









NEYGSSDSGASLGDILGAAI









RRRNTDA






GO_
s21p
SSU ribosomal
H

Up
MQVLVRDNNVDQALKALKKK
218


1844

protein S21p



MQREGVFREMKLRRHFEKPS









EKRAREAAEAVRRARKMERK









RLEREGF






GO_
s9p
SSU ribosomal
H

Up
MSETQERTGTLQDLASVAPA
219


188

protein S9p



VTSNAAPVHEVKRDAQGRSY





(S16e)



ATGRRKDAVARVWIKPGKGD









IIVNGRPVTTYFARPVLRML









LTQPFLIADRYNQFDVYCTV









TGGGLSGQAGAVRHGISRAL









TYYEPSLRGILKAAGFLTRD









SRIVERKKYGRAKARRSFQF









SKR“






GO_
sldB
Broad-
H

Up
MPNTYGSRTLTEWLTLLLGG
220


3173

specificity



VIILVGLYFVIAGGDLAMLG





glycerol



GSVYYVICGILLVAGGVFMV





dehydrogenase



MGRTLGAYLYLGALAYTWVW





(EC 1.1.99.22),



SLWEVGFSPVDLLPRAFGPT





subunit SldB



LLGILVALTIPVLRRMETRR





Gluconate 5-



TLRGAV





dehydrogenase,









smallsubunit










GO_
tolQ
Tol-Pal system
H

Up
MDHEVSSSALGAVGAAGLSP
221


1367

protein TolQ



LDLFLHASIVVKLVMLGLLL









CSAGVWAIIAEKIILIRRVN









REATEFEDRFWSGGSLDDLY









ESDGARPTHPMAAVFGAAMG









EWRRSARIGGIDLSRGGVRE









RVDRAIDITIMRENDRLTRR









LIFLATIGPVAPFVGLFGTV









WGIMHSFASIAQMHNTNLSV









VAPGISEALFATAIGLVTAI









PAYIAYNGLSNSFEKFADRM









EAFGTEFAAILSRQSEERAD









DTTGGKA






GO_
tolR
Tol biopolymer
H

Up
MGMSAGGRAGGGGRRKRRPA
222


1366

transport system,



SEINVTPLVDVMLVLLIIFM





TolR protein



VTAPMLTSGVNVDLPKTDAS









PVNSDTKPITVSLRTDGSLY









LGDQQVTSDQLIDQLKAQSQ









NDPTHRIFVRADAHIDYGQV









MQVMGQITSGGFTHVALLAQ









QPQSGQ






GO_
trxa
Thioredoxin
H

Up
MSANTVAVSDSSFEADVLKS
223


1087





EGPVLVDFWAEWCGPCKMIA









PALEEIGAEYQGRLKVAKVN









IDSNPEAPTKYGVRSIPTLI









VFKDGKPVAQQMGALPKSQL









KAWIDQSL






GO_
uvrD/
ATP-dependent DNA
H

Up
MPQDLPSPTPEYLSRLNPEQ
224


2012
pcrA
helicase UvrD/PcrA



RRAIETTEGPLLILAGAGTG





(EC 3.6.4.12)



KTRVLTTRFAHILLTGRAYP









SQILAVTFTNKAAREMRERV









SAILGEPAEGLWLGTFHAIC









ARMLRRHAEYVGLTSSFNIL









DTDDQIRLLKQVMEPWKIDT









KRWPPNQLMGIIQRWKDRGL









TPDRVTPVEDSDFANGHALA









IYRAYQERLIALNTCDFGDL









MLHMTEILRNQPNVLAQYHR









IFRYILVDEYQDTNTVQYLW









LRLLAKREHGPSNIACVGDD









DQSIYSWRGAEVENILRFEK









DFPGAEVVRLERNYRSTAQI









LAAAAGLIAHNEGRLGKTLR









PGRDDAQGEKVQIIGVRDSD









EEARIVGGAIERLRGDGHPL









SEIAILMRAGFQTRPFEERL









MMIGIPYRVVGGLRFYERSE









IRDCLAYLRVLSQPADDLAF









ERIINVPKRGVGAVAVQKLH









AQARALPGPLTAAVIWQLQE









GLLKGKSKEALDGLMAAFQR









AKATLETEGHVVAAEQLLED









SGYLQMWRDDRSVEAPGRLD









NIRELLRALGEFGTLQGFLE









HVALVMDTESETSDDKVSLM









TLHGAKGLEFDTVFLPGWEE









GVFPSQRSLDEGGNRALEEE









RRLAYVGLTRARRRAIVLHA









ASRRIYANWQSSMPSRFIEE









IPSEYVQLTGQAFETRRQAA









AAPSMFASGPLTSTRPSGFR









APRPKIHDVKPEPTVAIGAT









VFHHRFGEGTVIGADGPQLH









INFENGGVKRVMANFVEIRS






GO_
ybbN
FIG000875:
H

Up
MSSTFDEHLIGQSSGKAPAG
225


3271

Thioredoxin



AAATIIDADQTTFMADVVEA





domain-



SREIPVLVDFWAPWCGPCKQ





containing



FTPVLEKVVHAAGGRIRLVK





proteinEC-



VDVEANQALAAQLGQLGLPL





YbbN



QSIPLVVAFWKGQVLDLFQG









AQPESEVRRFVESLLKLAGD









VMPATEILAAARQALADGHA









DQAAGLFSQLLEAEPENPEA









WGGMIRALIALNEPEAAQDA









SAQVPAKLDSHPEITGARAA









LALHAEGAKAASELETLRQQ









SAAAPDDFDLRVRLAAALNG









AGERAEAANTLLDILRKDRN









WNEGAAKTELLRFFEAWGHT









DPDTLAARRKLSSLLFS






GO_
ycaR
FIG002473:
H

Up
MTTELDPRLLSLLVCPVTKG
226


3269

Protein



PLTYDRETQELISPRAKLAF





YcaR in KDO2-



PIRDGIPIMLPEEARQIDA





Lipid









Abiosynthesis









cluster










GO_
ftsJ
23S rRNA
H

Up
MKPPRSRSGSSKDTGPKRIP
227


2100

(uridine(2552)-



GKALKSASNPGENDATLDSA





2′-O)-



TARTARNKTVSLRTARGRTT





methyltransferase



AQQRWLNRQLNDPYVAAARK





(EC



QGWRSRAAFKLIEIDDRFKL





2.1.1.166)



IGEGTRIIDLGAAPGGWTQV









AVKRGAQHVVGLDLLPVDPV









AGAEIIEGDFTDPEMPDRLK









DMLGGPADLVMSDMAPNTTG









HAATDHMRIMGLAEGALDFA









FQVLAEGGSFIAKVFQGGSE









KDMLALMKTAFSSVKHVKPP









ASRKESSELYVIATGFRPER









LPEGGKGA






GO_
GO_
Alkyl
H

Up
MVRINSPLKPFSTDAFRNGE
228


47
47
hydroperoxide



FLTVTDSDVRGKWSVFFFYP





reductase



ADFTFVCPTELEDLADNQAA





protein C



FDKLGVEIYSVSTDKHFTHK





(EC 1.11.1.15)



AWHDTSPAIGKIKYTMLGDP









TGAIARNFDVLIEEAGLADR









GTFLIDPEGKIQYIEITAGG









VGRSATELLEKIQAAQYVAT









HPGEVCPAKWKEGGETLKPS









LDLVGKI






GO_
g6pd
Glucose-6-
H

Up
MEHFQQVEPFDYVIFGATGD
229


1805

phosphate



LTMRKLLPALYNRLRMGQIP





1-dehydrogenase



DDACIIGAARTELDREAYVA





(EC 1.1.1.49)



RARDALERFLPSDILSPGLV









ERFLARLDYVTLDSSREGPQ









WDALKSLLAKAQPDRVRVYY









FATAPQLYGSICENLNHYGL









ITPTSRVVLEKPIGTNMATA









TAINDGVGQYFPEKQIYRID









HYLGKETVQNVLALRFANPL









MNAAWSGEHIESVQITAVET









VGVESRAAYYDTSGALRDMI









QNHLLQVLCLVAMEAPDSLE









ADAVRNAKLAVLNALRPITD









ATAATETVRAQYTAGVVDGE









NVPGYLEELGKPSTTETYAA









IRAWVDTPRWKNVPFYIRTA









KRSGKKVSEIVITFRPAATT









MFGASPASNRLVLRIQPNEG









VDLRLNVKNPALDVFNLRPA









DLDTSIRMEGGLPFPDSYER









LLLDAVRGDPVLFIRRDEVE









AAWRWAEPILDAWKNDKAPM









QTYSAGSYGPEQATQLLASH









GDTWHEASE






GO_
GO_
Membrane
H

Up
MTDLHDTLLTLDSHIDIPWP
230


2091
2091
dipeptidase



DRQDAWVEETPRQVNVPKTR





(EC: 3.4.13.19)



KGGLRAVCLAAYIPQGPRDE









AGHAEGWERVQGMLDVIAGL









EGRQGDQGARVCRTAADVRA









AYKAGELAVIPAIENGHGLG









GRPERIAELARRYGVRYMTL









THNGHNALADAAIPRKDLAD









NETLHGGLSDLGRETIAKMN









RSGVLVDVSHAAKSTMMQAT









EVSITPVFASHSCARALCDH









PRNLDDEQLDRLKETGGLIQ









VTAMGSFLKKGGGGTVEDLV









RHVSYIADRIGVEHVGISSD









FDGGGGIPGWKDATETANVT









QALQAAGFSDTDISSIWGGN









MLRLLETAERAAEKV






GO_
GO_
Multimodular
H

Up
MTRRSFRSRNPQGSGNPQGP
231


2951
2951
transpeptidase-



GAPPPRPPRFRRYRQSLAII





transglycosylase



AGVGLVGIAGAGVLGWTTYA





(EC 2.4.1.129) (EC



KLVADLPSVDSLRAYQPPTV





3.4.—.—)



SRIYASDDRLMAELANERRI









FVPINAIPERVKNAFIATED









HNFYTHGGVDFMAIGRAGLT









DIFARHGRRPLGASTITQQV









AKVMLLNSNVLSFDRKIKEA









LLAMKMEQVLSKDKILEIYL









NGIYLGNGAYGVAAAAQSYF









NKPLDQLDDAEAASLAALPK









SPTNYNPFLHPQAAMARRNL









VLDLMVEAGVLTRQQADQEK









QEPLVPQQKQRFGPLPDSEW









FGEEVRRQLIAQYGQERAAQ









GGLEVHTSLDQSLQVTETRL









LHEGLMNYDRVHSGWRGPLR









NLPDIQDDGWESALDHITPP









GGMLREWRLAVVLPGATHVG









WIEEGTARKGALLATDMAWA









RRMRPLRAGDVIMIEPQEGG









SAALRQIPQVEGAAVTLDVH









TGRVLAMVGGWSFHESQFNR









VTQALRQPGSSFKPFVYLAA









MEKGISPSERFDDSPVSYGD









WHPQNYEHDNWGPTTLHDAL









RESRNLVTIRVAAHLGMKAV









ADTAIRAGLVAQMPHVLPAA









LGAVETTVMREAAAYATIAN









GGHIVTPTLVDDIQDRAGTV









LWQAGGLTLGTAMQAPPAEQ









PVPADGTTTSAAPATAPVAP









SATPTTPPPGSVAVPALTDG









RPVLASEQSTFQIVKMMQDV









IARGTGRMAGVGIDRPIAGK









TGTSQDFHDAWFAGFSPDIV









TVVWVGFDTPQTLGRNSDGG









RVAGPIWNRIMKVALANRPK









LDFRVPDGITLASYDTGRIS









AVDGFKTDQVPGASVELHGF









GAGTEALTAADTGADSVISD









SESDMAQTPGQGGGMAGAAP









GSGTAAAPGQAQKPAPSDGD









IGVGGLY







GO_
Prephenate
H

Up
MTPLFRSLAVIGPGLIGSSV
232



2112GO_
dehydrogenase



LRRARETGAIAETLIAADSN




2112
(EC



PGVLERVRELGIADITTSDP





1.3.1.12)



AVAAQADCVMICVPVGAVEP









VARQVLPFMKPGSILTDVAS









VRGQLGPTLAAILPENVAYV









PGHPMAGTEHSGPDAGFSTL









FEDRWALLVPPEGADPKAVT









TIGQLWTLCGARTKILSDEK









HDRICAMVSHLPHLLAFTIC









DTADNLSDEIRAAVLDYAAS









GFRDFTRIAASDPVMWRDIF









LANKEALLGTLDKFVADTQA









MADAIRTGDEATITSKIERG









RAIRRTLIENRQA







GO_
Pyrroline-5-
H

Up
MPSVPSVLLAGCGKMGGALL
233



2168GO_
carboxylate



DGWLASPTPPRLVILDRHRT




2168
reductase



GTDDAITVVRTAAEIPAGFK





(EC 1.5.1.2)



PDVIVLAVKPATAEIMIDAI









GKALGPRMSNAAILSVMAGR









TCAALSEAAQLAGADMPVLR









AMPNTPSAVGAGISGLYASP









SATPEQKSICHDLLFAVGDV









VPVEKEADLSIVTAISGSGP









AYVFLLAELLEKAGQQHGLS









PTIARRLARGTIYGAGRMLD









DLPDSAEDLRKAVTSPNGTT









AAALAVLMKSDAWPETVPKA









IDAATKRADELAG






GO_
GO_
Ribonuclease
H

Up
MKLSHTEALASMQAALGHDF
234


2617
2617
III (EC



KKPELLSEALTHRSAVSGRD





3.1.26.3)



