Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 6.529763 | - | upp | b2498 | uracil phosphoribosyltransferase |
EG11332 |
CATALYTIC ACTIVITY: UMP + PYROPHOSPHATE = URACIL + 5-PHOSPHO-
ALPHA-D-RIBOSE 1-DIPHOSPHATE.
PATHWAY: PYRIMIDINE SALVAGE PATHWAY.
SUBUNIT: HOMOTRIMER.
INDUCTION: BY PYRIMIDINE STARVATION.
SIMILARITY: BELONGS TO THE UPRTASE FAMILY.
|
 | | uraA | b2497 | uracil transport |
EG12129 |
FUNCTION: TRANSPORT OF URACIL IN THE CELL.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE XANTHINE/URACIL PERMEASES FAMILY.
|
| | b2496 | b2496 | putative DNA replication factor |
EG14201 |
SIMILARITY: BELONGS TO THE DNAA FAMILY. STRONG, TO H.INFLUENZAE
HI1225.1.
|
| 6.122468 | - | guaB | b2508 | IMP dehydrogenase |
EG10421 |
CATALYTIC ACTIVITY: INOSINE 5'-PHOSPHATE + NAD(+) + H(2)O =
XANTHOSINE 5'-PHOSPHATE + NADH.
PATHWAY: FIRST REACTION UNIQUE TO GMP BIOSYNTHESIS.
SUBUNIT: HOMOTETRAMER.
MISCELLANEOUS: IMP DEHYDROGENASE FROM OTHER BACTERIAL SOURCES HAS
BEEN SHOWN TO VARY WIDELY WITH RESPECT TO ALLOSTERIC PROPERTIES,
SIZE AND SUBUNIT COMPOSITIONS.
MISCELLANEOUS: IMP DEHYDROGENASE SUBUNIT OF E.COLI CONTAINS A
CYSTEINE AT THE IMP BINDING SITE & IS INHIBITED IN A SIMPLE
COMPETITIVE MANNER BY GMP. IT DOES NOT EXHIBIT ALLOSTERIC
PROPERTIES AS DOES IMP DEHYDROGENASE FROM BACILLUS SUBTILIS OR
SALMONELLA TYPHIMURIUM.
SIMILARITY: TO OTHER EUKARYOTIC AND PROKARYOTIC IMPDH AND TO
GMP REDUCTASE.
SIMILARITY: CONTAINS 2 CBS DOMAINS.
|
| | guaA | b2507 | GMP synthetase (glutamine-hydrolyzing) |
EG10420 |
CATALYTIC ACTIVITY: ATP + XANTHOSINE 5'-PHOSPHATE + L-GLUTAMINE +
H(2)O = AMP + PYROPHOSPHATE + GMP + L-GLUTAMATE.
PATHWAY: GMP BIOSYNTHESIS.
SUBUNIT: HOMODIMER.
SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE TYPE-1
GLUTAMINE AMIDOTRANSFERASE FAMILY.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE GMP SYNTHASE
FAMILY.
|
| 5.077871 | + | xseA | b2509 | exonuclease VII, large subunit |
EG11072 |
FUNCTION: BIDIRECTIONALLY DEGRADES SINGLE-STRANDED DNA INTO LARGE
ACID-INSOLUBLE OLIGONUCLEOTIDES, WHICH ARE THEN DEGRADED FURTHER
INTO SMALL ACID-SOLUBLE OLIGONUCLEOTIDES. IT CAN ALSO DEGRADE 3'
OR 5' SS REGIONS EXTENDING FROM THE TERMINI OF DUPLEX DNA
MOLECULES AND DISPLACED SS REGIONS.
CATALYTIC ACTIVITY: EXONUCLEOLYTIC CLEAVAGE IN EITHER 5'-TO 3'-OR
3'-TO 5'-DIRECTION TO YIELD 5'-PHOSPHOMONONUCLEOTIDES.
SUBUNIT: HETEROOLIGOMER COMPOSED OF TWO DIFFERENT SUBUNITS WITH
AN APPROXIMATE RATIO OF 4 SMALL SUBUNITS FOR 1 LARGE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE XSEA FAMILY.
|
| 4.395116 | + | mrcA | b3396 | peptidoglycan synthetase; penicillin-binding protein 1A |
EG10748 |
FUNCTION: CELL WALL FORMATION. SYNTHESIS OF CROSS-LINKED
PEPTIDOGLYCAN FROM THE LIPID INTERMEDIATES. THE ENZYME HAS A
PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE N-TERMINAL DOMAIN
(FORMATION OF LINEAR GLYCAN STRANDS) AND A PENICILLIN-SENSITIVE
TRANSPEPTIDASE C-TERMINAL DOMAIN (CROSS-LINKING OF THE PEPTIDE
SUBUNITS).
PATHWAY: FINAL STAGES IN PEPTIDOGLYCAN SYNTHESIS.
SUBCELLULAR LOCATION: TYPE II MEMBRANE PROTEIN. INNER MEMBRANE (BY
SIMILARITY).
SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE
TRANSGLYCOSYLASE FAMILY.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE
TRANSPEPTIDASE FAMILY.
|
| 4.139290 | + | tig | b0436 | trigger factor; a molecular chaperone involved in cell division |
EG11003 |
FUNCTION: INVOLVED IN PROTEIN EXPORT. ACTS AS A CHAPERONE BY
MAINTAINING THE NEWLY SYNTHESIZED PROTEIN IN AN OPEN CONFORMATION.
SIMILARITY: BELONGS TO THE FKBP-TYPE PPIASE FAMILY. TIG SUBFAMILY.
|
| 3.879938 | - | yrfD | b3395 | orf, hypothetical protein |
EG12925 |
|
| | yrfC | b3394 | orf, hypothetical protein |
EG12924 |
|
| | yrfB | b3393 | orf, hypothetical protein |
EG12923 |
|
| | yrfA | b3392 | orf, hypothetical protein |
EG12922 |
|
| | hofQ | b3391 | putative transport portein |
EG12113 |
SUBCELLULAR LOCATION: OUTER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE PULD/OUTD/EXED/XPSD FAMILY.
|
| 3.600748 | - | ygiR | b3016 | orf, hypothetical protein |
|
|
| | b3015 | b3015 | orf, hypothetical protein |
EG13019 |
SIMILARITY: TO M.JANNASCHII MJ1155. ALSO SOME SIMILARITY TO FAMILY
UPF0004.
CAUTION: THIS IS A CONCEPTUAL TRANSLATION; A FRAMESHIFT WAS
INTRODUCED IN POSITION 319 TO PRODUCE THIS ORF.
|
| 3.225086 | - | rplN | b3310 | 50S ribosomal subunit protein L14 |
EG10875 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 23S RIBOSOMAL RNA.
MASS SPECTROMETRY: MW=13540.2; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L14P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplX | b3309 | 50S ribosomal subunit protein L24 |
EG10884 |
FUNCTION: THIS PROTEIN IS FOUND IN THE RIBONUCLEOPROTEIN CORE AND
IS INVOLVED IN THE EARLY ASSEMBLY OF THE 50S SUBUNIT. IT IS NOT
INVOLVED IN THE FUNCTIONS OF THE MATURE 50S SUBUNIT.
MASS SPECTROMETRY: MW=11186.5; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L24P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplE | b3308 | 50S ribosomal subunit protein L5 |
EG10868 |
FUNCTION: THIS IS ONE OF 3 PROTEINS THAT MEDIATE THE ATTACHMENT OF
THE 5S RNA INTO THE LARGE RIBOSOMAL SUBUNIT.
MASS SPECTROMETRY: MW=20169.8; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L5P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsN | b3307 | 30S ribosomal subunit protein S14 |
EG10913 |
FUNCTION: KNOWN TO BE REQUIRED FOR THE ASSEMBLY OF 30S PARTICLES
AND MAY ALSO BE RESPONSIBLE FOR DETERMINING THE CONFORMATION OF
THE 16S RRNA AT THE A SITE.
MASS SPECTROMETRY: MW=11449.3; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S14P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsH | b3306 | 30S ribosomal subunit protein S8, and regulator |
EG10907 |
FUNCTION: BINDS DIRECTLY TO THE CENTRAL DOMAIN OF 16S RIBOSOMAL
RNA.
FUNCTION: PROTEIN S8 IS ALSO A TRANSLATIONAL REPRESSOR PROTEIN, IT
CONTROLS THE TRANSLATION OF THE SPC OPERON BY BINDING TO ITS MRNA.
MASS SPECTROMETRY: MW=13993.2; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S8P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplF | b3305 | 50S ribosomal subunit protein L6 |
EG10869 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 23S RIBOSOMAL RNA AND IS
LOCATED AT THE AMINOACYL-TRNA BINDING SITE OF THE
PEPTIDYLTRANSFERASE CENTER.
MASS SPECTROMETRY: MW=18772.7; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L6P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplR | b3304 | 50S ribosomal subunit protein L18 |
EG10879 |
FUNCTION: THIS IS ONE OF 3 PROTEINS THAT MEDIATE THE ATTACHMENT OF
THE 5S RNA INTO THE LARGE RIBOSOMAL SUBUNIT.
MASS SPECTROMETRY: MW=12769.8; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L18P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsE | b3303 | 30S ribosomal subunit protein S5 |
EG10904 |
FUNCTION: PROTEIN S5 IS IMPORTANT IN THE ASSEMBLY AND FUNCTION OF
THE 30S RIBOSOMAL SUBUNIT.
MASS SPECTROMETRY: MW=17514.8; METHOD=MALDI.
MISCELLANEOUS: ALTERED S5 PROTEINS HAVE BEEN IDENTIFIED IN A GREAT
VARIETY OF MUTANTS. MUTATIONS IN S5 HAVE BEEN SHOWN TO INCREASE
TRANSLATIONAL ERROR FREQUENCIES.
SIMILARITY: BELONGS TO THE S5P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpmD | b3302 | 50S ribosomal subunit protein L30 |
EG10888 |
MASS SPECTROMETRY: MW=6410.3; METHOD=MALDI.
MISCELLANEOUS: THIS PROTEIN IS LOCATED NEAR THE GUANOSINE
TRIPHOSPHATASE CENTER OF THE 50S SUBUNIT.
SIMILARITY: BELONGS TO THE L30P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplO | b3301 | 50S ribosomal subunit protein L15 |
EG10876 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 23S RIBOSOMAL RNA.
MASS SPECTROMETRY: MW=14980.1; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L15P FAMILY OF RIBOSOMAL PROTEINS.
|
| | prlA | b3300 | putative ATPase subunit of translocase |
EG10766 |
FUNCTION: INVOLVED IN PROTEIN EXPORT. INTERACTS WITH SECA AND SECE
TO ALLOW THE TRANSLOCATION OF PROTEINS ACROSS THE PLASMA MEMBRANE,
BY FORMING PART OF A CHANNEL.
SUBUNIT: ONE OF SEVEN SECRETORY PROTEINS (SECA-F & SECY) THAT
COMPRISE THE PROKARYOTIC PROTEIN TRANSLOCATION APPARATUS.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE SECY/SEC61-ALPHA FAMILY.
|
| | rpmJ | b3299 | 50S ribosomal subunit protein L36 |
EG11232 |
MASS SPECTROMETRY: MW=4364.2; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L36P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsM | b3298 | 30S ribosomal subunit protein S13 |
EG10912 |
FUNCTION: INVOLVED IN THE BINDING OF FMET-TRNA AND, HENCE, IN THE
INITIATION OF TRANSLATION.