PRRARRNQRPKGSGSNERLE









FIGDRVLGLLMAEWLLERYP









DEQEGALGPRHAHLVSRTVL









AEIADQVGLSASLQISPHEE









DAGIRRLSSIRADAMEALLG









ALYLDGGLEPARRVVRQYWQ









SRIESADRPHKEPKTLLQEY









MLSQGLPLPHYELLSSDGPS









HAPVFRVSVTTMGHTGTGEA









GSKRLAESAAATALLKHLGO









NVAS






GO_
GO_
Sugar phosphate
H

Up
MRDFTHDHSALALNTATLGH
235


493
493
isomerases/



NMLGAGAGWSAERTIDACAE





epimerase



RGIGGIVFWRPELQGRASAI









GQHARQVGVEVVGLCRSPFL









VGPLAPHGRQAVVDDFRRSI









DETADLGGKILTIVVGGVEP









GTKGVRESLDIVTDRLSEVL









DYASERDVKLALEPLHPMYG









GDRSCLPTVRDALDICDALN









SDTLGVAVDVYHVWWDTDLP









RQLERAGTRIMGFHLCDWLV









PTTDFLLDRGMMGDGVADLK









GLRAGVERAGYDGFCEVEIF









SANNWWKRDPAEVLDVIIQR









FRDIC






GO_
GO_
TonB-dependent
H

Up
MTTSVQHSLKRRTPAPRTVI
236


2343
2343
outer membrane



RMFLMAGISYSVLPSFGAHA





receptor



QTTDATKHAAVHKTAAKKKT









AAKQQVMPAAKNTPATTPVA









AAAPAAKPATTTSVQTSNRT









TLTTDPTPVAETVTVTGTRL









SQTRLTNVMAGTTVDAEQLR









ARGYTDLGLALLRENTAFTV









GDNSPIGSQGSFGAGQSFIA









LLGLGSQRTLTLIDGMRMVG









GSTASNYGAGSGSQVDVSTI









PTSLIKKIDTKLGGAGAAYG









ADAVAGVVNYQLDDHFKGVD









FNAQGNWTQKLDAPQEKITF









KAGTSFDHDKGGVVFDVEYR









NSGGMVANDRRYLTGDQATT









YARAPVGSTSPYSYVLTPAV









RFLQNSVTGVPMTSAAYGSL









PLTYGQASQYGIANASGAGL









MFSQDGKSLVPITTNAALKD









GLRGSGGNGLALTDYNQLYA









PSSKLNLTTLGHYDFTDHLH









ATWQGWYARGTASSLTAQGT









WNTPQFDDPLSAESYQQDTV









VNGAYTLSTSNPYLTSAERT









AIKSALAAAGQSTDTFYLSR









LNQDLDAGNYTTTVQMFRFQ









GGLNGDFDAVGRHFDWSVKG









EYSKYMSDTWEPMIDTQNLV









NALNATTDASGNIICTPGYT









NSTAKTRSSTCSPLDPFGYD









QMTLGAKNYITADAHSKESN









VQRDIQAEIHSTVFRLPAGD









IRWDLGYEHRREGYDFNPGS









FMEGEEQADGTYKQYGNFTS









IPYTGGAYHTHEVFGELDVP









FVSPSMHIPGIYNLSATANG









RYINNSVTGSYWTYMFGGAW









WPTQDFGLSGNYAQSVRNPS









VTELYSPTSTSYETANDPCS









VEYISSGPNPATRAANCAKG









GMAGGFESNINYYTLPGTTG









GNRNLKNEVSKSFTGNLEIR









PRFMKGFDFTGSFVDVKVNN









EITSLDASDLMAACYDSTSY









PSNAYCNAFTRDPSTHQVTS









FTDGYFNIANQHMQVLQAKL









DYYIPLRRFGLPSSAGNLEL









QGNYTHYVKNQQTYLGSTYL









LTGSTTSPNNLFTLDLNYTR









GPLFVQWQTVYYGKSKYALQ









VSDYTYQHNNRPDFAYFNTT









IGYKITKNFDVNFMMNNITN









ALPKYPGTVSLTRYYEAIMG









RSFQMNLGAHF






GO_
GO_
Tryptophan
H

Up
MSRIQTRFAALKKEGRGALI
237


2864
2864
synthase



PYLQACDPDYDTSLELLRAM





alpha chain (EC



PAAGADLIEIGVPFSDPSAD





4.2.1.20)



GPTIQAAALRGLKAGATLGC









VLEMVRAFRETDNETPIVLM









GYLNPIDSYGPAEFCFDAAQ









AGVDGIIVVDMPTEEADLLD









AHAREAGLDIISLVAPTTSN









SRLFHVLRDASGFVYYVSIT









GITGTNSASAADLEKALPRI









REATSLPVAVGFGISTPEQA









RTASRIGDAAVVASALIKTM









AGTLDDGRATERTVPAVLKQ









LEGLAAAVRA






GO_
GO_
Two-component
H

Up
MVPNLSDPDLPARILVVEDD
238


3253
3253
transcriptional



AGMRTLILRALQGGGFRARG





responseregulator,



VACGDEMWAALEVAPVDLII





LuxR family



MDIMLPGKSGIELCRALRSG









QGATHENETPPAQVPIIMVS









ARGEERDRVNGLESGADDYV









PKPFGQRELLARVRAVLRRG









IATGAPQERVRRETLRFAGW









TLDLRRRELTDPSGATVDIS









GAEHDLLTSFLDNPQRVIAR









DRLLELSRTRLGDVSDRSID









VLVSRLRRKLGSDADQLIRT









VRGLGYIFVAEVERV






GO_
GO_
Fructose-
L
F
Down
MSTAETMMSQMAEKGGFIAA
239


1509
1509
bisphosphate



LDQSGGSTPGALKQYGIPES





aldolase



DYSGESEMFARMHEMRVRII





class I



TAPSFTGDKVIGAILFERTM





(EC 4.1.2.13)



DGDVKGEPVPAYLWRERGVV









PFVKIDKGLEAEADGVQLMK









PMPGLDDLLERAVKLGVYGT









KERSTIRLPSESGIRAIVQQ









QFAVAEQVRRHGLVPILEPE









VLIKSPDKKACEQLLHDYVL









EELQKLPEDARIMLKVTIPE









VPDLYDDITRDPRMVRVVAL









SGGYPLDQACEKLRHNHRMI









ASFSRALIGDLRHQMDEAQF









DATLGKTIDEIYDASVHKV






GO_
GO_
Transport-
L
F
Down
MSGSTISSGQPTPDNTTTRP
240


1829
1829
related



APLRPRARPFLSWLYAPSPS





membrane protein



SVTFALRNTIAACLAVGIAF









WMELDDPAWAAMTVWAVAQT









SRGESQSKAKWRIVGTISGA









IAAITIMAAAPQAPWMFFPM









IALWIGLCSGFATFVSNFRS









YALVLAGYTCSIICMGAASN









PDNVFMVAMSRGTYIVLGVL









CEAFMGLIFATSQERHARAQ









LRQKLESALVLVTTTLCSLL









GEERGALNAARRQFGTILTI









NDQIEFAEVEMGPHGHEGDH









ARAALAAVSALLSRGFGMAM









RLQVLNHNHPAFTKTADEIL









AFLKQFPQRLPDQNAVPALL









ADLQHFRDICRLYAAPHRES









DIRPDLEPIPGLEPFDQTDE









GQGMRADRLDERILFVSLGE









LLGDLEQAIKEYEASTHRIK









GDHFHFQLETHRDTREAVHN









GLRGACAVLITAYIYEVTAW









PNGLGFIAITTLVCGLFATK









ENPVLGTTEFLKGAVAAYFM









AWILVFVLMPKVTTFETLAL









FLGPAMFLGGLAKGNPATAG









GSAAYGLLLPAMLGLENHHV









MNEIAFYNGNMATVLAVAVS









VIVFRSVLPFSSDAERFRLR









RIMLGELQRLAHPGFTPRIS









VWIGRNTDRFARLIRHAGPT









PAPLIEACILGTLATLTLGL









NVIRLRTLLDREYLPESARR









PILLVLHYVEQSTKRHDKAA









RIAEAAVRRLRVLDAQETDL









VTRLELTRAITYLVVIAYTM









RTNEDFLDASKPFRGERNSR









LLNSGQG






GO_
LepA
None (6 bp
L
F
Down
MTDTPLSLIRNFSIIAHIDH
241


2805

upstream



GKSTLADRLIQACGALTARE





from Translation



MKNQVLDSMELEQERGITIK





elongation factor



AQTVRLTYPAKDGKVYTLNL





LepA)



MDTPGHVDFAYEVSRSLAAC









EGSLLVVDASQGVEAQTLAN









VYQALDANHEIVPVLNKIDL









PAAEPERVRAQIEDVVGIPA









DDAVEISAKTGINIEGVLEA









LVQRLPAPTGDAEAPLQALL









VDSWYDAYLGVIILVRIKDG









RLKRGDRIRMMQTGATYHVD









QVGVFLPKMQSVESLGPGEM









GYINAAIKTVADCNVGDTVT









LDKRPAEKALPGFKPSIPVV









WCGLFPIDADDFEKLRDSLG









KLRLNDASFHFEAETSAALG









FGFRCGFLGLLHLEIIQERL









SREFNLDLIATAPSVVYKMH









MTDGTSEDLHNPADMPELSK









IETIEEPWIKATIMVQDEYL









GPVLTLCSERRGIQVDLTYV









GNRAMAVYRLPLNEVVFDFY









DRLKSISRGYASFDYQMDGY









EESDLVRISILVNHEPVDAL









SFISHRTVAEQRGRSICAKL









KDLIPKQLFKIAIQAAIGSK









VIARETIGALSKDVTAKCYG









GDISRKRKLLDKQKEGKKRM









RQFGKVEIPQSAFLAALKMD






GO_
GO_
Fructose-
L
F
Down
MSRVSPGVVSGASYTALIRA
242


3252
3252
bisphosphate



CHEGGYALPAINVVGTDSVN





aldolase



AVLEAAARNGSDVIIQVSNG





class II



GARFYAGEGLPDAHRARVLG





(EC 4.1.2.13)



AASMARHVHLLAKEYGIAVI









LHTDHADRKLIPWLDDLITM









SEDEFKATGKPLFTSHMLDL









STEPLEENLATSASMLKRLA









PLGMGLEIELGVTGGEEDGI









GHDLEEGADNAHLYTQPEDV









LKAWELLSPIGTVSIAASFG









NVHGVYKPGNVQLRPEILKN









SQEAVQKATQSGPKPLPLVF









HGGSGSTIAEIDAAVSYGVF









KMNLDTDIQFAFAHGVGSYV









LEHPVAFQHQIDPGTDKPMK









SLYDPRKWLRVGEKSIVERL









DEAFEILGSKGRSVARKS






GO_
GO_
Transcriptional
L
F
Down
MSQTIVPHTLPLKNVHVPAR
243


1025
acrR
regulator, AcrR



DRTATRAPGRPVNLRLKDNI





family



LAAIAQVLVEEGYQGLTISR









VAKAAGVSTATVYRRWPTKQ









AMFFDAMRLWRDDLTPQIDT









GSFAGDVDELIAARIRFLVT









PLGRTYGTLLGEAVHDPEFG









QVLWEVSVVPARAQMTLFLE









RASRRGEKVFCQNPDTVLDM









LLSTIHFRAMNLLGREPMDA









DSTLKEIRSLARSLIAG






GO_
GO_
MBL-fold
L
S
Both
MHDAAVQAATGQIRRTEEGT
244


1035
1035
metallo-



APAPVVCTFFDEATNTASHV





hydrolase



VHCPVTKRAAVIDSVLDYDA





superfamily



AAGRTSHGSAQAIVDYVERE









GLTVDWQLETHAHADHLSAA









PWLQEKIGGKLGIGADITRV









QAVFGKIFNAGTRFARDGSQ









FDHLFTDGETFRIGDLPVTV









LHVPGHTPADMAFVIGNAAF









VGDTIFMPDFGTARADFPGG









DPRQLFRSIRRLLSLPVETR









LFLCHDYKAPGRDEYAWLTT









VGHERDYNIHVHDGVSEEEF









VKMRTERDATLAMPRLLMPS









VQVNMRGGHLPEPEADGVSY









IKIPVNRV






GO_
lipB
Octanoate-[acy1-
L
S
Both
MPKTRAMTRNEIYEEILWKS
245


1921

carrier-protein]-



SPGLTAYPEALTFMEERARA





protein-N-



IHQGTAAPLVWLVEHPPVFT





octanoy



AGTSARDTDLYNPHGYPTYS





ltransferase



AGRGGQWTYHGPGQRLGYVM





EC 2.3.1.181)



MDLTKPNGTVPPRDLRAFVA









GLEGWMTGALAQLGVTAFTR









EGRIGVWTIDPLTGLEAKIG









ALGIRVSRWVSWHGVSINVS









PDLTDFDGIVPCGIREFGVT









SLQRFDSSLTMADLDDALAA









AWPGRFGSIPRAA






GO_
elf-2B
Nucleoside-
L

Down
MIVIPMAGLSSRFTKAGYTK
246


1731

diphosphate-sugar



PKYMLPLAGKSVFAHSIESF





pyrophosphorylase



SAYFGLIPFVFIARPVADTE





involved in



AFIRKETAKLGIKDVRIIIL





lipopolysaccharide



DHETAGQAETVELGVRKAGL





biosynthesis



GLETPLTIFNIDTFRKNFRF





/translation



PDEPWFKKSDGYLEVFKGEG





initiation



ANWSYVGPEENSNEPLVART





factor



TEKKPISDLCCDGLYHFAHT





2B, gamma/epsilon



RDFLDALTQERLTPSASELY





subunits(eIF-



IAPLYNYLIKAGRKIHYNLL





2Bgamma/eIF-



PADMITFCGVPAEYTALLNA





2Bepsilon)



IED






GO_
GO_
Transcriptional
L

Down
MTTDAEQDGPLRQRKKDRTH
247


1683
1683
regulator, AcrR



AALVREAMRLFSTHGYEETS





family



VDEIAEAAQISRRTLFRYFP









GKADIILAWTGSVTTILTEA









IRDVPLDVPLQDAVLAGLVP









VVACYSSDRMDAYAVVRLVE









RTPALRDMALRRYSEWEETL









ASALIARLPATEMPSLVARL









LARTAIATFRTALDEWMKTE









GKSDLEAILRQTFTLQPLLW









QDDFPLSSG






GO_
bamE
Outer membrane
L

Down
MNNASSPTPQSRTRLLRRFA
248


1849

beta-



QAGVACVPLLLGGCSFFSPI





barrel assembly



PEPRGSLIEKTDYAQLVPGT





protein BamE



STRTDVLDLLGSPTAHATFD









DNTWIYVSMITSPTPLTFPS









VKKQQVVVLNFDNGGVLRKM









DTLNKKNAMYVGMVGAKTPT









PGTSSSILQELLGNVGRYNP









MSGMSSQFGGSTGPMGGQGT









GNGGAGNTLP






GO_
envZ
Osmolarity
L

Down
MRERDDAWQKLDRPLRRILP
249


1848

sensor



RSLMGRSMLIVLIPLLVTQA





protein EnvZ (EC



IALGLFYGTYLNVVSRRLSD





2.7.3. )



GVTGEVSLVIAMIEHTSSEA









ERTLVLQDASSRTQLGFSFQ









PGETLSRYGTNHVLGPMDDD









FARSIRQNLGRPYDVDWSES









PQTVRASIQLPQGVMVVMVP









VKRLNIGPIWLFVVWAVSSS









IVLFLIAGLFMRNQVRAIRR









LGHAAELFGMGRDQGPIRPQ









GAREVRQAAIAFNRMQARVN









RFVAQRTAVLAGVSHDLRTP









LTRLRLTVAMFPTFGPIRAE









TLKPDLADMVADIEDMERLI









GSYLSFARGEGAEEPVLTDL









RGMLDDVAAATVRAGGQVLG









VEGREGVEATVRPDALRRVL









TNLAENARRHGGAMRFSLRE









GERNVEITVEDNGPGLSASR









RAAISELNGTTASQDGNSGL









GLTIVRDIIHAHGGSIRLVE









SPLGGLGVVLSLPK






GO_
ggt1
Gamma-
L

Down
MAHRQHQISTPDATQARRVS
250


1517

glutamyl



SRLPASLMASVASGLLLGAC





transpeptidase (EC



SWIPGSHLVGISETSAPAGG





2.3.2.2)



SIGTVVADEPQAALVGHDVL





Glutathione



ARGGNAADAATATALALGVT





hydrolase (EC



LPSRASFGGGGACLVSRPGE





3.4.19.13)



VAQSIAFQPRAGTSKGADRP









AATPADFRGLYLMQLHYGTV









DFNDLIAPALNLASTGITVS









RTLAADLAAVRPALLADDSA









RAIFGRGDASTLVAGDSLAQ









PRLAGFLERIRVAGVGDLYN









GALADVYVTAAQKAGGGLND









DDMRQTLPLQTEALITRQGG









VDASFLAPPADGGLGAAVRY









TTGASAQGTVAAWRASGNTS









LAAAQAALNSGRSGGGSLPA









LPASTSFVVTDHSGMAVACV









LSDNNLFGTGRIAGSTGVVL









GASPAHTPQPLLSAAVLRDQ









RNLRAVIAASGQNEAADAVG









DAARAAAHETPIPHEGAGRI









NAILCHGNDSCRGSTDPRAA









GLAAGTTNDSRN






GO_
GO_
Putative outer
L

Down
MLNDNLPHFDGRHYRNPEAW
251


1348
1348
membrane



RPDETRTARTTSQRIGNIFR





protein



WQMGLRPRWPDALPPQKSWP









QVTPAPGECCVTFIGHATVL









LQFGRTGRAPLRIITDPVFS









ERCSPFRSFGPRRVRPPGIP









LDALPRIDIILVSHCHYDHL









DLPSLRALAERDDPLCLSLP









GNRRHLEKADLPRIAELDWW









ESTTDDGARITATPALHGSA









RTPFDSNRALWGGFTIEADG









HTVFFAGDTAWGKHFDAIHR









RWPDINLAILPIGAYDPRDL









MRRVHMSPEEALMAFDTLRA









KQGLPIHFGTFQLTDEAILE









PPTRLEFASRPGSRPFAALE









NGESLTLPPADTKS






GO_
GO_
hypothetical
L

Down
MGIAGASCVLDVMINDRSAL
252


1415
1415
protein



VRDSAAFIVLLERIWKARDV









EASLVWSELDERIRLADELR









ASGIRPYKGGRFRSTKLP






GO_
GO_
Glycosyl
L

Down
MQHPVLTILPPRERYEEGHA
253


1438
1438
transferase,



GAISLLVSREAQFSDVVAGM





group 1



GRIGTPLPGGQYRPLILPRV









PLLRNWRLRLACVAMMRFCR









PALTEIHNRPDLARFLARFG









PVRLILHNDPCTMRGARSPR









QREDLARHVLVCGVSEWVTG









RFCEGCGPIRTEVQPNCIDL









SVLPTVGLRQKIVLFAGRVV









ADKGVDAFVRAWGAIRAQYP









GWRAVIMGADRFGPDSPETP









FLEKLRPQAAAVGIMMTGYR









PHDDVLEAMAGAAVVVVPSR









WEEPFGMTALEAMGCGAAVV









ASPVGALPDLVGDAALLAAP









DEAGALEQALSRLMGDEGLR









TRLGERGRERAALFDVAAAR









VRQEELRRAAIAFARRPPRL






GO_
GO_
Two-component
L

Down
MHIVPRSLVARTSLLLIVGL
254


1455
1455
system sensor



AVVEAAGLGIHALDRFDLEE





histidine



RSQVHEEQVQVFSIYRTVAE





kinase



AKPADRHDAIDDLHVPSNVT









VLLLKEPDPLIEGHEIPFPA









MTSPSFLHRLHEDPQGHEGF









LPPGPMDPGGPHPGPDMGGP









GFPGAGPGPMGPMGGGPGGP









EFHFPADHADGERADAEHLN









GDPRFPGAIRRRDMPPFMRW









ALLPSSLYPRKVLIGQKMRT









HSTSILLPDRDCWLVVRFVT









PLPNPFGSPTFMIAFLVMSI









AGSAMIVWATQRLIAPVTTL









ANAAEALGRDVHTAALPENG









PSEIRRAAIAFNTMAMRIRR









FVTDRTLMLTAIGHDLRTPI









TRLKLRAEFIDDEELRNKVL









ADLDEMESMVSATLAFGRDS









ASAEPIVSLDLRALLQTIMD









EAAESVPDKADDLFYEPPNV









PVRIKARSVALKRALNNLIL









NALKYGGSAHVTLIPATNPG









EKDNVVKILIEDNGPGLPES









ELDRVFEPFVRIESSRNRET









GGSGLGLSIARTILHGQGGN









VRLENRPSGGLRVIVTLAP






GO_
GO_
hypothetical
L

Down
MPPRDRRTRPTVDRRRALVG
255


1728
1728
protein



LGLAAPFLASRSIAAEKSVP









CLRIDEVELRRFGAALDGIT









DDLHVLQACIDSSGVNTPDV









PCPSILFDFPAVTVCLSGPI









VTGGRNITLRGAGQDLTVLI









MKTGASGILTHGTSEYPAEG









YLQLQDIGFDDGNIKGSGCT









GISVHFAPGAPQAAMTWQGV









ALRKWSQAATITNCPRNWHC









ENVTVFGPDFTMQDDAGFRI









ISEPHFAQGCFTYVFINVLV









ANYSWGWDYSISAPLEGQRF









YSCTCYNGWGMVRSRVHATP









DQQSGIDETYRSVIWYFMEC









DWQGFGYALDLVHCRNIIVR









GGFYIANRNVDHLPIPEGRV









RRRYMSFVDCGDILLDGVKF









DVFTGSEPDLALIYVDGRSD









NFRARDTNILSYAPIYCAFE









FADPSHPNLKRNTLSEIDTL









WASWSGGEKVRDAGGNQITQ









TSVRDLGGDMTSGGRISFQG









HVTLSRGKSMIAFPHRQNGN









SWFSKTPIVFLQTEGTEDVP









KLLNVTSDGISIEVTSNSAA









IMWQATGT






GO_
GO_
Transcription-
L

Down
MEQNETMTREMSTASVGRSF
256


1912
1912
repair



GPTVWGVPDGSVAFLLRQRL





coupling



AEHDGPLLHVARDDAAVAAL





factor



ADMLAWLMPEVEVLRLPAWD









CLPYDRVSPNPVLIAERAGT









LCRLLEPTKARRIVLTTVHS









LIQRVPPRSAFRGQSISVKT









GESLDQAMLIELLIANGYTR









TDTVMEAGEFATRGGIFDLF









PAGESDPIRLDLFGDEVENI









RAFDVGTQRSTETLKRFELR









PVSEFSLGPDSISRFRTGWR









DSFGPAATSDTIYENVSDGR









RYPGLEHYLPLFHDGDGHQM









ETLLDYLPGGAVSFDHHAPE









ILKARLDMIADHYQARRVPT









REGEIPYRPLPPHRLYLDAH









GWESMLADVPSVILNAFAMP









DTAQGVDAGYRPGPLFARAK









DGSRAGMFEAFGQQVKTWAE









AGRRTYVTAWSRGSRERISH









LLAEHGVTATSYEDWPDAAG









MPKGTTGLLTLGLERGFVSD









RLCFVSEQDLLGERISRPPR









RRKRGEQFISQVGEIAEGDL









VVHSDYGIGRYVGLETVVEG









RVAHDYLSILYDGEQRLLLP









VENIELLSRFGSEQAGVQLD









KLGGTAWQARKAKMKSRIRV









MAGELIKTAAARALKDAPTL









APAEGLWDEFCARFPFVETE









DQSRAIADVLEDMSAGRPMD









RLVCGDVGFGKTEVALRAAF









VAALSGMQVAVVVPTTLLAR









QHFRSFSTRFEGFPVNVAQL









SRLITPKEATKVREGMADGT









VDIVVGTHALLAKTVSFERL









GLLIIDEEQHFGVAHKERLK









ALREDVHVLTLSATPLPRTL









QLSLSGVREMSLIATPPTDR









LAVRTFITPFDSVMIREAIQ









RERFRGGQIFCVVPRLADMD









RMAERLTEIVPDAKTVQAHG









RLTPTELERVMTEFADGKYD









ILLSTNIVESGLDMPSVNTI









IIHRADMFGLGQLYQLRGRV









GRGKQRGYAYLTWPQTRPLS









PSSEKRLEVMQTLDSLGAGF









TLASHDLDLRGAGNLLGDEQ









SGHIKEVGIELYQQMLEDAV









IDMRRERGKRQDDEDSWTPT









IILGLPVLIPEAYVPDLPVR









LGLYRRIASLTNEAEVEAMR









AELVDRFGSLPPEVGNLLDV









VLIKRLCREAGVERLETGPK









GMVIQFRRNRFANPAALIDW









VARKKESGVKIRPDHKLAVI









REMTNATRIGYAKKVTTVLC









KMIRKLEAAKSGD






GO_
GO_
Xanthine
L

Down
MTAAAQFSPLPQWPLYGLTD
257


192
192
and CO



DLFPTLERWSAEGKRAALAT





dehydrogenases



LVSITGSSPRPLGSEMAICE





maturation



DGEVQGYVSGGCVEAAVRAE





factor,



ALESLKDGQPRMLDYGAGSP





XdhC/CoxF



VLDIQLTCGGRIGIFVRALP





family



DLTAHVATLKAARENRRPIT









LLTDLDTGAMQFCPEARATG









LEGRTFARQYLPPLRLILSG









GDPITLALLSLSALMGLETT









LLRPYGPPGPPPGLSPTRYI









RGSLDAALPTLSLDRWTAVY









SLTHDAFADLTLTAHALKSE









AFCVSILGSRRKIPGRLEAL









RTAGVPEEAFSRLHLPAGLE









IGARTPMEIALSILTQMITT









RPR






GO_
GO_
hypothetical
L

Down
MKKEKSAIVLFVKDEAHDIM
258


2170
2170
protein



AWLSWHISLGFDKIFVYDDH









STDGTYEIAKSCEGIYNVEV









CRTSMLEGNFYYRQRDSYFD









AIKKSIDHYEWIAMLDGDEY









VSIDGTQDINGFLDKFRKDD









TGIALSWCIYGSSSRVLKDK









VPTYQVFNHRSTPELNDNTL









VKSFVRPEAVSFVYENPHKF









NLSYGNYADAAGQPVEWRPG









ATKNILWEGARINHYICRSM









EHFIDCIKRRLGSDLSNSTV









YWSHFDRNDVYDPQDQARIN









AANTVYNNIKKSVFQYSMKN









FLEKGNALENTENSLTPHRK









VDLFHLKSIHGEYLSLNNID









GHLFQGEGFERILAAIPYDS









NKIWLFRNPFVYSSNVRFHI









SHSAQSNYCYEFAFDSNESD









GSIFIQSPKTQKYLTCIPVG









HGGSVEFSREEASDWEKFYF









GEKVSELTFVGDNEGPASDL









IYYMLNSAGSFPYEEFLLKS









STLESNDRMNLKSLLGPQIM









SII






GO_
GO_
Glycosyl
L

Down
MRDDPRETLTESYRSAARLN
259


2173
2173
transferase



GLRAEHLQKENQKLLRQLFL









IQTSLSWRVTLPLRAVRALT









FGRLLSGRPVSELPGRFLRL









WGREGLAGIRKTVIHRVRRL









KRIHGDRQKVSTASTAETGG









LHPYRATPECGAARLKPQVL









IIAELSLRQCAKYRVWQKRD









FLQTLGWSVQVVDWRDLAEA









QSALQLCTHVIFYRVPGFDD









VMKLVQEAHRLGLAPRWEVD









DLIFDEGEYRQNGNIDTLPA









AERDLLLSGVALFRRCMLAC









GRGIASTAALAGAMREAGLT









DVAVLENALDAQTLGIAEVL









PLPVPSGRIWVSYGSGTNTH









DADFRQAEAGLLAAMDEEPR









LCLRVIGQLQLSSAFSRFGD









RVERLTELTYPDYLKALSQT









DIAIAPLEKTLFNDCKSNIK









FLEAAIVRVAAICSPCAAFL









TVLRDGKNGLLAADTAAWRN









GFLALARDGDYRKRLAEAAY









KDVMARYAPKAMAQTQARAL









FGLPPSREAEGLRILMANVY









FAPRSFGGATIVAEEMGRRL









VRKGVQVSVMTSRPPAVDIP









DGDVRYDVDGMMVFASVLPD









GLDGVGHLDNPAMASRFADM









LDACQPDVVHVHAAQGLGTG









ILRICQERGIPYVLTLHDAW









WLCERQFMVKGDGRYCFQTT









IDPAVCQACVPGVRHLADRT









VVMRQALAGAALLISPSHAH









RELYLANGIAPERIVVNRNG









FCWPKRARRPRSPGTPLRFG









FVGGTEAVKGYGLLKEAMQS









LSRSDWELVVVDNKLNLGFQ









SIFPEDWTVRGKLRVVPAYT









QASLDDFYDQIDVLLFPSQW









KESYGLTVREALARDVWVVT









TSPGGQSEDVVDGVNGTWLP









LDGKPQTLVQAVSALLEAPE









RFEGYVNPYKEQLATYDMQA









DELYGFLKRAAGQPSGRGAG









L






GO_
GO_
hypothetical
L

Down
MDLLRWTIAFLILALCAAVL
260


2178
2178
protein



GFGGISADFAYIGKILFFIF









LVLLIISLIFGRGRGTRL






GO_
GO_
Uricase
L

Down
MTQDSYPRDMIGYGRTPPDP
261


2386
2386
(urate



KWPNGARIAVQFVINYEEGA





oxidase) (EC



ENSVLHGDAGSEAFLSEMVG





1.7.3.3)



TKSIIGARCAQMESLYEYGS









RAGFWRLRRLFDEAGMPVTV









FGVAKALARNPDAVAAMKES









GWEIASHGLRWIDYQDFPED









LERAHIRKAIALHTEVTGER









PLGWYQGRTSPNTARLVAEE









GGFVYDADSYADDLPYYDRS









NGRAQLIVPYTLDANDMKFA









ALNGFTEGEQFFIYLRDAFD









MLYREGGRMMSVGLHCRLAG









KPARAMGLLKFLEHIRKHED









VWVATRLDIARHWLSVHPA






GO_
GO_
Uncharacterized
L

Down
MMSRIQLTVLRPLHRPTTRL
262


2634
2634
protein



ALGFLALGALAACGSGRDPS





CC_3748



TLTAPRNHLLGVDRGAEGGA









DELRGGVNAYLWRGAIDTLS









FMPLASADAVGGVILTDWYQ









PSASQNERFKIAAYVLDRRL









RSDALRVSVFRQVLQDGQWE









DTPVSATTTSDITTRILTRA









RQLRAENGERDN






GO_
GO_
Type II
L

Down
MSGEFPVDQILRGECIETMK
263


2698
2698
restriction



TLPDGSVDCIFADPPYNLQL





adenine-



RGELRRPDETVVDGVDDDWD





specific



KFADYATYDNFTREWLSEAR





methylase



RILHKDGTIWVIGSYHNVFR





(EC 2.1.1.72)