MASS SPECTROMETRY: MW=12968.1; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S13P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsK | b3297 | 30S ribosomal subunit protein S11 |
EG10910 |
FUNCTION: S11 PLAYS AN ESSENTIAL ROLE FOR THE SELECTION OF THE
CORRECT TRNA IN PROTEIN BIOSYNTHESIS. IT IS LOCATED ON THE LARGE
LOBE OF THE SMALL SUBUNIT.
MASS SPECTROMETRY: MW=13727.7; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S11P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsD | b3296 | 30S ribosomal subunit protein S4 |
EG10903 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 16S RIBOSOMAL RNA.
FUNCTION: PROTEIN S4 IS ALSO A TRANSLATIONAL REPRESSOR PROTEIN, IT
CONTROLS THE TRANSLATION OF THE ALPHA-OPERON (WHICH CODES FOR S13,
S11, S4, RNA POLYMERASE ALPHA SUBUNIT, AND L17) BY BINDING TO ITS
MRNA.
MASS SPECTROMETRY: MW=23339.5; METHOD=MALDI.
MISCELLANEOUS: MUTATIONS IN S4 HAVE BEEN SHOWN TO INCREASE
TRANSLATIONAL ERROR FREQUENCIES.
SIMILARITY: CONTAINS 1 S4 RNA-BINDING DOMAIN.
SIMILARITY: BELONGS TO THE S4P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpoA | b3295 | RNA polymerase, alpha subunit |
EG10893 |
FUNCTION: DNA-DEPENDENT RNA POLYMERASE CATALYZES THE TRANSCRIPTION
OF DNA INTO RNA USING THE FOUR RIBONUCLEOSIDE TRIPHOSPHATES AS
SUBSTRATES. THIS SUBUNIT PLAYS AN IMPORTANT ROLE IN SUBUNIT
ASSEMBLY SINCE ITS DIMERIZATION IS THE FIRST STEP IN THE
SEQUENTIAL ASSEMBLY OF SUBUNITS TO FORM THE HOLOENZYME.
CATALYTIC ACTIVITY: N NUCLEOSIDE TRIPHOSPHATE = N PYROPHOSPHATE +
RNA(N).
SUBUNIT: CONSISTS OF A SIGMA FACTOR AND THE RNAP CORE ENZYME WHICH
IS COMPOSED OF 2 ALPHA CHAINS, 1 BETA CHAIN, 1 BETA' CHAIN AND 1
OMEGA CHAIN.
DOMAIN: THE AMINO-TERMINAL PORTION IS INVOLVED IN THE ASSEMBLY OF
CORE RNAP, WHEREAS THE C-TERMINAL IS INVOLVED IN INTERACTION WITH
TRANSCRIPTIONAL REGULATORS.
MISCELLANEOUS: BOTH MUTANTS RPOA101 AND RPOA112 ARE TEMPERATURE-
SENSITIVE. RPOA112 ALSO BLOCKS ASSEMBLY OF THE RNA POLYMERASE.
SIMILARITY: BELONGS TO THE RNA POLYMERASE ALPHA CHAIN FAMILY.
|
| | rplQ | b3294 | 50S ribosomal subunit protein L17 |
EG10878 |
MASS SPECTROMETRY: MW=14364.7; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L17P FAMILY OF RIBOSOMAL PROTEINS.
|
| | yhdN | b3293 | orf, hypothetical protein |
EG11970 |
|
| | yhdM | b3292 | putative transcriptional regulator |
EG11969 |
FUNCTION: ZN(II)-RESPONSIVE TRANSCRIPTIONAL REGULATOR OF ZNTA.
SIMILARITY: BELONGS TO THE MERR FAMILY OF TRANSCRIPTIONAL
REGULATORS. STRONG, TO H.INFLUENZAE ZNTR.
|
| 2.484257 | + | cmk | b0910 | cytidylate kinase |
EG11265 |
FUNCTION: ATP, DATP, AND GTP ARE EQUALLY EFFECTIVE AS PHOSPHATE
DONORS. CMP AND DCMP ARE THE BEST PHOSPHATE ACCEPTORS.
CATALYTIC ACTIVITY: ATP + CMP = ADP + CDP.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE CYTIDYLATE KINASE FAMILY. SUBFAMILY 1.
|
| | rpsA | b0911 | 30S ribosomal subunit protein S1 |
EG10900 |
FUNCTION: BINDS MRNA; THUS FACILITATING RECOGNITION OF THE
INITIATION POINT. IT IS NEEDED TO TRANSLATE MRNA WITH A SHORT
SHINE-DALGARNO (SD) PURINE-RICH SEQUENCE.
PTM: PHOSPHORYLATED; PROBABLY ON A SERINE.
SIMILARITY: BELONGS TO THE S1P FAMILY OF RIBOSOMAL PROTEINS.
SIMILARITY: CONTAINS 6 'S1 MOTIF' DOMAINS.
|
| 2.449655 | - | rnd | b1804 | RNase D, processes tRNA precursor |
EG10858 |
FUNCTION: CLEAVES MULTIMERIC TRNA PRECURSOR AT THE SPACER REGION.
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE TO 5'-PHOSPHO-
MONOESTER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
|
| 2.068578 | - | rph | b3643 | RNase PH |
EG10863 |
FUNCTION: RNASE PH IS A PHOSPHOROLYTIC EXORIBONUCLEASE THAT
REMOVES NUCLEOTIDE RESIDUES FOLLOWING THE -CCA TERMINUS OF TRNA
AND ADDS NUCLEOTIDES TO THE ENDS OF RNA MOLECULES BY USING
NUCLEOSIDE DIPHOSPHATES AS SUBSTRATES. ALSO ACTS TO REGULATE THE
ATTENUATION OF PYRE.
CATALYTIC ACTIVITY: TRNA(N+1) + ORTHOPHOSPHATE = TRNA(N) +
A NUCLEOSIDE DIPHOSPHATE.
SIMILARITY: BELONGS TO THE RNASE PH FAMILY.
|
| | pyrE | b3642 | orotate phosphoribosyltransferase |
EG10808 |
CATALYTIC ACTIVITY: OROTIDINE-5'-PHOSPHATE + PYROPHOSPHATE =
OROTATE + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE.
PATHWAY: FIFTH STEP IN PYRIMIDINE BIOSYNTHESIS.
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO THE PURINE/PYRIMIDINE
PHOSPHORIBOSYLTRANSFERASE FAMILY.
|
| 1.802587 | + | yecF | b1915 | orf, hypothetical protein |
EG12861 |
CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO
FRAMESHIFTS.
|
| 1.582149 | - | yeaZ | b1807 | orf, hypothetical protein |
EG13512 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0388.
SIMILARITY: SOME, TO PEPTIDASE FAMILY M22; ALSO KNOWN AS THE
GLYCOPROTEASE FAMILY.
|
| | b1806 | b1806 | putative outer membrane protein |
|
|
| 1.503941 | + | argS | b1876 | arginine tRNA synthetase |
EG10071 |
CATALYTIC ACTIVITY: ATP + L-ARGININE + TRNA(ARG) = AMP +
PYROPHOSPHATE + L-ARGINYL-TRNA(ARG).
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY.
|
| 1.449027 | + | b1626 | b1626 | orf, hypothetical protein |
EG13932 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: TO SYNECHOCYSTIS PCC 6803 SLL0481.
|
| | b1627 | b1627 | orf, hypothetical protein |
|
|
| | b1628 | b1628 | orf, hypothetical protein |
EG13934 |
SIMILARITY: BELONGS TO THE 4FE4S BACTERIAL-TYPE FERREDOXIN FAMILY.
STRONG, TO H.INFLUENZAE HI1684.
|
| | b1629 | b1629 | putative membrane protein |
|
|
| | ydgO | b1630 | orf, hypothetical protein |
EG13936 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE RNFD FAMILY. STRONG, TO H.INFLUENZAE
HI1686.
|
| | b1631 | b1631 | orf, hypothetical protein |
EG13937 |
SIMILARITY: BELONGS TO THE RNFG FAMILY. STRONG, TO H.INFLUENZAE
HI1687.
|
| | ydgQ | b1632 | orf, hypothetical protein |
EG13938 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: STRONG, TO H.INFLUENZAE HI1688.
SIMILARITY: TO H.INFLUENZAE HI0168.
|
| | nth | b1633 | endonuclease III; specific for apurinic and/or apyrimidinic sites |
EG10662 |
FUNCTION: HAS BOTH AN APURINIC AND/OR APYRIMIDINIC ENDONUCLEASE
ACTIVITY AND A DNA N-GLYCOSYLASE ACTIVITY. INCISES DAMAGED DNA AT
CYTOSINES, THYMINES AND GUANINES. ACTS ON A DAMAGED STRAND, 5'
FROM THE DAMAGED SITE. REQUIRED FOR THE REPAIR OF BOTH OXIDATIVE
DNA DAMAGE AND SPONTANEOUS MUTAGENIC LESIONS.
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE NEAR APURINIC OR
APYRIMIDINIC SITES TO PRODUCTS WITH 5'-PHOSPHATE.
COFACTOR: BINDS A 4FE-4S CLUSTER WHICH IS NOT IMPORTANT FOR THE
CATALYTIC ACTIVITY, BUT WHICH IS PROBABLY INVOLVED IN THE PROPER
POSITIONING OF THE ENZYME ALONG THE DNA STRAND.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE NTH/MUTY FAMILY.
|
| 1.347144 | + | rhsD | b0497 | rhsD protein in rhs element |
EG10849 |
FUNCTION: RHS ELEMENTS HAVE A NONESSENTIAL FUNCTION. THEY MAY
PLAY AN IMPORTANT ROLE IN THE NATURAL ECOLOGY OF THE CELL.
DOMAIN: EACH RHS APPEARS TO CONSIST OF A HIGHLY CONSERVED 141 KDA
AMINO FRAGMENT FOLLOWED BY A HIGHLY DIVERGENT CARBOXY TERMINUS.
SIMILARITY: BELONGS TO THE RHS FAMILY.
|
| | ybbC | b0498 | orf, hypothetical protein |
EG11769 |
|
| | b0499 | b0499 | orf, hypothetical protein |
|
|
| | ybbD | b0500 | orf, hypothetical protein |
EG11770 |
|
| | b0501 | b0501 | orf, hypothetical protein |
|
|
| 1.320443 | + | yicC | b3644 | putative alpha helix protein |
EG11192 |
MISCELLANEOUS: ESSENTIAL FOR E.COLI UNDER SPECIAL GROWTH
CONDITION.
SIMILARITY: STRONG, TO H.INFLUENZAE HI0467.
|
| 1.163164 | - | ybjH | b0843 | orf, hypothetical protein |
EG13677 |
|
| 1.067365 | - | yiaT | b3584 | putative outer membrane protein |
EG12288 |
SUBCELLULAR LOCATION: OUTER MEMBRANE (POTENTIAL).
SIMILARITY: BELONGS TO THE MIPA/OMPV FAMILY.
|
| 0.986415 | + | pphB | b2734 | protein phosphatase 2 |
EG13102 |
FUNCTION: HAS BEEN SHOWN, IN VITRO, TO ACT ON SER, THR AND
TYR-PHOSPHORYLATED SUBSTRATES.
CATALYTIC ACTIVITY: A PHOSPHOPROTEIN + H(2)O = A PROTEIN +
ORTHOPHOSPHATE.
SIMILARITY: BELONGS TO THE PPP FAMILY OF PHOSPHATASES.
|
| 0.950705 | - | purC | b2476 | phosphoribosylaminoimidazole-succinocarboxamide synthetase = SAICAR synthetase |
EG10791 |
CATALYTIC ACTIVITY: ATP + 1-(5-PHOSPHORIBOSYL)-4-CARBOXY-5-
AMINOIMIDAZOLE + L-ASPARTATE = ADP + ORTHOPHOSPHATE + 1-(5-
PHOSPHORIBOSYL)-4-(N-SUCCINO-CARBOXAMIDE)-5-AMINOIMIDAZOLE.