LGAIMQDLGFWILNDIVWRK









SNPMPNFRGRRFTNAHETLI









WAARGPQSKYRFNYQAMKAL









NDDLQMRSDWYLPLCTGNER









LKNEHGLKLHPTQKPESLLH









RVLVASTNANDVVLDPFCGS









GTTPAMAKRLGRHYIAIERH









PDYVKAARERVAREERLTSE









QLATTPAKREMPRIPFGSFV









ETGVLPAGTLLYDRQKRLKA









TVTPDGTLVSGNQRGSIHKL









GAMLTNAPSCNGWTFWYFER









DGQYVQIDVLRQESQALRNV









G






GO_
GO_
Two-component
L

Down
MPLVTPNMPRVVLVEPDCDH
264


2776
2776
system sensor



ARQIVQVLVKEGFALTCATS





histidine



GEEALGTIEETMPDLVVACT





kinase



ELPGMSGGQLARRLRLDALT









RNIPILMLTEDASPGVEREG









LESGADAYISKSAHPDLMVL









RMRALLREGPELLQVDEASR









LRRARIVIVNSPREDEDEEE









VVEDVPETTLGELLWRDGHT









VTSIERSDDLIEGGWLRGAD









SPDCLVLELGSGDEDLKFCR









LLDARRQAVLEAGGIPFRTL









GIVEASRFRRQSSGEFFEAG









IDDLVPSDIALEALAMRIRT









LAQRRMAQDEFRQQEIERQQ









NALTLEAARAKAEMAEALAQ









ANMELARTNERLLQVQSKLV









QTAKMASLGELVAGIAHEIN









NPLAFTIAHADTVTRTLKRL









QGVNASDEAMSLTKKGMSRL









ESMKLGLQRIQNLVLSLRRF









SRLDESSFQKVDVPAALETA









LALLAHKLGPGIIVQKDLQA









PAELVCQPAFLNQVVMNIIS









NAADALADMSTDGDIVRGRI









VIASRLENGRYEMRVSDDGP









GLPPDLRTRIFDPFFTTKPV









GTGTGLGLAIAYSVMEAHDG









VIEVTDANLPDGRGIGACFR









MSLPVRMTEEGPVATGRAA






GO_
GO_
Oxidoreductase
L

Down
MKLFELGERTAQVHDVLVTV
265


2861
2861
probably



AELAERDDARAVLLESADDP





involved in



ALLKPYLNRLDLVVLRFPVF





sulfitereduction



RDGRGFTQARELREYLRFSG









EIRAEGHILPDQAAFLRRCG









VDSVVLPKDGNGDPALWEKQ









LRQFPVAYQRSVLPERSVGP









GLRVEEAS






GO_
GO_
hypothetical
L

Down
MTRIILQHGQNAPLTLDIEE
266


3031
3031
protein



GSTTPIHLHFSQALPVAAPQ









PEIAPVGPQAAPASKIRRFL









PVAATAAVCAGLLFTFGGPR









ASAPAMPESAPLPPLPSSGP









LETQPQGPAPTAPQQILKAL









HQPAHVEMPPSAPAQAGSPF









GLEN






GO_
GO_
hypothetical
L

Down
MTQGVAEEMANSESQTPKAL
267


967
967
protein



LAAVILMGVLIIAAVFGLIG









VIAYRFLHPRPSVTATVPLA









EGGFSRLALPLGAGEHITAV









TSRPDGLMAVTLSGAGSDRV









LLWNPEAGKIAAELDFGTPA









QSTP






GO_
hII
Ribonuclease HII
L

Down
MPDYALEAAHGGLVVGIDEV
268


2697

(EC 3.1.26.4)



GRGPLAGPVVASAVAFTAPP









SETLSSLLDDSKKLTARRRM









LAYEALMADEQALIGVGAAS









VAEIERINIAQACYLAMRRA









LSRLGCTPDLALVDGKHAPK









LPCPIKMVIGGDGISLSIAA









ASIIAKVTRDRLMARLAVRH









DAYGWERNAGYGTAAHLQGL









KLRGVTPHHRRGFAPIRNMI









EAEAHAA






GO_
htrB
Lipid A
L

Down
MTSFLYRAETLLVRALLAAI
269


2440

biosynthesis



RTLPPAASSSLGGFVARTVG





lauroy1



PLLPVSKVADRNLQLALPEY





acyltransferase



DASARRRIVRDCWENLGSTV





(EC 2.3.1.241)



GEFPHISRLKQNTPSGAGWS









VEGAEHLEAARASGRPVIFF









SGHIGNWELMPPVVARYGMP









FASFYRAASNPGVDRLIHRL









RQDAMGQDVPMFPKGAKGAR









AALKYLSKGGNLGVLGDQKM









NDGIEARLFGRPAMTASAAA









VFALRHDALIVTGHVRRDGP









ARLVLVVDAPFMPTKTDDRA









KDVLVLTQLFNDRLESWIRD









IPGSWLWLHRRWDKSLYRNM









TTQC






GO_
moeA
Molybdopterin
L

Down
MSELLSVTRAMELVLDYAGS
270


193

molybdenum



FGTETVDLTMAAGRILRQTV





transferase



RAERAQPPYDRVMMDGIAFR





(EC 2.10.1.1)



HGSGPTLVSHGIQRAGASGQ









VLPEGHVCLEVMTGAVLPDG









ADTVVPVERLVREGRLIRFE









EGYEPRKGQFIHRRGSDCAA









GTELLAPGQRLDGPALAVLA









GNGHAQVSVSRIPSIGIVAT









GDELVDVSAPVRDWEIRRSN









EYALTGAMLSRGFNCIERSV









VPDDLAETVVALREQLSRHD









VLILSGGVSMGAFDHVPKAL









SKIGVERVFHKVAQRPGKPL









WFGVGPEGQRVFGLPGNPVS









ATTCGVRYVMPMLLAGQGLC









RPEPYTVMLDAEADLIPTLT









RFLPVKLRHDATGQALATPC









PMPTSGDFSFLASTDGFMEL









PRGEGVAPRGTAAMFHGW






GO_
nifS
Cysteine
L

Down
MIYLDYLSTTPCDPAVVKAM
271


85

desulfurase



LPWFGEDFGNPHSPHGPGRK





(EC 2.8.1.7)



AAEAVERAREIVARLLGVEA









REIVFTSGATEANNLAIKGA









VRHLARVGDPRRRIVTLATE









HKCVLESVRDLESEGFEAVV









LGVDSEGRVDPEALRDALKV









PTLLVSIMAANNETGVLQDI









PQLAQIVKERDALMHVDLAQ









MAGKMPVSLRNVDLASVSAH









KMYGPKGIGALYVRRKPRVR









LEPLFSGGGQERGLRSGTLA









TPLVVGFGEAADLAAETMGD









EAARQVFLRDDLWAQLREGL









PGIVLNGAGAPRLAGALNVC









LPEGCRALDVLEACPDVAAS









TGSACTAAEIAPSYVLTAMG









LSAEKASRCLRLSVGRFTSK









ADIDRAASFLIAAARACHPN






GO_
oprB
Carbohydrate-
L

Down
MGKFGQDWTKALLTACAMTA
272


628

selective



VLPGITAVGHAQTTPAGVVD





porin OprB



GHQKAAARTSTATMGTPQIR









TKSISPVPLLVKPAPTKTGV









ETAAKTSDTTESRFFPASFH









DWLTQSTMTGDWGGWRTWLT









DKGINIGGHYLEDSAGNPMG









GKTKAVRYADEFGINVDFNL









KKLTGLNLGMFHTLITARQG









LGIGATLPALDSPQQIFGSG









ETVRLTRLSWEMPWNKYVTT









EVGEINTENDFEQSSVYWGM









SQYCQFESNAICGMPQSIAM









NSGYGWYPTAHPGAWVKFYP









AGNDHYLVQFGAYSVDPVIS









NTHNGWKLNLHDATGTYLPF









QLGWHQGGKDDYSGPLQTNI









KIGGYWDTSEVSDVYSHLGT









FGVPAQYLISAPSEKVRGRF









GGWFQFDRMLQRDEADPNRG









TTLFTSFTWGDPRTSVAPYF









ITWGVTRKGTFRSRPNDTIS









IGMKMLWVNPKLTNWVRQIQ









AAGGTDIYKPSGEHALELNY









GWRPTPWLVIRPGAQYIWST









GGTNRYKNPLLLDFETGITF






GO_
pdh1
Pyruvate
L

Down
MASLILMPALSPTMTEGTLA
273


2072

dehydrogenase E1



RWVRKAGDTVAAGDVIAEIE





component beta



TDKATMEVEAVDEGVIGKTL





subunit



VDEGTQNIAVNTPIAVLLAE





(EC 1.2.4.1)



GEDASAADNVVRSSDPAVGA









PVAIETPSDPAITEAPAVAQ









AEDDRDWGETSEITVRQALR









DAMAAELRRDEDVFLIGEEV









AQYQGAYKISQGLLEEFGEK









RVIDTPITEHGFTGMAVGAA









LTGLKPIVEFMTMNFSLQAI









DHIINSAAKTLYMSGGQMGC









PIVFRGPNGAAARVGAQHSQ









CFASWYAHIPGLKVVAPWSA









ADAKGLLRAAIRDPNPVIVL









ENEILYGQKFPCPVDEDFIL









PIGRAKIEREGTDVTLVAFS









IMVGVALEAAAILADEGISA









EVINLRSIRPLDTETIVRSV









KKTNRIVSVEEGWPVAGIGA









EICTVAVEQAFDWLDAPPAR









VCGLDLPMPYAANLEKLALP









KPEWVVDAVRKQLRD






GO_
petP
HTH-type
L

Down
MDVSSSATAHLYLREDRIRQ
274


1846

transcriptional



SYEAMMLAWRTLNADCEALL





regulator PetP



REKGLGPAHHRILFLTAAHP









GITPGVLLNSLGITKQSLGR









ALGDLRERKLLIQEEDRHDR









RKRPLRLTASGEALERELFL









MIREVMTRAYREAGMTAVEG









FRRVLAPLQVPAESRAR






GO_
petR
DNA-binding
L

Down
MSDEHILVVDDDPRLLRLLQ
275


1847

response



RYLSENGYRVSTALDAQTAR





regulator



DVLQRIQPDALVLDVTMPGE





PetR



DGLSLTNSLRRDGLSLPILL









LTARGEPADRIGGLEAGADD









YLGKPFEPRELLLRLRAHLR









RMVPSLPAVDEVPDVLRLGE









LEFDVKRGLLSGPQGAVHLT









GGESALLGVLTRQPGTVLSR









EAIARALEMDEIGERAVDVQ









VTRLRRRIEADPKEPRFLHT









VRGKGYVLKPGR






GO_
phoR
Phosphate
L

Down
MVLVCVALAGWVLAVWLLLR
276


1161

regulon



QPRVPTSPPDDYLTPVSPAD





sensor protein



LPVDPLPACAVVLDGLGAIV





PhoR



QVNEEAASQFGETVGAILRH





(SphS)



PAARAALSAALRAPVPASPS





(EC 2.7.13.3)



GSSNRGDLPPVCSTTFTLDV









PVPRTLHLMLRRLPGGKGQD









RRVLVVLTDRSEAQAADRMR









MDFVAHASHELRTPLASLSG









FIDALQGAAGENPVMRQQFL









DIMRQQSERLKRLIDRLLYL









SRVQAHEHQRPRDVVDVADL









MAVVLGEVAPRFEQEGRTLK









LEIEDDLLVRADEDEMVQVL









LNLIENALRYGAQEGDPLTI









TLSARRAASPDDRWPADGGV









ILGIEDNGCGMEAHHLPRLT









ERFYRVGAPTDGAGQGTGLG









LSIVRHILDRHGGRLRIASA









PGKGTTCLVWLPPAGATLAV









SMVE






GO_
pstA
Phosphate
L

Down
MSETVVSTTGWKPNPRAARR
277


1165

transport



RRADHLATAFGMVMAGILVL





system permease



VLASILWTLLSRGLAGLSAA





protein PstA(TC



AIMKPMGPPGSSSGLANAIV





3.A.1.7.1)



GSLIQTFMALLMATPLGLGC









GIYLSEYGTETNKFASCVRF









VSDVLMSVPSILVGLFVYQV









LVAPFGHFSALAGSVALAIL









AVPIIVRTTEDMLRLVPTSM









REAGAALGATRWRVTLSLCL









RSAKTGVLTGILLALARVSG









ETAPLLFTSLGNQNWSFSLN









RPMASLPVTIYQYAGASYED









WVQLAWAGALLVTMGVLAIN









IAVRVSARRG






GO_
pstB
Phosphate
L

Down
MIQDSMMTETDPQVAKSPEV
278


1164

transport



ALAVRNLNFYYGENHALHDI





ATP-binding



SIDFPARRVTAMIGPSGCGK





protein



STLLRVFNRMYDLYPGQRAT





PstB (TC



GEVIFDGRNVLERDLDLNIL





3.A.1.7.1)



RARVGMVFQKPTPFPMSIYD









NIAFGVRLHEKLNKADMDAR









VQDVLTRVALWNEVRDRLNA









PASGLSGGQQQRLCIARSIA









TRPEVLLLDEPTSALDPIST









ARIEELLDELKEEFTIAIVT









HNMQQAARCADQVAFFYMGR









LIEVDSADRMFTNPKQQQTQ









DYITGRFG






GO_
pstC
Phosphate
L

Down
MTLATATQPEEARDKAGVSH
279


1166

transport



SGSRRSGPDTAFHLLVAASA





system permease



LLVLVVLGGLVVLMGVGGSQ





protein PstC(TC



AFRTFGLGFAFHDVWNPVAD





3.A.1.7.1)



QYGAWAPLFGTIVSTLIGVA









IALPLAFGTAFWLTAMAPPR









IAAIVGTAVQLLAAVPSIIF









GMWGFFTIVPFMARTVQPFL









THHFRHVPGIRFIIHGAPFG









TGLMTAGLVLAVMIAPFMTA









VMRDVFAAMPAMLRESAYGL









GATRWDVMWKVVVPWSRTGM









IGAIVLGMGRALGETMAVTF









VIGNVTAVGWSLFAPRSTVA









SLIALQFPESPAGSLRLSAL









LALGFILMLLSFASLALARM









LRGDTK






GO_
pstS
Phosphate ABC
L

Down
MIKSRAPLFGLLVATALGTA
280


2369

transporter,



AMTPFVSSAKAADITGAGSS





periplasmicphosphate-



FAAPIYGAWGTAAKSQAGIA





binding protein PstS



VNYQSVGSSAGQDQVIARTV





(TC 3.A.1.7.1)



DFGASDKPMSGDRLAKEKLY









QFPTVMSGIVVVANVPGIAP









GQLRLDGPTLAGLYDGEITT









WDDDRIKALNPGLKLPDTDV









APIHRADGSGTSYVFTSYLS









QVSPTWKQKLGAGTSIAWPG









GSGARGNDGIAAMVRQTEGG









VGYVEYSYAAQNHLNIAQMK









NHSGAFVAPTLASFAEAAKA









ADWVHADHYAVNLLDTDGAS









SWPIVTATFVLVPVDAAQKE









SGKAVRNFFAWGFQHGDADN









ARLDYVGLPQNVKTDILANW









PK






GO_
speC
Pyridoxal 5-
L

Down
MTPKITRFLAEQQPATPCLV
281


201

phosphate (PLP)-



VDLDVVGAHYRALHDALPEA





dependent ornithine



KIYYAIKANPAPAILDRLVA





decarboxylase (EC



LGSSFDVASPAEIRMCLDAG





4.1.1.17)