PATHWAY: SEVENTH STEP IN DE NOVO PURINE BIOSYNTHESIS.
SUBUNIT: HOMOTRIMER.
SIMILARITY: BELONGS TO THE SAICAR SYNTHETASE FAMILY.
|
| 0.944338 | - | menF | b2265 | isochorismate hydroxymutase 2, menaquinone biosynthesis |
EG12362 |
CATALYTIC ACTIVITY: CHORISMATE = ISOCHORISMATE.
PATHWAY: MENAQUINONE BIOSYNTHESIS.
SIMILARITY: STRONG, TO OTHER ISOCHORISMATE SYNTHASES; WEAK, TO
TRPE AND PABB.
CAUTION: REF.7 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO
FRAMESHIFTS.
|
| | menD | b2264 | 2-oxoglutarate decarboxylase; SHCHC synthase |
EG10579 |
CATALYTIC ACTIVITY: ISOCHORISMATE + 2-KETOGLUTARATE =
2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE + PYRUVATE
+ CO(2).
CATALYTIC ACTIVITY: 2-OXOGLUTARATE = SUCCINATE SEMIALDEHYDE +
CO(2).
COFACTOR: THIAMINE PYROPHOSPHATE.
PATHWAY: FIRST STEP OF MENAQUINONE BIOSYNTHESIS.
INDUCTION: BY ISOPROPYL-BETA-D-THIOGALACTOSIDE (IPTG).
SIMILARITY: WITH OTHER ENZYMES WHICH REQUIRE TPP.
CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN IN THE C-TERMINUS
AND IS SHORTER (395 AA) DUE TO A FRAMESHIFT.
|
| | yfbB | b2263 | putative enzyme |
EG12438 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0282.
CAUTION: REF.1 AND REF.4 SEQUENCES DIFFER FROM THAT SHOWN DUE TO A
FRAMESHIFT IN POSITION 182.
|
| | menB | b2262 | dihydroxynaphtoic acid synthetase |
EG11368 |
FUNCTION: CONVERT O-SUCCINYLBENZOYL-COA (OSB-COA) TO 1,4-
DIHYDROXY-2-NAPHTHOIC ACID (DHNA).
CATALYTIC ACTIVITY: O-SUCCINYLBENZOYL-COA = 1,4-DIHYDROXY-2-
NAPHTHOATE + COA.
PATHWAY: MENAQUINONE BIOSYNTHESIS.
SIMILARITY: BELONGS TO THE ENOYL-COA HYDRATASE/ISOMERASE FAMILY.
|
| | menC | b2261 | o-succinylbenzoyl-CoA synthase; conversion of chorismate to 2-o-succinylbenzoyl-CoA |
EG11532 |
FUNCTION: CONVERTS SHCHC TO OSB.
CATALYTIC ACTIVITY: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-
CARBOXYLATE = O-SUCCINYLBENZOATE + H(2)O.
PATHWAY: MENAQUINONE BIOSYNTHESIS.
|
| | menE | b2260 | o-succinylbenzoate-CoA ligase |
EG12437 |
FUNCTION: O-SUCCINYLBENZOIC ACID (OSB) TO O-SUCCINYLBENZOYL-COA
(OSB-COA).
CATALYTIC ACTIVITY: ATP + O-SUCCINYLBENZOATE + COA = AMP +
PYROPHOSPHATE + O-SUCCINYLBENZOYL-COA.
PATHWAY: MENAQUINONE BIOSYNTHESIS.
SIMILARITY: BELONGS TO THE ATP-DEPENDENT AMP-BINDING ENZYME
FAMILY.
|
| | pmrD | b2259 | polymyxin resistance protein B |
EG12671 |
FUNCTION: CONFERS RESISTANCE TO POLYMYXIN B. POLYMYXIN RESISTANCE
MAY BE MEDIATED BY AN INTERACTION BETWEEN PMRA OR A PMRA-REGULATED
GENE PRODUCT AND PMRD (BY SIMILARITY).
|
| 0.907887 | - | yecM | b1875 | orf, hypothetical protein |
EG13405 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI1582/HI1581.
CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A
FRAMESHIFT IN POSITION 128 THAT PRODUCES TWO SEPARATE ORFS.
|
| 0.860682 | + | narG | b1224 | nitrate reductase 1, alpha subunit |
EG10638 |
FUNCTION: THE NITRATE REDUCTASE ENZYME COMPLEX ALLOWS E.COLI
TO USE NITRATE AS AN ELECTRON ACCEPTOR DURING ANAEROBIC GROWTH.
FUNCTION: THE ALPHA CHAIN IS THE ACTUAL SITE OF NITRATE REDUCTION.
CATALYTIC ACTIVITY: NITRITE + ACCEPTOR = NITRATE + REDUCED
ACCEPTOR.
COFACTOR: MOLYBDENUM (MOLYBDOPTERIN); MAY BIND A 4FE-4S CLUSTER.
SUBUNIT: TETRAMER COMPOSED OF AN ALPHA, A BETA AND 2 GAMMA CHAINS.
ALPHA AND BETA ARE CATALYTIC CHAINS; GAMMA CHAINS ARE INVOLVED IN
BINDING THE ENZYME COMPLEX TO THE CYTOPLASMIC MEMBRANE.
SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED.
INDUCTION: BY NITRATE.
SIMILARITY: BELONGS TO THE PROKARYOTIC MOLYBDOPTERIN-CONTAINING
OXIDOREDUCTASE FAMILY. STRONG, TO NARZ.
DATABASE: NAME=Worthington enzyme manual;
WWW="http://www.worthington-biochem.com/manual/N/NAR.html".
|
| | narH | b1225 | nitrate reductase 1, beta subunit |
EG10647 |
FUNCTION: THIS IS A SECOND NITRATE REDUCTASE ENZYME WHICH CAN
SUBSTITUTE FOR THE NRA ENZYME AND ALLOWS E.COLI TO USE NITRATE
AS AN ELECTRON ACCEPTOR DURING ANAEROBIC GROWTH.
THE BETA CHAIN IS AN ELECTRON TRANSFER UNIT CONTAINING FOUR
CYSTEINE CLUSTERS INVOLVED IN THE FORMATION OF IRON-SULFUR
CENTRES. ELECTRONS ARE TRANSFERRED FROM THE GAMMA CHAIN TO THE
MOLYBDENUM COFACTOR OF THE ALPHA SUBUNIT.
CATALYTIC ACTIVITY: NITRITE + ACCEPTOR = NITRATE + REDUCED
ACCEPTOR.
SUBUNIT: TETRAMER COMPOSED OF AN ALPHA, A BETA AND 2 GAMMA CHAINS.
ALPHA AND BETA ARE CATALYTIC CHAINS; GAMMA CHAINS ARE INVOLVED IN
BINDING THE ENZYME COMPLEX TO THE CYTOPLASMIC MEMBRANE.
SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED.
SIMILARITY: 75% IDENTITY TO NARH (THE BETA CHAIN OF THE FIRST
E.COLI NITRATE REDUCTASE ENZYME).
|
| | narJ | b1226 | nitrate reductase 1, delta subunit, assembly function |
EG10641 |
FUNCTION: REQUIRED FOR THE ASSEMBLY OF THE NITRATE REDUCTASE-
CYTOCHROME B-NR COMPLEX TO BE FULLY ACTIVE IN THE MEMBRANE.
CATALYTIC ACTIVITY: NITRITE + ACCEPTOR = NITRATE + REDUCED
ACCEPTOR.
SIMILARITY: 69% IDENTITY TO NARW (THE DELTA CHAIN OF THE SECOND
E.COLI NITRATE REDUCTASE ENZYME).
|
| | narI | b1227 | nitrate reductase 1, cytochrome b(NR), gamma subunit |
EG10640 |
FUNCTION: THE NITRATE REDUCTASE ENZYME COMPLEX ALLOWS E.COLI TO
USE NITRATE AS AN ELECTRON ACCEPTOR DURING ANAEROBIC GROWTH.
FUNCTION: THE GAMMA CHAIN IS A MEMBRANE-EMBEDDED HEME-IRON UNIT
RESEMBLING CYTOCHROME B, WHICH TRANSFERS ELECTRONS FROM QUINONES
TO THE BETA SUBUNIT.
CATALYTIC ACTIVITY: NITRITE + ACCEPTOR = NITRATE + REDUCED
ACCEPTOR.
SUBUNIT: TETRAMER COMPOSED OF AN ALPHA, A BETA AND 2 GAMMA CHAINS.
ALPHA AND BETA ARE CATALYTIC CHAINS; GAMMA CHAINS ARE INVOLVED IN
BINDING THE ENZYME COMPLEX TO THE CYTOPLASMIC MEMBRANE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
INDUCTION: BY NITRATE.
SIMILARITY: 86% IDENTITY TO NARV (THE GAMMA CHAIN OF THE SECOND
E.COLI NITRATE REDUCTASE ENZYME).
DATABASE: NAME=Worthington enzyme manual;
WWW="http://www.worthington-biochem.com/manual/N/NAR.html".
|
| 0.831990 | - | lepA | b2569 | GTP-binding elongation factor, may be inner membrane protein |
EG10529 |
SUBCELLULAR LOCATION: PRESENT IN THE CYTOPLASMIC MEMBRANE AND IS
ALSO FOUND IN THE PERIPLASM.
MISCELLANEOUS: THE OVERPRODUCTION OF THIS PROTEIN IS LETHAL TO
E.COLI.
SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY.
LEPA SUBFAMILY.
|
| | lepB | b2568 | leader peptidase (signal peptidase I) |
EG10530 |
CATALYTIC ACTIVITY: CLEAVAGE OF N-TERMINAL LEADER SEQUENCES FROM
SECRETED AND PERIPLASMIC PROTEINS PRECURSOR.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S26; ALSO KNOWN AS TYPE
I LEADER PEPTIDASE FAMILY.
|
| 0.786803 | - | sbcD | b0398 | ATP-dependent dsDNA exonuclease |
EG11094 |
FUNCTION: AFFECTS GENETIC RECOMBINATION AND THE VIABILITY OF
DNA PALINDROMES IN E.COLI. SBCD MAY HAVE A NUCLEASE ACTIVITY THAT
IS FUNCTIONALLY RELATED TO ONE OF THE NUCLEASE ACTIVITIES OF THE
RECBCD ENZYME.
SIMILARITY: BELONGS TO THE SBCD FAMILY.
|
| | sbcC | b0397 | ATP-dependent dsDNA exonuclease |
EG10927 |
FUNCTION: AFFECTS GENETIC RECOMBINATION AND THE VIABILITY OF
DNA PALINDROMES IN E.COLI. SBCC MAY HAVE A NUCLEASE ACTIVITY THAT
IS FUNCTIONALLY RELATED TO ONE OF THE NUCLEASE ACTIVITIES OF THE
RECBCD ENZYME.
SIMILARITY: TO PHAGE T4 GENE 46 PROTEIN AND PHAGE T5 D13 AND TO
UVRA/RECC.
|
| | araJ | b0396 | involved in either transport or processing of arabinose polymers |
EG10060 |
FUNCTION: MAY BE INVOLVED IN EITHER THE TRANSPORT OR PROCESSING
OF ARABINOSE POLYMERS.