AAPDRISYGNTLKKAEWIRE









AHDLGISLFVFDSIEELEKL









AKHAPGARVFCRLAVENEGA









DWPLSRKFGTTLSNARALML









RARELGLKPYGLSFHVGSQQ









TGVAAYDHAIAKAAGLYHDL









RAQGVDLQMLNLGGGFPTHY









RENVPSVQDFAHTIHTSLKT









HFPDGAPEILLEPGRYMVGQ









SGVVSSEVILVSRRGGALTD









PRWVYLDIGRFGGLAETEGE









AIRYTFRTSRDSEDAARSPC









VVAGPSCDGVDIMYEKNRIP









LPDSLECGDRVEILATGAYV









STYCSIGFNGFPPLTEYYI






GO_
surA
Periplasmic
L

Down
MSKTHCIASTALAALLAFSA
282


2743

chaperone and



ALPATAAPHHKADPKAASKT





peptidyl-prolylcis-



AATKQEAPPAKPPEDQILAV





trans isomerase of



INGQVLTQRDVDNRAKLFVL





outer membrane



STGLPISPEIMNRMRGQIIH





proteins SurA



QLIDERLKTQEILKLHINVE





(EC



PDQIAGAISNIEQRNGMPKN





5.2.1.8)



ALRDRLASDGVSLTTLIDQI









RVQIGWMQVLREKLGEEGRI









TATQISQREQALQAEQGRAQ









YFMSEIFVPVADPRHDENEL









AFTKTIISQLREGAPFPIVA









AQFSQAQSALDGGSMGWVQE









DNLDPQVVNIVRQMPIGAIS









NPIQVAGGFVIATVQSKRVV









GKQMGTLLDLRQAFFPFDAP









LNPQNPTEQQRAALQKATTA









VQTVHSCDAMEALNKSLGEK









RPSNPGSQILERLMPQMKAV









LEALPPNRVSRPLVSMDGIA









LLMVCNRQQKNLAQQSPSEI









ADQLMNERVEQASRQLQRDL









QRRAIIEMRPAAKTAFN






GO_
tonB
TPR domain protein,
L

Down
MSLSLYRRLSARNLLLAGVF
283


2957

putative component



GIAALAGSAHADDVLGQAVG





of TonBsystem



KDLQQAQSALAAKNYAKAMD









AVDAADAVKGKTDYEAYTTA









QMRAAIAAQSGNTDAAIKAY









DVLINSSRTPKATKGQMLMA









QATMAYSAKQYARAIPATER









YLKEYGADPRMQTMLIQCYY









LQQDWKGTAKAAQEQVDATI









KAGKVPAENQLQMLATAYTN









LKDADAKTHAYVLLAKYYSK









PDYWSMLIHDLVANPNLSPP









LVFYVERLRLATGVLKDPSD









YQDMGERAVOMGLPQLALNL









LNQGYANHSLGNGPTAAADA









KFHAFVAQQAATNRSQLASA









VTQAASAPNAGPALTAGYNQ









VLNGQVDAGLALMKTGLGKN









PRYPDLAQVEYGMAQMDGGQ









KAEAIKTFASVQGNGPAKDV









AELWSLLLSRPTK






GO_
top1
DNA topoisomerase
L

Down
MTDVVVVESPAKAKTINKYL
284


2929

I (EC 5.99.1.2)



GSGYTVLASFGHVRDLPPKD









GSVRPDENFAMSWQTDERGA









KQISAITKALKGAKNLYLAT









DPDREGEAISWHVRSVLEEK









KLLKNVDVHRVTFNEITKSA









VTAAMAAPRELDRPLIDAYL









ARRALDYLVGFTLSPVLWRK









LPGSRSAGRVQSVALRLICE









REAEIEVFRPKEYWTVTGGF









TTPGKAAFQARLTHLKGEKL









DQFDLNNEQLAFGARDTVLG









GQFTVRSVERKRTKRNPPPP









FTTSTLQQEASRKLGMSAQT









TMRTAQQLYEGVDLRGETTG









LITYMRTDGVTMAKEAVGAI









RGHIGKAFGDEYVPDYPRSY









STKAKNAQEAHEAIRPTDVF









LTPQQVAHALTPEQKKLYEL









IWKRSVASQMQSAELDQVAV









TLADASGQTLLRATGSTIAF









DGFLKLYIEGRDDTKAEDED









GKLLPPMKEGDRLTTGTVDA









EQHFTQPPPRYSEASLVKKM









EEIGIGRPSTYASILGVLRD









RNYVRLDARRFVPEDRGRLV









TAFLTSFFERYVDTGFTASL









EEQLDDISGGRADWHDVMAA









FWHDFSAAVAQTKDLKISDV









IDALDEDLGPHFFPPRPDGA









DPRVCTSCGTGRLGLRLGKF









GAFIGCSNYPTCQFTRRLVA









EEGDSEGLNDGPKVLGQDPE









TGEDISIRRGPYGLYIQRGE









PNPEDKKAKPKRTTIPKGID









GNTMTMEQALGLLSLPRLIG









LHPETGEKIEAGLGRFGPYV









KMGAIYGTLDKDDDVLTVGL









NRAVDALAKKLASIRNLGPH









PKDGEPVMIRKGRFGPYAQH









GQLITNLPKGQDMDEVTLDE









AVALLAEKGKPLKGGAKKTS









AKKAAPKAAKAKKAVAAAEG









DEAAPKKVTKRSPAKSATKT









KTTTPRKRKTVSDTSSEG






GO_
ykoH
Two-component
L

Down
MSRADLRFSELFRADLFRTA
285


2648

system sensor



TFRLTLAFVVAIIAGMALQF





histidine kinase



GLVYGQMSGYEQQRSTDLLQ









REAALLVHETPAELEYEVRE









RSKTDLRVILNGAALFDMSR









NRIAGDIKKWPVGLEVSPKT









QRLWDAPPGDTPYEMRYLAV









EVEGTNGNRDRILVLARSLH









MANELRYITKRAALMSVVPV









VAFALMAGIFLSHRALGRIK









DMHEAIDRIMDGDLHERLPT









GRERDDIERLAVSVNRMLDR









LEHLLDEIRDVGNDIAHDLR









TPLARVKARLERVSAITNDP









AALQGAIERAALDLEQCFSV









ITALLRIGEIENGRRRAGFA









MLDLRELLAGVVDLYEPIAE









TEGVMLEVVDSDKPVPLFGD









KDLLNEVLANLVDNAIKFTP









EPGTVRLSAGQGPDGATWLQ









VADTGIGIAEDERKAVMGRF









YRSDKSRHVPGSGLGLSLVS









AILRLHGASVDIVSAHPGQA









LPGAVFTIHFAPPASV






GO_
GO_
Amidohydrolase

F
Down
MTIRSSFAALLLATPAALSV
286


2942
2942
precursor



GSAMAEPVAFEHARLIDGTG









ALAQPDATVVIDNGTIISVG









IPAPAQVRHVDLTGKTLMPA









LISDHVHVGLVKGTGASRDN









YTRANILAALKQYSDYGVLT









VTALGLNRSPLFDTLRQEQH









DGRNPGADLYGVDQGIGAPD









GVPPAAMVKGVGPDQVFRPT









TPEEARKDVDQMIAEHTDLV









KLWVDDFRNDVPDGKTYPML









PPAIYQAVIDEAHQHGTRVA









VHIHDLAVAKAIVASKADIL









AHGVRDQPVDHDLIAAMLRQ









GTWYIATLDLDEANYLYAEQ









PELLSNPFVLAGVNPALRRQ









FTDPKWRAETLAKPLTKASH









YALSVNQKNLAVLYRAGVKV









GFGTDSGAAPTRIPGFAEHR









ELYLTVQAGLSPVQAISLAT









GNAAALLHLSDRGVIAPGRR









ADLLVVNGNADENIGAVDQI









DQVWQRGMLVSHGPVRSKN






GO_
GO_
Uncharacterized

F
Down
MTLSVIHDKTTTLTGAPVAA
287


313
0313
SAM-dependentO-



LLERLFAEAETATNPAIADI





methyltransferase



PREEFQRLAGSRTEYRKFYG









LAKHLWLPVSRETGTLLYML









ARATWAKNIVEFGTSFGIST









IHLAAALRDNGGGKVITTEF









EPSKVARARAHLEEAGLADL









VEFREGDALQTLAAGLPESI









DIVLLDGAKPLYPDILDLLE









DRLQAGALIVADNADHSPEY









LARVRSPAAGYLSLPFAEDV









ELSVRLH






GO_
GO_
Glutamate N-

F
Down
MAKPLPVSPLARPLPDLATI
288


1376
1376
acetyltransferase



AGVRLSAVAAGIRYQGRTDL





(EC



MLAEFVPGTVAAGVYTKNAC





2.3.1.35)



PGAPVLWCREALTTPYARAL





N-



LVNAGNANVFTGRAGMQACE





acetylglutamate



DCADATAQLLDCPPQDVFLA





synthase (EC



STGVIGEKLPQDRIIAALPA





2.3.1.1)



ARAGLEENGWADAARAIMTT









DTFPKAARRDVKINGTPVRI









QGIAKGSGMVAPDMATMLAY









VATDARLPQNVLQSLLASGC









AQSFNSITVDSDTSTSDMLM









IFATGLADNPEVDDVNDPAL









AEFTLALNDLLLELALMVVR









DGEGATKLVRIAVTGADSNL









SAHRIALCIANSPLVKTAIA









GEDANWGRVVMAVGKSGEPA









DRDRLSVAIGGTWIAKDGGV









VENYDEAPVVAHMKGQEIEI









AVDLGLGDGQARVWTCDLTH









GYIDINGSYRS






GO_
GO_
hypothetical

F
Down
MIDFSSWHSLLATLIGLALF
289


178
178
protein



TLIGVGIRLLTMLTIQQRRE









RMNRQINERLRVLMAAYRTL









GGSFTGTLLVDPTHKRDLEP









DQLSGSDRNRRIRDAVEAAL









SDIILLGTEEQVRMAGRAAA









ELVAGRPVPTHDLVVSLRNF









IRKALNLESLPSDLVLPEQG









PARPSSSGGNKGDGKEGGKG









GGGGGDGGGGGGMGMQGGMD









PALHHSETDSHTL






GO_
GO_
Phage shock

F
Down
MSPDNLALLIPIVAIIAWSV
290


2357
2357
protein



TSMVKHTTRQADPPGQPDPM





B



LQAALTQAEAHATRLEERID









OLERILDEDIPGWRARNAR






GO_
GO_
Threonine

F
Down
MRYRSTRGELTADAPNFSDI
291


2556
2556
synthase



LLAGLAGDGGLYMPESWPRI





(EC 4.2.3.1)



SPQTLREWRTLSYPDLAAEV









IALFTEGAIDVDTLRDMTRD









AYADFDHAAVVPLVEVEQDL









YSLELFHGPTLAFKDMAMQM









LGRLFDHVLTQRNRHVTIVG









ATSGDTGSAAIEACRGRERL









SVVILHPKGRTSDVQRRQMT









TVQDDNILNIAVEGDFDTCQ









DLVKAMFADHAFRDEVSLSA









VNSINWARIAAQIPYYVRAA









LALGAPDREVSFSVPTGNFG









NVLAAWAAKQMGLPIKKLCI









GSNRNDILTRFVIDNDMSVR









TVEPSLSPSMDIQVSSNFER









LLFELLDRNSTRCAAIMREF









RETGRMAVPHDAWTRMKEVF









EGMTLTDEQTSEAMRLFYNE









SLYLADPHSAIGLAVGKRFQ









EPGIPMVAAATAHPAKFPDA









VIAATGIHPKLPPHLSDLFE









RTERYECMDSQIAGLQDAVR









AHIRRG






GO_
GO_
hypothetical

F
Down
MIASQGPSMRRNRLSVARLS
292


2916
2916
protein



VQMGAMASVGLLLSGCSGAD









VSRAIGLERAMPDEYTVTTR









APLSMPPSEQMQLPGAADAH









RPDESPRMQALETLSPDTAL









HPDAGQGSSGQTALVGQVDK









SASAPNNAELGAADAGFVDN









LMFWKGGNAGSVVDGDAENR









RIRENSALGRNPATGATPTV









RKKKAFLGVL






GO_
GO_
ATP synthase

F
Down
MPLRIEIVSPEKRLVEREVD
293


2979
2979
epsilon chain



MAVVPGMEGDIAAMPDRAPL





(EC



MLQLRGGVVALYQGDKIVDR





3.6.3.14)



YFVTGGFADMGADHCTILAD









SAQLMSELSVDEAKSRLRDL









ESRWAEIGPNDVDMHDQISR









ELQSVRAELEAVQEHGPA






GO_
idnk
Gluconokinase

F
Down
MTENETQLGLKPHFLVVMGV
294


1341

(EC



SGTGKTTVASGLATRLGWHF





2.7.1.12)



QEGDALHPPANVEKMSTGQP









LTDADRAPWLALCHEWLRKQ









VEAGHGAVLTCSALKRSYRE









QLRGEDLPIEFVHIDTSVGE









LADRLQRREGHFMPASLLPS









QLATLEVPGDDEPVIRVSGE









KHPDVVLEELIRHFQAED






GO_
mobA
Molybdenum

F
Down
MTPLYGLILAGGASKRMGTD
295


196

cofactor



KAALDYHGKPQLQVAFEVLS





guanylyl



PLVEKCFVSVRPDQTADPLR





transferase



SSFPQIVDTVDVDGPAAGLL





(EC 2.7.7.77)/



SAHRAYPDVAWLVLACDLPM





Molybdopterin



LDRGTLDTLIAARDAGHVAV





synthase sulfur



SYRSEHDGLPEPLCAIWEPE





carrier subunit



ALDRLEKQVAGGRICPRKLL









INSPTKLLEPHRRGALDNIN









TPEERDDAARRLKDLPGGPM









IRLTLEYFAQLRELAGTREQ









SLETAFVTVGPLYEELREKY









AFPFEASKLRVAINGDFAPW









TQALKDGDHIVFIPPVTGG



GO_
nifS
Cysteine

F
Down
MTALKTVSGTTYLDANATEP
296


84

desulfurase



LRPCAKEAAVEGMMLSGNPS





(EC 2.8.1.7)



SVHAEGREARRFLEDARSRV









AAGFGRISGTCVFTSGATEA









DAMAVHAFGQERRIFVGSTE









HDAILRAAPEAEILPVNRDG









ILDVEHLRSRLQDTGPALVC









VMSANNETGVLSPLEDVLAV









CRDSGAHLHVDAVQSAGRLP









FALGGCSVAVSGHKMGGPKG









AGALLLAEDEPMDALVAGGG









QERGRRGGTQALPAILGMAA









AFDAARAQDWAPVQRLRDRV









EAAAKSVGARVAGEAVDRLP









NTSCLILDGVAAQVQLMALD









LAGFCVSAGSACSSGKVSSS









HVLRAMGETEGASQAIRVSL









PWNVREAQVEAFCEAYEAMA









RRLRK






GO_
phgdH
D-3-

F
Down
MSSKPDILTIDPLVPVMKER
297


2626

phosphoglycerate



LEKSFTLHPYTSLENLKSIA





dehydrogenase



PAIRGITTGGGSGVPSEIMN





(EC



ALPNLEVISVNGVGTDRINL





1.1.1.95)