INDUCTION: BY ARABINOSE.
|
| 0.686636 | - | b2462 | b2462 | orf, hypothetical protein |
EG14192 |
FUNCTION: MAY BE INVOLVED IN THE FORMATION OF A SPECIFIC
MICROCOMPARTIMENT IN THE CELL IN WHICH THE METABOLISM OF
POTENTIALLY TOXIC BY-PRODUCTS TAKES PLACE.
PATHWAY: ETHANOLAMINE UTILIZATION.
SIMILARITY: DISTANTLY RELATED TO THE CCHA/CCMK/CSOS1/PDUA FAMILY.
|
| | b2461 | b2461 | orf, hypothetical protein |
EG14191 |
PATHWAY: ETHANOLAMINE UTILIZATION.
SIMILARITY: BELONGS TO THE EUTP/PDUV FAMILY.
|
| | b2460 | b2460 | orf, hypothetical protein |
EG14190 |
PATHWAY: ETHANOLAMINE UTILIZATION.
|
| | b2459 | b2459 | orf, hypothetical protein |
EG14189 |
FUNCTION: CONVERTS CNB12 TO ADOB12 (BY SIMILARITY).
CATALYTIC ACTIVITY: ATP + COB(I)ALAMIN + H(2)O = ORTHOPHOSPHATE +
PYROPHOSPHATE + ADENOSYLCOBALAMIN.
PATHWAY: ETHANOLAMINE UTILIZATION.
|
| | eutI | b2458 | ethanolamine utilization; homolog of Salmonella acetyl/butyryl P transferase |
EG14188 |
PATHWAY: ETHANOLAMINE UTILIZATION.
SIMILARITY: BELONGS TO THE PHOSPHATE ACETYLTRANSFERASE AND
BUTYRYLTRANSFERASE FAMILY.
|
| | cchA | b2457 | detox protein |
EG14187 |
FUNCTION: MAY BE INVOLVED IN THE FORMATION OF A SPECIFIC
MICROCOMPARTIMENT IN THE CELL IN WHICH THE METABOLISM OF
POTENTIALLY TOXIC BY-PRODUCTS TAKES PLACE.
PATHWAY: ETHANOLAMINE UTILIZATION.
SIMILARITY: BELONGS TO THE CCHA/CCMK/CSOS1/PDUA FAMILY.
|
| | cchB | b2456 | detox protein |
EG14186 |
FUNCTION: MAY BE INVOLVED IN THE FORMATION OF A SPECIFIC
MICROCOMPARTIMENT IN THE CELL IN WHICH THE METABOLISM OF
POTENTIALLY TOXIC BY-PRODUCTS TAKES PLACE.
PATHWAY: ETHANOLAMINE UTILIZATION.
SIMILARITY: TO CYANOBACTERIAL CARBON DIOXIDE CONCENTRATING
MECHANISM PROTEIN CCML.
|
| | eutE | b2455 | ethanolamine utilization; similar to acetaldehyde dehydrogenase |
EG14185 |
FUNCTION: MAY ACT AS AN ACETALDEHYDE DEHYDROGENASE THAT CONVERTS
ACETALDEHYDE INTO ACETYL-COA.
PATHWAY: ETHANOLAMINE UTILIZATION.
SIMILARITY: TO THE N-TERMINAL OF E.COLI AND C.ACETOBUTYLICUM ADHE.
|
| | eutJ | b2454 | ethanolamine utilization; homolog of Salmonella gene |
EG14184 |
PATHWAY: ETHANOLAMINE UTILIZATION.
|
| | eutG | b2453 | ethanolamine utilization; homolog of Salmonella enzyme, similar to iron-containing alcohol dehydrogenase |
EG14183 |
FUNCTION: MAY ACT ON THE ACETALDEHYDE PRODUCED FROM THE
DEGRADATION OF ETHANOLAMINE.
PATHWAY: ETHANOLAMINE UTILIZATION.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE IRON-CONTAINING ALCOHOL DEHYDROGENASE
FAMILY.
|
| 0.684624 | + | rstA | b1608 | response transcriptional regulatory protein (RstB sensor) |
EG13190 |
FUNCTION: MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM RSTB/RSTA.
SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL).
PTM: PHOSPHORYLATED BY RSTB (POTENTIAL).
SIMILARITY: TO OTHER BACTERIAL REGULATORY PROTEINS INVOLVED IN
SIGNAL TRANSDUCTION.
|
| | rstB | b1609 | sensor histidine protein kinase (RstA regulator) |
EG11233 |
FUNCTION: MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM RSTB/RSTA.
RSTB FUNCTIONS AS A MEMBRANE-ASSOCIATED PROTEIN KINASE THAT
PHOSPHORYLATES RSTA (POTENTIAL).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: TO OTHER PROKARYOTIC SENSORY TRANSDUCTION HISTIDINE
KINASES.
|
| | tus | b1610 | DNA-binding protein; inhibition of replication at Ter sites |
EG11038 |
FUNCTION: TRANS-ACTING PROTEIN REQUIRED FOR TERMINATION OF DNA
REPLICATION IN ESCHERICHIA COLI. BINDS TO DNA REPLICATION
TERMINATOR SEQUENCES (TERA TO TERF) TO PREVENT THE PASSAGE OF
REPLICATION FORKS. THE TERMINATION EFFICIENCY WILL BE AFFECTED BY
THE AFFINITY OF THIS PROTEIN FOR THE TERMINATOR SEQUENCE.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
|
| 0.681144 | + | mutT | b0099 | 7,8-dihydro-8-oxoguanine-triphosphatase, prefers dGTP, causes AT-GC transversions |
EG10626 |
FUNCTION: INVOLVED IN THE GO SYSTEM RESPONSIBLE FOR REMOVING AN
OXIDATIVELY DAMAGED FORM OF GUANINE (7,8-DIHYDRO-8-OXOGUANINE)
FROM DNA AND THE NUCLEOTIDE POOL. 8-OXO-DGTP IS INSERTED OPPOSITE
DA AND DC RESIDUES OF TEMPLATE DNA WITH ALMOST EQUAL EFFICIENCY
THUS LEADING TO A.T TO G.C TRANSVERSIONS. MUTT SPECIFICALLY
DEGRADES 8-OXO-DGTP TO THE MONOPHOSPHATE.