DEARRRNIGVATTQNTLTDD









VADMAVALMMTVMRGIVTND









AFVRAGKWPSATPPLGRSLT









RKKVGIAGFGHIGQAIAKRV









SAFGMEVAYFNSHARPESTC









HFEPDLKALATWCDVLILAV









SGGPRSANMIDRDILNALGK









DGFLVNIARGTVVDEAALLS









ALQEKRIAGAGLDVFQNEPN









INPVFLSLPNTVLQAHQASA









TVETRTAMAHLVVDNLIAYF









TDKTLLTPVI






GO_
lychF
GTP-binding and

F
Down
MGFNCGIVGLPNVGKSTLFN
298


2153

nucleic



ALTETAAAQAANYPFCTIEP





acid-binding



NTGRVAVPDPRLDELARIGK





proteinYchF



SIRKVPTSLEFVDIAGLVRG









ASKGEGLGNQFLANIREVDA









IVHVLRCFEDDDITHVEGGV









DPVRDADIIETELMLADLES









LEKRQVGLQKRARGNDREAQ









AQLELMEPLLAALRDGKPAR









TAVSKGQEAEASRLQLLTTK









PVLYVCNVEEASAATGNAFS









EAVRKRAEAEGAGVVVVSAA









IEAEVSQLPQEDRTEFLEGL









GLTDSGLDRVIAAGYKLLGL









RTYFTVGPKESRAWTITAGT









KAPQAAAVIHNDFERGFIAC









ETVAFDDYVACNGEAGAKES









GKLRIEGKEYVVQDGDVLLF









RFNV






GO_
GO_
Transcriptional

F
Down
MSDDPPFLRDADQTRKNILE
299


29
29
regulator,



VALKEFAEYGLAGARVDRIA





AcrR



RGTRTTKGMIYYHFGDKDGL





family



YKAVLEKVYPSLRSDEEHLD









VRNTDPVEALERIIDFTLDY









HEKHEDFVRIVMIENINKGE









HLRKTGIDSTVSYRIMMVIA









DILNRGMALGLFKREITPVD









LHIFYTSFCFYRVGNHHTVS









SVLGINMLSAQSCARHRRMV









KDAVIAYLASSD






GO_
GO_
Pyruvate

F
Down
MTYTVGHYLAERLTQIGLKH
300


2220
2220
decarboxylase



HFAVAGDYNLVLLDQLIEQG





(EC



GTKQIYDCNELNCSFAAEGY





4.1.1.1)



ARANGAAAAVITFSVGAISA









MNGLGGAYAENLPILVISGA









PNSNDHGSGHILHHTIGTTE









YSYQMEMAKHVTCAAESITS









AEAAPAKIDHVIRTMLREKK









PAYLEIACNISAAPCVRPGP









VSSLHAHPRPDEASLKAALD









ESLSFLNKANKVAILVGTKL









RAAEALKETVELADKLGCPV









TVMAAAKSYFPETHPGFRGV









YWGDVSSPGAQEIIEGADAV









ICLAPVWNDYSSGGWKSIVR









GEKVLEVDPSRVTVNGKTFD









GFRLKEFVKALTEKAPKKSA









ALTGEYKPVMLPKADPSKPL









SNDEMTRQINELVDGNTTLF









AETGDSWFNAVRMHLPEGAK









VETEMQWGHIGWSVPSMFGN









ATASPERKHVLMVGDGSFQL









TAQEVAQMVRYELPVIIFLV









NNHGYVIEIAIHDGPYNYIQ









NWDYAALMQCFNQGVPGEES









GKYGLGLHATTGAELAEAIA









KAKKNTRGPTLIECKLDRTD









CTKTLVEWGKAVAAANSRKP









QSV






GO_
asns
Asparagine

S
Up
MCGIAGLSCLPGHHPDQDAL
301


2458

synthetase



ERMSQAIFHRGPDGEGRLDL





[glutamine-



GGAALRHRRLSIVDIAGGAQ





hydrolyzing] (EC



PFRLGAAALIANGEIYNDPA





6.3.5.4)



IRRRFPKTCFQTYSDCEPPL









HLWLHDGAGYTHELRGMYAI









AIVENEHGRHEMVLSRDPFG









IKPLYIAAYEGGIAFASEPQ









ALLAGGFGKRSIRDSARDEL









MQLQFTTGQDIIFDGIRRLL









PGETLRIVDGRIVESRRRHV









LHEARDTVPARLSDEQALER









LDTALLDSVSAHLRADVPLG









LFLSGGIDSSVILAAAHRLG









LPHPRTWTARFDAGKADESA









DAAALAASVGAEHHVLTVTE









DMVWRELPSIVACMDDPAAD









YATIPTWFLAREARKDVTVI









LSGEGGDELFAGYGRYRRVM









KPWWKGGRAPYRSGTFGRRF









AEHGRQWRRGIAMTELALGV









SGLEGAQALDIAEWLPNDLL









LKLDRCLMAHSVEGRTPLLD









PVVAKAIWPLPEHFKVRDGY









GKWLLRRWLQDALPQARPFA









PKQGFTVPVGPWIEKQAHRL









GPLVARQPCIRAMMPAVDVE









RLFARASQRGVARQAWTLLF









FALWHRHHIEGVPVEGDTFE









TLARAS






GO_
czcD
None (Cobalt-

S
Up
MTPDPHHDCACDHAHHGTTV
302


1427

zinc-cadmium



PHEHHAHDHADHDHDDHHHD





resistance



HDHCDGHSHGFGFGHQHVHA





protein



PASFGMAFAVGITLNTAYVA





CzcD)



GEALWGVWAHSLSLLADAGH









NLSDVLGLAGAWLAQVLATR









PSSARFTYGLRRSTILSALA









NAMILLLVTGGIVWESVLRL









FSHQNVQGEVISWVALVGIA









VNAVTALLFMKGASSDLNVR









GAFLHMAADAVMAFSVVIAG









LLIAFTGYTIIDPIMSLIVS









VSIVIGTWSLLRSSLDLALD









AVPAGIDPDAVQAALLSLDG









VSGLHHLHIWAMSTTETALT









VHLVCDPTKPVSTDLVIARA









AELVRTRFDIAHPTFQLETQ









PSVCDTHQPCC






GO_
GO_
hypothetical

S
Up
MLASGIFQFLPAGVVTEKGV
303


1177
1177
protein



FSIHEKMNWRSCLWCRPLVR









LGATTA






GO_
GO_
Putative

S
Up
MSHPVSRRDFAVGLVAGVAA
304


1928
1928
hemagglutinin-



AGTGVAGAADPEKAVPTPPP





related



PPKPVAKTICFVGGYTKHGP





protein



PGGGTGNGQGISVFDMDRDT









GVLTPITTFTDIASPSFLAI









SKDQRFLYALSEIDDFNKDG









DGSVTAFAIDPKTGSLRKLN









VVSSKGAVPAHLSIHHSGRY









VLVANYVGGCVAVLPIRSDG









SLGEASDVVHNTGPRQPERA









SDNPQGNFAVSDHSGSHPHM









IHSDPSGKFVLADDAGLDRV









YVWTLNIDTGKLIPAKTPYY









DMEPGSAPRHFQFNHSGRIL









YNLCEQDSKVVVSNFDPATG









AINDIQTVSTVTSHFRGSTL









AAEILISASGKFVYVSNRLG









DSLAVFAIGADGTLTLQDEV









WMHADYGRALMFDPSGAFLF









CANQRSDAVTSFKVDKKTGE









IAFTNNFTPVGSPTTFAFMN









TQV






GO_
GO_
hypothetical

S
Up
MGSYCGIHFDKLSICGSKSE
305


783
783
protein



VPGDWAALFQERDRRETRPT









QEVGADPDLCVEYAASRDVI









LRRLSILGATDEAVQRAFET









WLTEEQEQWRDNTEGWSDQE









VISEHAAKMLKGLNGLTYQE









WCRFASGALRIRYDFANYDR









IQSDLASDPFRNQFHEPDDG









YLWFAGYGSHLGLRALLDAV









PDIKEVRLDISDLLGEYVDE









HEPICSRARENAPCQLQMLA









PTMVMAEGSSDLTALRLGLG









AMHPDLMDYFSFFNHAELSV









DGGAHYLVKFLKAIAAARST









SRILAIFDNDTVGIQAYEQA









RALKLPFNIIVTRYPDSDVA









KAYPTVGRSGPAILDVNGQA









AGIELYMGREALLSNGELRP









VRWASYVASAGKYQGEVDGK









RQVLEAFRKNIATVEGPEAA









RASFPDLERVWQHNFDLVQE









NSGLVYLRTGKRLA






GO_
hlyD
HlyD family

S
Up
MSSSDMIPNEGQPSGQSDED
306


1175

secretion



FNQHVPRTATDPFAPNDMPL





protein



ALLEFHSPTAGLINLPATPA









ARYIILLIGGLFLACLAVMA









LFPINRVVSTPGRLISTQPT









IVVQPLETSIIRSIDVHVGD









FVKKGDVLAHLDPTITEADI









TNMHLQRDAYQAEYDRLKAE









AAGQDYHVNLNDPASVEQGA









AFLRRKTEYQAHVENYAQQI









ASLESDIQGYRANAAMYGSK









MRVASEVLQMRQREQADQVG









SRLSTLGAQTELMEAERAEI









AAQQSANSAEKKLAAMKAER









DGYIGNWQAKIYSDLTEAGH









HLAEYRSSYEKARLRQDLVL









LRAPEDGIVLTIAQGSVGSV









LQSAGQFITLVPTGYGLEME









AVLRSQDVGFVQVGDHALLK









FATFPYDQYGGAEATVRVIS









ADAFTPSSQNAGGGSNGNTP









SDDATASGVYRVRLRIDRYT









LHGQPSFFHPMPGMSLTADI









DVGKRTVLQYLFNKITPALT









NGMREP






GO_
pal
Tol-Pal system

S
Up
MKFKVFGALGLALVLAACSN
307


1363

peptidoglycan-



GNTNKGDSTGAGAVAQEAGP





associated



TPGSEADLVANVGDRVFYEL





lipoprotein



NQSQLSEEARATLDKQVAWL





PAL



AKYPQVSIQVAGNCDDRGTE









EYNIALGORRANAARDYLVA









KGVSASRITTISYGKDRPTA









DGDDEQSWAQNRNAITSVR






GO_
PhoB
Phosphate regulon


Up
MKGPSLARAKGLVLLVEDDP
308


1162

transcriptional



ALLLMTCYNLEQRGYRVETA





regulatory



EDGEAALLALETARPDAVVL





protein



DWMLPGLSGLDVCRRIRANP





PhoB (SphR)



ALRDVPVLLLTARSAEQDAI









RGLDTGADDYLMKPCSIDTL









DARLRALLRRHQSSYDRLSF









ADITLDPETHRVERAGRMLS









LGPTEYRLLDLLIRNPRKVF









SREDLLRRIWGQNIHVEIRT









IDVHIRRLRKAINGPGEVDL









VRTVRAAGYALDDGPTTDGA









In embodiments, the modified bacteria have at least one engineered genetic change that is correlated with improved bioleaching of REEs, relative to REE bioleaching by unmodified bacteria of the same species as the modified bacteria. The disclosure includes the proviso that the set of modified genes may exclude a disruption of membrane bound glucose dehydrogenase (mgdh) gene as the only modification of the described bacteria. However, this gene may also be disrupted, provided it is in the context of at least one other gene modification that is described herein. In non-limiting examples, at least one genetic change increases acidification of a medium in which the modified bacteria are present. In a non-limiting example, the at least one genetic change is in a gene that is part of a phosphate transport system. In embodiments, the bacteria are modified such that they comprise a mutated gene that comprises or consists of at least one of: GO_1415, pstA, pstB, pstC, pstS, ggtl, surA, petP, ykoH, speC, and tonB. In embodiments, the modification comprises a disruption of at least GO_1415, or pstC, or a combination thereof.


The disclosure includes compositions comprising one or more REEs and modified bacteria of the disclosure. The disclosure includes a biolixiviant produced by the modified bacteria and one or more REEs. In embodiments, the disclosure relates to separating combinations of REEs. In embodiments, the disclosure relates to separating any one or combination of lanthanum, cerium, praseodymium, neodymium, promethium, samarium, europium, gadolinium, terbium, dysprosium, holmium, erbium, thulium, ytterbium, lutetium, scandium, and yttrium, from a composition comprising one or more of the REEs. The composition comprising the REEs may be any composition of matter, including but not limited to solids, semi-solids, and liquids. In embodiments, the REEs are present in a feedstock. In non-limiting embodiments, the REEs are present in coal fly ash, virgin ore, electronic waste, fluid cracking catalysts, and the like.


The disclosure includes a method comprising contacting a composition comprising one or more types of REEs with a biolixiviant produced by modified bacteria of this disclosure. In an embodiment, the method further comprising separating and optionally purifying one or more types of REEs from the composition comprising the REEs and the biolixiviant.


The disclosure comprises isolated modified bacteria, cell cultures comprising the modified bacteria, and kits comprising the modified bacteria. In an embodiment, a kit comprises one or more sealed containers comprising the modified bacteria, which can be used in REE bioleaching approaches.


The disclosure includes media in which the bacteria are cultured, and bacterial secretions. In an embodiment, the disclosure provides a biolixiviant produced by the described bacteria. In embodiments, the kit contains a sealable or sealed container that contains a biolixiviant produced by the described bacteria. The disclosure also includes modifying bacteria so that they comprise at least one of the described gene modifications.


The disclosure includes all modified microorganisms described herein. The described approaches may be used to engineer any type of bacteria. In embodiments, the bacteria are Gram-negative bacteria. In embodiments, the bacteria are obligate aerobes. In embodiments, the bacteria modified as described herein comprise any member of the bacteria family Acetobacteraceae. In an embodiment, the bacteria is a type of Gluconobacter. In an embodiment, the modified bacteria are Gluconobacter oxydans. In this regard, G. oxydans secretes a biolixiviant rich in gluconic acid. This is produced by periplasmic glucose oxidation by the pyrroloquinoline quinone (PQQ)-dependent membrane-bound glucose dehydrogenase (mGDH). The final pH of the biolixiviant is a major factor in REE bioleaching. But, gluconic acid alone fails to explain bioleaching by G. oxydans: pure gluconic acid is far less effective at bioleaching than the biolixiviant produced by G. oxydans. This means that even the most previous successful efforts to up-regulate mGDH activity and gluconic acid production are unlikely to take full advantage of G. oxydans' biolixiviant production capabilities. Thus, the present disclosure reveals a curated set of genes that can be modified to improve REE extraction, as demonstrated in the following Examples.


EXAMPLES

To characterize the genome of G. oxydans and identify a comprehensive set of genes underlying its bioleaching capabilities, we built a carefully curated whole-genome knockout collection of single-gene transposon disruption mutants using Knockout Sudoku (FIG. 1). Final pH of the biolixiviant is a good predictor for bioleaching efficiency, thus we used acidification as a proxy for bioleaching potential and have thoroughly screened the collection to identify mutants that differ in their ability to produce acidic biolixiviant (FIGS. 2 and 3). In one non-limiting example, we demonstrate that a single gene disruption—only one of several potential enhancement strategies—can significantly improve G. oxydans bioleaching capabilities (FIG. 4). In one limiting example, we demonstrate that increasing expression of mgdh or cleanly deleting pstb or psts can significantly improve G. oxydans bioleaching capabilities (FIG. 5).


Development of a Knockout Collection for G. oxydans Covering 2,733 Genes


We built a saturating coverage transposon insertion mutant collection for G. oxydans B58 and catalogued and condensed it with the Knockout Sudoku combinatorial pooling method (FIG. 1). We sequenced the G. oxydans B58 genome and identified 3,283 open reading frames (FIG. 1A). Following the recommendation of Monte Carlo simulations, we constructed a saturating coverage transposon insertion collection (the progenitor collection; PC) containing 49,256 mutants (FIG. 1B).


The progenitor collection catalog indicates that we were able to generate at least one disruption mutant for almost every non-essential gene in the G. oxydans genome. In total, we identified disruption strains for 2,733 genes out of the 3,283 genes in the G. oxydans B58 genome. Since every predicted gene contains at least seven AT or TA transposon insertion sites, the remaining 550 non-disrupted genes are likely to be essential. A Fisher's Exact Test for gene ontology (GO) enrichment representing 268 of the non-disrupted genes demonstrated significant enrichment in several essential ontologies, with the greatest enrichment in those relating to the ribosome and translation (FIG. 1C).


The progenitor collection catalog was used to create a condensed G. oxydans disruption collection with at least one representative per non-essential gene. 47 progenitor strains were verified by Sanger sequencing prior to condensing, of which 43 (92%) were confirmed to have the predicted transposon coordinate. We selected one mutant for all 2,733 disrupted genes, a second mutant for 2,354 genes, and a third mutant for 50 genes where mutant location information was poor. All mutants were struck out for single colonies, and 2-10 colonies per mutant were picked, depending on the predicted number of cross-contaminating disruption strains in the originating well. This condensed collection contains 17,706 mutants in 185 96-well plates.


The condensed collection catalog was validated by a second round of combinatorial pooling and sequencing. Of the 17,706 wells in the condensed collection, we were able to confirm the identity for 15,257. We confirmed 25 of these wells by Sanger sequencing, and 100% have the predicted transposon coordinate. Among these wells, we were able to verify the identity and location of 4,419 independent transposon insertion sites, representing a disruption mutant for 2,556 unique genes (FIG. 1D). 1,587 genes are represented by more than one disruption, and 3,317 of all disruptions occur in the first half of the gene.


Genome-Wide Screening Discovers 165 Genes Significantly Linked to Acid Production

We screened the new G. oxydans B58 whole genome knockout collection for disruption mutants with differential acidification capability (FIG. 2). We used the colorimetric pH sensitive dyes Thymol Blue (TB) to screen for changes in final biolixiviant pH (FIG. 2A), and Bromophenol Blue (BPB) to screen for changes in rate of acidification (FIG. 2B).


In total, we observed 304 genes that apparently controlled acidification (FIG. 2C). The TB screen discovered 282 genes whose disruption leads to a differential change in biolixiviant acidity (FIG. 2C). 47 mutants produced a more acidic biolixiviant, while 235 produced a less acidic one (FIG. 2C). The BPB screen identified 82 gene disruptions with differential rate of acidification: 49 with a faster rate, and 33 with a slower rate. 60 mutants were identified by both screens (FIG. 2C). Overall, we identified 165 genes that statistically significantly changed the final biolixiviant pH, rate of acidification, or both, but did not change the growth rate (FIG. 2C). We re-arrayed disruption strains with differential acidification into new 96-well plates alongside proxy wild-type (pWT) strains that have a transposon insertion in an intergenic region and show non-differential growth or biolixiviant production. The new collection was re-assayed with the TB and BPB assays and the strength and significance of each result was determined by comparison with pWT through a Bonferroni-corrected t-test. Mutants that cause the 25 largest reductions, and 50 largest increases in endpoint acidity yet do not affect growth rate are shown in FIG. 2D. 31 mutants that cause significant changes in acidification rate without changing growth rate are shown in FIG. 2E. However, 14 of the faster strains, including δGO_868, a disruption of a LacI type transcriptional repressor which was the fastest strain, produced a less acidic biolixiviant than the wild-type, indicating that targeting these genes for engineering a faster acidifier would likely be at the expense of a more acidic biolixiviant. None of the strains with a faster rate of acidification also created a more acidic biolixiviant. These results indicated that multiple genetic engineering interventions are needed to construct a strain of G. oxydans that simultaneously produces a more acidic biolixiviant than the wild-type at a faster initial rate.


Phosphate Transport and PQQ Synthesis are the Biggest Controllers of Acidification

We used gene ontology enrichment to determine which biological processes, metabolic functions, and cellular components the most significant gene disruption mutants are involved in (FIG. 3). Among the disrupted genes that led to a stronger acidity (FIG. 3A), the most significant enrichment for all three GO categories involves the phosphate-specific transport system, represented by pstA, pstB, pstC, pstS, and phoR. Other enriched ontologies include those related to phosphate signaling and binding.


Among the disrupted genes that led to a weaker acidity, several enrichment groups are related to the synthesis or use of the redox cofactor, PQQ, represented by pqqB, pqqC, pqqE, tldD, and mgdh (FIG. 3B). Other enriched ontologies include those related to carbohydrate metabolism.


Acidification rate is controlled by carbohydrate metabolism and respiration. Disruptions in the pentose phosphate pathway increase acidification rate (FIG. 3C). Meanwhile, disruptions of the electron transport pathway components are the most significantly enriched group of mutants that decrease acidification rate (FIG. 3D).


Single Gene Knockout Mutants can Significantly Change REE Bioleaching
Validation of Dye Assays by Direct pH Measurements

We selected 14 strains with some of the most significantly increased or decreased acidification for further testing (FIGS. 2D and E). Dye pH measurements were validated by direct pH measurements. 11 of the 13 strains that produced significantly lower pH biolixiviant in TB assays did the same in direct pH measurements. The most acidic biolixiviant was produced by a disruption in the phosphate transport gene, δpstC at pH 2.09 (FIG. 4A). 4 of the 11 mutant strains that produced a more acidic biolixiviant were disrupted in genes involved in the pst phosphate-specific transport system (δpstA, δpstB, δpstC, and δpstS).


Additional disruptions that led to a more acidic biolixiviant included those in a hypothetical protein with no similarity to anything previously characterized (δGO_1415S); a gamma-glutamyltranspeptidase (δggtl); a periplasmic chaperone (δsurA); an HTH-type transcriptional regulator (δpetP); a two-component system sensor histidine kinase (δykoH); a Pyridoxal 5-phosphate (PLP)-dependent ornithine decarboxylase (δspeC); and a TPR domain protein that is a putative component of the TonB iron uptake system (δtonB).


9 of the tested strains produced biolixiviant significantly higher in pH than pWT (FIG. 4B). The most alkaline biolixiviant was produced by a disruption in the PQQ synthesis system, δpqqC. at pH 4.71. While δpqqC produced very little acid, this is below the pH of glucose in media alone, indicating that some bacterial acidification still occurred. 3 of the 9 mutants that produce reduced acidity biolixiviant either synthesize PQQ (δpqqC and δtldD), or use it as a cofactor (δmgdh). Additional disruptions that led to a more alkaline biolixiviant than pWT include a Fructose-bisphosphate aldolase class II (δGO_3252); a GTP and nucleic acid binding protein (δchF); a lipid A biosynthesis protein (δhtrB); a peptide chain release factor (δhemK); the LacI type transcriptional repressor that increases initial acidification rate (δGO_868); components of a proteolytic complex (δtldD and δtldE); and the glucose dehydrogenase (δmgdh).


Disrupting the Phosphate Transport System Significantly Increases Bioleaching

We tested if 10 of the mutants that produced a more acidic biolixiviant could bioleach REE from retorted phosphor powder (RPP) from spent fluorescent lightbulbs more efficiently than pWT (FIG. 4C). For each mutant, the elemental composition of REE leachate was similar to previous reported values. Six of these mutants significantly increased bioleaching. Two of the better bioleaching mutants disrupted the pst phosphate transport system (δpstC and δpstB). Overall, we found that bioleaching efficiency correlates with biolixiviant pH, as expected (FIG. 4E).


The δpstC mutant produced the most acidic biolixivant, and extracted the most REE from RPP: 5.5% total extraction efficiency as compared with pWT's 4.7%. Stated differently, δpstC removed 18% more REE from RPP than pWT. This increase in REE extraction remains significant even under a Bonferonni correction, the most stringent statistical test for significance. Without the adjustment, six of the better acidifiers were also better bioleachers than pWT (FIG. 4C). The remaining better bioleachers increased REE extraction by between 11% (δspeC) and 18% (δggtl) (FIG. 4C).


Without intending to be bound by any particular theory, it is considered that disrupting the phosphate transport system de-represses acid production in G. oxydans. Six of the disruption strains that resulted in a lower biolixiviant pH (δpstC, δpstB, δggtl, δpstA, δpstS, and δykoH), including three that increased bioleaching (δpstC, δpstB, δggtl), are involved in phosphate transport, sensing and signaling.


In its natural environment, G. oxydans produces biolixiviants to liberate phosphate from minerals, not metals. Under phosphate-limiting conditions, the PstSCAB phosphate transporter will activate the histidine kinase, PhoR, which in turn phosphorylates the transcription factor PhoB, and activates the pho regulon, enabling phosphate assimilation and uptake. Under sufficient phosphate conditions, PhoB is deactivated by PhoR, which in turn inhibits expression of these genes. Without intending to be constrained by any particular view, it is considered that disrupting any of these genes prevents G. oxydans from sensing when it has released adequate phosphate and when to stop producing biolixiviants.


Disrupting Mgdh and PQQ Synthesis Genes Significantly Decreases Bioleaching

We also tested REE extraction by 4 mutants that produce a less acidic biolixiviant than pWT. Even under the most stringent statistical test, the Bonferonni correction, they were all worse bioleachers than pWT (FIGS. 4C and D).


The δmgdh mutant was the worst bioleacher of all tested, considering its lack of gluconic-acid production. δmgdh reduced bioleaching by 97%. Disruption mutants that knocked out synthesis of mGDH's essential redox cofactor, PQQ, also produced significant reductions in biolixiviant acidity. δpqqC reduced bioleaching by ≈94%. While bioleaching by δmgdh and δpqqC was negligible compared to pWT, they were able to bioleach a statistically significant amount of REE compared to glucose alone. This indicates, that a bioleaching mechanism independent of mGDH exists in G. oxydans (FIG. 4D).


Disruption mutants in tldD and tldE were also much worse at bioleaching than pWT. δtldD reduces bioleaching by 92%, while δtldE reduces it by 63% (FIG. 4C). It is considered that TldD and TldE may contribute to the supply of the PQQ cofactor to mGDH. δtldD strongly attenuates acid production (FIG. 4B), and the gene has already been implicated in PQQ synthesis in G. oxydans 621H. In E. coli, TldD and TldE form a two-component protease for the final cleavage step in the processing of the peptide antibiotic, Microcin B17. In a similar manner, PqqF and PqqG from Methylorubrum extorquens form a protease that releases PQQ in the final step of its synthesis. It is considered that TldD in G. oxydans may play the same role as PqqF from M. extorquens, while TldE plays the same role as PqqG. Deletion of pqqF in M. extorquens completely inhibits final cleavage of PQQ, while we find that disruption of tldD in G. oxydans reduces REE bioleaching by 92%. Moreover, deletion of pqqG in M. extorquens only reduces PQQ cleavage to 50%, while disruption of tldE only reduces REE bioleaching by 63%. These parallels strongly indicate a novel role for TldE in the biosynthesis of PQQ in G. oxydans.


It will be recognized from the foregoing description that bioleaching has the potential to revolutionize the environmental impact of REE production, and dramatically increase access to these critical ingredients for sustainable energy technology. The present disclosure related to this potential by providing for improved bioleaching by genetic engineering.


By constructing a whole genome knockout collection for G. oxydans, we are able to characterize the genetics of this process with high sensitivity and high completeness. In total we identified 165 gene disruption mutants that significantly change the acidity of its biolixiviant, rate of production, or both.


REE bioleaching by G. oxydans is predominantly controlled by two well-characterized systems: phosphate signaling and glucose oxidation that is supported by production of the redox cofactor PQQ. Interrupting phosphate signaling control of biolixiviant production by disrupting a single gene (pstC) can increase REE extraction by 18%. Disrupting the supply of the PQQ cofactor to the membrane bound glucose dehydrogenase reduces REE extraction by up to 92%.


Comprehensive screening of the G. oxydans genome also discovers completely new targets that contribute as much to REE bioleaching as previously characterized ones. For example, disrupting GO_1415, which encodes a protein of completely unknown function, increases REE bioleaching by 15%. Additionally, these results highlight the potential for a previously uncharacterized role of TldE in PQQ synthesis.


The discovery of the potential contribution of TldE to PQQ biosynthesis may allow for marked enhancement of the cofactor production through the additional over overexpression of this gene, and a consequent increase in dehydrogenase activity, including production of gluconic acid by mGDH and any useful downstream products. PQQ is an essential cofactor important for several other industrial applications of G. oxydans, including production of L-sorbose. Furthermore, PQQ alone has many applications across many biological processes from plant protection to neuron regeneration.


Without intending to be bound by any particular theory, it is believed that the present disclosure provides the first demonstration of improvement of bioleaching through genetic engineering. Furthermore, the creation of a whole-genome knockout collection in G. oxydans can facilitate its use as a model species for further studies in REE bioleaching and other industrially important applications of similar acetic acid bacteria. The findings of the two major systems contributing to acidification in G. oxydans according to this disclosure show that, for greatly improving bioleaching: reduce inhibition of regulation of acid production by disabling the phosphate-specific transport system, while over-expressing mgdh along with the expanded synthesis pathway for its cofactor PQQ.


Materials and Methods


Gluconobacter oxydans B58 Genome Sequencing



Gluconobacter oxydans strain NRRL B-58 (GoB58) was obtained from the American Type Culture Collection (ATTC), Manassas, VA. In all experiments, G. oxydans was cultured in yeast peptone mannitol media (YPM; 5 g L−1 yeast extract, 3 g L−1 peptone, 25 g L−1 mannitol), with or without antibiotic, as specified.


Genomic DNA was extracted from saturated culture using a Quick-DNA Miniprep kit from Zymo Research (Part number D3024, Irvine, CA). Genomic DNA library was prepared and sequenced using a TruSeq DNA PCR-Free Library Prep Kit (Illumina, San Diego, CA).


The prepared library was sequenced on a MiSeq Nano (Illumina, San Diego, CA, USA) with a 500 bp kit at the Cornell University Institute of Biotechnology (Ithaca, NY, USA). Resulting paired end reads were trimmed using Trimmomatic and assembled with SPAdes using k-mer sizes 21, 33, 55, 77, 99, and 127, and an auto coverage cutoff. Assembly quality was checked with QUAST and genome completeness was verified with BUSCO using the proteobacteria_odb9 database for comparison. The resulting 62 contigs were annotated online using RAST (rast.nmpdr.org).


Gene Ontology Enrichment

DIAMOND was used to assign annotated protein models with a closest blast hit using the uniref90 database, an E-value threshold of 10−10, and a block size of 10. InterProScan (version 5.50-84.0) was used to assign family and domain information to protein models.