CATALYTIC ACTIVITY: 8-OXO-DGTP + H(2)O = 8-OXO-DGMP +
PYROPHOSPHATE.
COFACTOR: REQUIRES MAGNESIUM.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE NUDIX HYDROLASE FAMILY.
|
| 0.669544 | - | b1963 | b1963 | orf, hypothetical protein |
EG14041 |
|
| | yedJ | b1962 | orf, hypothetical protein |
EG12710 |
SIMILARITY: TO B.SUBTILIS YPGQ.
|
| | dcm | b1961 | DNA cytosine methylase |
EG10211 |
FUNCTION: THIS METHYLASE RECOGNIZES THE DOUBLE-STRANDED SEQUENCE
CCWGG, CAUSES SPECIFIC METHYLATION ON C-2 ON BOTH STRANDS.
CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE + DNA CYTOSINE =
S-ADENOSYL-L-HOMOCYSTEINE + DNA 5-METHYLCYTOSINE.
SIMILARITY: STRONG, TO OTHER C5-DNA METHYLASES.
|
| | vsr | b1960 | DNA mismatch endonuclease, patch repair protein |
EG11068 |
FUNCTION: DEAMINATION OF 5-METHYLCYTOSINE IN DNA RESULTS IN T/G
MISMATCHES. IF UNREPAIRED, THESE MISMATCHES CAN LEAD TO C-TO-T
TRANSITION MUTATIONS. THE VERY SHORT PATCH (VSP) REPAIR PROCESS
IN E.COLI COUNTERACTS THE MUTAGENIC PROCESS BY REPAIRING THE
MISMATCHES IN FAVOR OF THE G-CONTAINING STRAND. THIS ENZYME IS AN
ENDONUCLEASE THAT NICKS DOUBLE-STRANDED DNA WITHIN THE SEQUENCE
CT(AT)GN OR NT(AT)GG NEXT TO THE THYMIDINE RESIDUE, WHICH IS
MISMATCHED TO 2'-DEOXYGUANOSINE. THE INCISION IS MISMATCH-
DEPENDENT AND STRAND SPECIFIC.
SIMILARITY: BELONGS TO THE VSR FAMILY.
|
| 0.663303 | + | fimD | b4317 | outer membrane protein; export and assembly of type 1 fimbriae, interrupted |
EG10311 |
FUNCTION: INVOLVED IN THE EXPORT AND ASSEMBLY OF FIMA FIMBRIAL
SUBUNITS ACROSS THE OUTER MEMBRANE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. OUTER MEMBRANE
(BY SIMILARITY).
SIMILARITY: BELONGS TO THE FIMBRIAL EXPORT USHER FAMILY.
|
| | fimF | b4318 | fimbrial morphology |
EG10313 |
FUNCTION: INVOLVED IN REGULATION OF LENGTH AND MEDIATION OF
ADHESION OF TYPE 1 FIMBRIAE (BUT NOT NECESSARY FOR THE PRODUCTION
OF FIMBRIAE). INVOLVED IN THE INTEGRATION OF FIMH IN THE FIMBRIAE.
SIMILARITY: TO TYPE-1 FIMBRIAL SUBUNITS.
|
| | fimG | b4319 | fimbrial morphology |
EG10314 |
FUNCTION: INVOLVED IN REGULATION OF LENGTH AND MEDIATION OF
ADHESION OF TYPE 1 FIMBRIAE (BUT NOT NECESSARY FOR THE PRODUCTION
OF FIMBRIAE). INVOLVED IN THE INTEGRATION OF FIMH IN THE FIMBRIAE.
SIMILARITY: TO TYPE-1 FIMBRIAL SUBUNITS.
|
| | fimH | b4320 | minor fimbrial subunit, D-mannose specific adhesin |
EG10315 |
FUNCTION: INVOLVED IN REGULATION OF LENGTH AND MEDIATION OF
ADHESION OF TYPE 1 FIMBRIAE (BUT NOT NECESSARY FOR THE PRODUCTION
OF FIMBRIAE). ADHESIN RESPONSIBLE FOR THE BINDING TO D-MANNOSE. IT
IS LATERALLY POSITIONED AT INTERVALS IN THE STRUCTURE OF THE TYPE
1 FIMBRIAE. IN ORDER TO INTEGRATE FIMH IN THE FIMBRIAE FIMF AND
FIMG ARE NEEDED.
SIMILARITY: THIS PROTEIN EXHIBITS HOMOLOGY WITH THE FIMBRIAL
SUBUNIT PROTEIN FIMA.
|
| 0.654164 | + | pheA | b2599 | chorismate mutase-P and prephenate dehydratase |
EG10707 |
CATALYTIC ACTIVITY: CHORISMATE = PREPHENATE.
CATALYTIC ACTIVITY: PREPHENATE = PHENYLPYRUVATE + H(2)O + CO(2).
PATHWAY: L-PHENYLALANINE BIOSYNTHESIS.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: TO OTHER PDT ENZYMES OR DOMAINS.
|
| 0.645865 | + | yiaU | b3585 | putative transcriptional regulator LYSR-type |
EG12289 |
SIMILARITY: BELONGS TO THE LYSR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.639700 | + | ydaL | b1340 | orf, hypothetical protein |
EG13354 |
|
| 0.638790 | + | adk | b0474 | adenylate kinase activity; pleiotropic effects on glycerol-3-phosphate acyltransferase activity |
EG10032 |
FUNCTION: THIS SMALL UBIQUITOUS ENZYME IS ESSENTIAL FOR
MAINTENANCE AND CELL GROWTH.
CATALYTIC ACTIVITY: ATP + AMP = ADP + ADP.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ADENYLATE KINASE FAMILY.
|