Output from both of these searches was used to assign gene ontologies with BLAST2GO. Gene set enrichment analysis was done with BioConductor topGO package, using the default weight algorithm, the TopGO Fisher test, with a p-value threshold of 0.05.


Mating for Transposon Insertional Mutagenesis

The transposon insertion plasmid, pMiniHimarFRT was delivered to GoB58 by conjugation with E. coli WM3064. E. coli WM3064 transformed with pMiniHimarFRT was grown overnight to saturation in 50 mL LB (10 g L−1 tryptone, 5 g L−1 yeast extract, and 10 g L−1 NaCl) supplemented with 50 μg mL−1 kanamycin (kan) and 90 μM diaminopimelic acid (DAP), rinsed once with 50 mL LB, then re-suspended in 20 mL YPM.


We used a Monte Carlo numerical simulation (collectionmc) to approximate how many insertions would need to occur before a mutant is found representing a knockout of each gene in the genome. Our calculations demonstrated that we would be able to identify mutants in at least 99% of all G. oxydans B58 genes if we generated and selected at least 55,000 mutants (FIG. 1B).


GoB58 was grown for approximately 24 hours in YPM, then back-diluted to an optical density (OD) of 0.05 in 750 mL YPM and incubated at 30° C. for two doublings until the OD reached 0.2. GoB58 culture was distributed into 13 50 mL conical tubes, to which rinsed and re-suspended WM3064 was added at a ratio of 1:1 by density (approximately 1 mL WM3064 to 50 mL B58). Bacteria were mixed by inversion then spun down at 1900 g for 5 minutes. Supernatant was poured off, and the mixture was resuspended in the remaining liquid (≈0.5 mL), pipetted onto a YPM plate in 5 spots of 0.1 mL, and allowed to dry on the bench under a flame.


Mating plates were incubated at 30° C. for 24 hours. Mating spots were collected by adding 4 mL YPM to a plate, scraping the spots into the liquid, then suspending by pipetting up and down several times. Suspended cells were collected from each plate, and the suspension was plated onto YPM agar with 100 μg mL−1 kanamycin at 100 μL per plate.


After 3 days of incubation at 30° C., colonies were picked into 96-well microplates using a CP7200 colony picking robot (Norgren Systems, Ronceverte WV, USA). Each well contained 150 μL YPM with 100 μg mL−1 kanamycin. For all experiments, GoB58 was grown in polypropylene microplates sealed with a sterile porous membrane (Aeraseal, Catalog Number BS-25, Excel Scientific) and incubated at 30° C. shaking at 800 rpm. Isolated disruption strains were grown for three days to allow nearly all wells to reach saturation. Wells B2 and E7 of each plate were reserved as no-bacteria controls.


In total 18 matings were required to recover and pick a progenitor collection of 49,256 disruption strains into 525 microplates over the course of about two months. Microplates with saturated wells were maintained at 4° C. for up to 3 weeks and incubated an extra night at 30° C. before pooling.


Combinatorial pooling which was done in three batches. The 525 plates were virtually arranged in a 20 by 27 grid, and combinatorial pooling, cryopreservation, pool amplicon library generation, and sequencing were all done as previously described.


Curation of a Whole-Genome Knockout Collection

Sequencing data for the progenitor collection was processed into a progenitor collection catalog using the KOSUDOKU suite of algorithms. To create a condensed collection, a disruption strain was chosen for each of the 2,733 disrupted genes available in the progenitor collection, first prioritizing close proximity to the translation start, then the total probability of the proposed progenitor collection address. A second strain was chosen from the remaining strains for each gene that had another available. For 50 genes, both disruption strains selected were ambiguously located, and thus a third strain was selected from the remaining collection.


In total, 5,137 disruption strains were isolated and struck-out for single colonies. Many progenitor wells were predicted to have more than one possible strain per well, so for each strain, the number of colonies isolated was two times the predicted number of strains in the progenitor well, up to ten. The condensed collection, which amounted to 17,706 wells, was pooled, sequenced, and validated as previously described. Unknown disruption strains significantly linked to acidification were identified with Sanger sequencing, also as previously described, with the exception of the transposon-specific primers. For the first and second rounds of nested PCR, the transposon-specific primers were (5′-GTATCGCCGCTCCCG-3′ (SEQ ID NO: 309), and (5′-CATCGCCTTCTATCGCCTTC-3′ (SEQ ID NO: 310)), respectively.


Thymol Blue Endpoint Acidity Assay

Endpoint acidity was measured using the pH indicator thymol blue (TB, Sigma-Aldrich, St. Louis, MO), which changes from red to yellow below a pH of 2.8 (www.sigmaaldrich.com/US/en/product/sial/114545). The lowest pH of biolixiviant generated by GoB58 was 2.3 (Reed2016a), thus TB allows for distinguishing strains that lower the pH below that of the wild type biolixiviant. To generate biolixiviant, the condensed collection was pin replicated into new growth plates containing 100 μL YPM with 100 μg mL−1 kanamycin per well. After two days of growth, an equal volume of 40% w/v glucose was added to the cultures for a final solution of 20% w/v glucose. The amount of glucose needed to lower the pH below 2.3 via the production of gluconic acid was estimated to be 13% w/v, but the higher concentration was used to account for any use of glucose as a carbon source and still maintain an excess amount. Viability tests demonstrated that the bacteria were still viable after two days of culture in such a solution (data not shown).


Bacteria were incubated with glucose for 48 hours to allow acid production to reach completion. Plates were then centrifuged for 3 minutes at 3200 g (top speed) and 90 μL of the biolixiviant supernatant was removed and add to TB at a final concentration of 40 μg mL−1. After 1 minute of vortexing, absorbance was measured for each well at 435 nm and 545 nm on a Synergy 2 plate reader (Biotek Instruments, Winooski, VT, USA). Because of variation in background absorbance from well to well on each plate, absorbance was measured at these two wavelengths, and their ratio was used as a proxy for pH, which correlates linearly within the range of pH for the majority of biolixiviants produced by the collection.


Bromophenol Blue Acidification Rate Screen

Acidification rate was measured using the pH indicating dye, Bromophenol Blue (BPB). Knockout collection strains were grown for two days. OD was measured at 590 nm for each well, then 5 μL of culture was transferred to a polystyrene assay plate containing 95 μL of 2% w/v glucose and 20 μg mL−1 BPB in deionized water. The initial pH of the culture is just above 5, and within moments of adding culture to glucose with BPB, the color begins to change rapidly. Assay plates were vortexed for one minute after addition of bacterial culture, then immediately transferred to a plate reader where the change in color was tracked by measuring absorbance at 600 nm every minute for 6 minutes, resulting in 7 reads. Mean rate (V) and R-squared were calculated by the Gen5 microplate reader and imager software (Biotek Instruments). A plot of all V relative to OD demonstrated that the two are correlated, thus V was normalized to OD for each well.


Hit Identification in Acidification End Point and Rate Screens

Once every well had its assigned data point (A435/A545 for TB, and V/OD for BPB), hits were determined by first identifying outliers for each plate. The interquartile range and upper and lower bounds were calculated in Microsoft Excel considering all wells with cultured disruption strains. Any data point that was more than 1.5 times over or under the upper or lower bound, respectively, was considered an outlier. A disruption strain was considered a hit if over half of the wells for that strain (or 1 of 2) were outliers.


Acidification End Point and Rate Quantification with Colorimetric Dyes


For each assay, knockout strains identified as hits were isolated from the knockout collection into new microplates, along with several blanks per plate, and proxy wild type strains—GoB58 strains with an intergenic transposon insertion that should not affect the acidification phenotype. OD and acidification phenotypes were measured for each proxy WT strain separately to verify that growth and acidification are unaffected in these strains.


Acidification phenotypes for the disruption strains were compared to that of proxy WT with a Student's t-test in Microsoft Excel, two-tailed with equal variance. A Bonferroni correction was used to determine significance to account for the possibility a comparison is significant by chance alone: a phenotype was considered significant if p>0.05/n, where n is the number of comparisons being made (n=120 or n=242 for endpoint acidity comparisons with pWT set A or set B, respectively; n=60 for rate of acidification comparisons with pWT).


Choice of Proxy Wild-Type Comparison

The biolixiviant end point pH and acidification rate of each G. oxydans mutant were compared against a proxy wild-type set of mutants for each phenotype. To account for the presence of a kanamycin cassette in the genome, the proxy wild-type set for each phenotype was constructed of several mutants with the transposon inserted in an intergenic region, that had no growth defect, and no apparent change in phenotype.


As the efficiency of the E. coli WM3064 to G. oxydans mating was low, we constructed the G. oxydans progenitor collection in 18 mating batches. As a result of this, the possibility existed that there might be slight variations in the wild type background from batch to batch.


For the acidification rate, we found that these variations did not affect the wild-type behavior across the collection, and a single set of proxy wild-type strains could be used as a comparison with notable disruption strains in the quantification assays. For the end point pH measurement, we found two distinct proxy wild-type behaviors in the condensed collection. For plates 1 to 76; 110 to 130; and 160 to 185, we used proxy wild-type set A, and for plates 77 to 109 and 130 to 159 we used proxy wild-type set B.


For both wild-type sets, we compared ODs after two days of growth, and endpoint acidity using the TB absorbance ration (A435/A545). For wild-type set A, which we used for the BPB quantification assay, we also compared acidification rate of individual proxy WT strains of set A. Comparisons were all made using a linear model, one-way ANOVA, and post-hoc Tukey HSD in R.


Direct Measurement of Biolixiviant pH

Bacteria were grown for 48 hours in tubes containing 4 mL YPM with 100 μg mL−1 kanamycin. One tube was left uninoculated as a no-bacteria control. OD was normalized to 1.9 and diluted in half with 40% glucose for a final 20% solution in 1.5 mL. Five replicates were created for each strain and controls, and all mixtures were randomly distributed across two deep well plates. 750 μL of mixture was transferred from each well to a second set of deep-well plates for bioleaching experiments. All plates were incubated shaking at 900 rpm at room temperature.


After two days, one set of deep-well plates was centrifuged for 10 minutes at 3200 g (top speed), and the pH of the supernatant was measured by insertion of a micro-probe to the same depth in each well.


Four standards were used for meter calibration—pH 1, 2, 4, and 7—and the meter was re-calibrated after every 12 measurements. pH measurements for each disruption strain were compared with those of proxy WT using a Student's t-test in Microsoft Excel, two-tailed, with equal variance. A biolixiviant pH was considered significantly different if p<0.05/n, with n=27.


Direct Measurement of REE Bioleaching

The second set of deep-well plates was centrifuged for 10 minutes at 3200 g (top speed), and 500 μL of biolixiviant was transferred from each well to a 1.7 mL Eppendorf tube. 20 mg (4% w/v) of retorted phosphor powder was added to each tube for bioleaching. Tubes were shaken horizontally for 36 hours at room temperature, then centrifuged to pellet remaining solids. Supernatant with leached REE was filtered through a 0.45 μm AcroPrep Advance 96-well Filter Plates (Pall Corporation, Show Low, AZ, USA) by centrifuging at 1500×g for 5 minutes.


All samples were diluted 1/200 in 2% trace metal grade nitric acid (Thermo Fisher Scientific) and analyzed by an Agilent 7800 ICP-MS for all REE concentrations using a rare earth element mix standard (Sigma-Aldrich) and a rhodium in-line internal standard (Sigma-Aldrich). Quality control was performed by periodic measurement of standards, blanks, and repeat samples


An additional 1/20 dilution in 2% nitric acid was analyzed for mgdh and pqqc disruption strains, and the no-bacteria control (glucose).


Bioleaching measurements for each disruption strain were compared with those of proxy WT or glucose using a Student's t-test in Microsoft Excel, two-tailed, with equal variance. Total REE extracted was considered significantly different if p<0.05/n, with n=12 for those compared to pWT, and n=2 for those compared to gluco

Claims
  • 1. Modified bacteria for use in bioleaching rare earth elements (REEs) from a composition comprising the REEs, the modified bacteria comprising at least one engineered genetic change that is correlated with improved bioleaching of the REEs, relative to REE bioleaching by unmodified bacteria of the same species as the modified bacteria, and wherein the at least one genetic change comprises a change that results in decreased expression, or increased expression, of at least one gene, and wherein the at least one gene optionally encodes a protein that participates phosphate-specific transport system signaling, or encodes a protein that participates in pyrroloquinoline quinone (PQQ) synthesis.
  • 2. The modified bacteria of claim 1, wherein expression of the gene that encodes a protein that participates in the phosphate-specific transport system signaling is suppressed, and wherein said gene is optionally pstS, pstB or pstC.
  • 3. The modified bacteria of claim 1, wherein expression of the gene that encodes a protein that participates in the PQQ synthesis is increased, and wherein said gene is optionally selected from the group consisting of pqqA, pqqB, pqqC, pqqD, pqqE, tldD and tldE.
  • 4. The modified bacteria of claim 1, wherein, in addition to the at least one genetic change, the modified bacteria have been modified to increase expression of mgdh relative to expression of mgdh by unmodified bacteria.
  • 5. The modified bacteria of claim 1, wherein expression of pstS is reduced.
  • 6. The modified bacteria of claim 1, wherein expression of pstB is reduced.
  • 7. The modified bacteria of claim 1, wherein pstS, pstB, pstC, or a combination thereof is reduced, wherein expression of pqqA, pqqB, pgqC, pqqD, pqqE, tldD, tldE, or a combination thereof is increased, and wherein the expression of mgdh is also increased.
  • 8. The modified bacteria of claim 5, wherein the modified bacteria are Gluconobacter oxydans.
  • 9. The modified bacteria of claim 6 wherein the modified bacteria are Gluconobacter oxydans.
  • 10. The modified bacteria of claim 7, wherein the modified bacteria are Gluconobacter oxydans.
  • 11. A method comprising contacting a composition comprising rare earth elements (REEs) with a biolixivant produced by modified bacteria of claim 1.
  • 12. The method of claim 11, further comprising separating REEs from the composition.
  • 13. The method of claim 11, wherein expression of pstS is reduced in the modified bacteria.
  • 14. The method of claim 13, further comprising separating REEs from the composition.
  • 15. The method of claim 11, wherein expression of pstB is reduced in the modified bacteria.
  • 16. The method of claim 15, further comprising separating REEs from the composition.
  • 17. The method of claim 11, wherein pstS, pstB, pstC, or a combination thereof is reduced, wherein expression of pqqA, pqqB, pqqC, pqqD, pqqE, tldD, tldE, or a combination thereof is increased, and wherein the expression of mgdh is also increased in the modified bacteria.
  • 18. The method of claim 17, further comprising separating REEs from the composition.
  • 19. A kit comprising modified bacteria of claim 1 the kit further comprising one more sealable containers in which said modified bacteria are held.
  • 20. The kit of claim 19, wherein the modified bacteria are modified Gluconobacter oxydans.
CROSS REFERENCE TO RELATED APPLICATIONS

This application claims priority to U.S. provisional application No. 63/220,475, filed Jul. 10, 2021, and to U.S. provisional application No. 63/152,798, filed Feb. 23, 2021, the disclosures of each of which are incorporated herein by reference.

PCT Information
Filing Document Filing Date Country Kind
PCT/US2022/017101 2/18/2022 WO
Provisional Applications (2)
Number Date Country
63220475 Jul 2021 US
63152798 Feb 2021 US