Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 1.977471 | + | b0846 | b0846 | putative DEOR-type transcriptional regulator |
 |
|
| 0.877750 | - | yfgB | b2517 | orf, hypothetical protein |
EG12401 |
SIMILARITY: BELONGS TO THE UPF0063 FAMILY. STRONG, TO H.INFLUENZAE
HI0365.
|
| 0.579841 | + | ybbI | b0487 | putative transcriptional regulator |
EG13256 |
FUNCTION: REGULATES THE TRANSCRIPTION OF THE COPA GENE.
SIMILARITY: BELONGS TO THE MERR FAMILY OF TRANSCRIPTIONAL
REGULATORS. STRONG, TO H.INFLUENZAE HI0293.
|
| 0.532789 | + | fliO | b1947 | flagellar biosynthesis |
EG11224 |
SUBCELLULAR LOCATION: MEMBRANE-ASSOCIATED (POTENTIAL).
SIMILARITY: BELONGS TO THE FLIO/MOPB FAMILY.
|
| | fliP | b1948 | flagellar biosynthesis |
EG11975 |
FUNCTION: PLAYS A ROLE IN THE FLAGELLUM-SPECIFIC TRANSPORT SYSTEM.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
SIMILARITY: BELONGS TO THE FLIP/MOPC/SPAP FAMILY.
|
| | fliQ | b1949 | flagellar biosynthesis |
EG11976 |
FUNCTION: REQUIRED FOR THE ASSEMBLY OF THE RIVET AT THE EARLIEST
STAGE OF FLAGELLAR BIOSYNTHESIS.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
SIMILARITY: BELONGS TO THE FLIQ/MOPD/SPAQ FAMILY.
|
| | fliR | b1950 | flagellar biosynthesis |
EG11977 |
FUNCTION: ROLE IN FLAGELLAR BIOSYNTHESIS.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
SIMILARITY: BELONGS TO THE FLIR/MOPE/SPAR FAMILY.
|
| 0.420031 | - | b0845 | b0845 | putative DEOR-type transcriptional regulator |
|
|
| | b0844 | b0844 | orf, hypothetical protein |
EG13678 |
SIMILARITY: BELONGS TO THE COF/YBHA/YIDA/YIGL (E.COLI) / YCSE/YXEH
(B.SUBTILIS) FAMILY.
|
| | ybjH | b0843 | orf, hypothetical protein |
EG13677 |
|
| 0.355303 | + | ycdC | b1013 | putative tet operon regulator |
EG12301 |
SIMILARITY: BELONGS TO THE TETR/ACRR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.285397 | - | yhfZ | b3383 | orf, hypothetical protein |
EG12921 |
|
| | yhfY | b3382 | orf, hypothetical protein |
EG12920 |
SIMILARITY: TO H.INFLUENZAE HI0487.
|
| | yhfX | b3381 | orf, hypothetical protein |
EG12919 |
|
| | yhfW | b3380 | putative mutase |
EG12918 |
SIMILARITY: BELONGS TO THE PHOSPHOPENTOMUTASE FAMILY.
|
| | yhfV | b3379 | putative hydrolase |
EG12917 |
FUNCTION: ITS REAL ENZYMATIC ACTIVITY IS NOT YET KNOWN. IT WAS
TESTED FOR GENERAL ESTERASE, AMINOPEPTIDASE, SULFATASE,
PHOSPHATASE, CARBONIC ANHYDRASE, PHOSPHODIESTERASE, AND
PHOSPHOTRIESTERASE ACTIVITIES WITH THE FOLLOWING SUBSTRATES: P-
NITROPHENYL ACETATE, L-ALANINE NITROANILIDE, P-NITROPHENYL
SULFATE, BIS(P-NITROPHENYL) PHOSPHATE, PARAOXON, AND P-NITROPHENYL
PHOSPHATE. NO ENZYMATIC ACTIVITY WAS DETECTED WITH ANY OF THESE
NONSPECIFIC SUBSTRATES.
COFACTOR: CONTAINS 2 MOLES OF ZINC PER SUBUNIT.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE PHOSPHOTRIESTERASE FAMILY.
|
| | yhfU | b3378 | orf, hypothetical protein |
EG12916 |
|
| | yhfT | b3377 | putative transport system permease protein |
EG12915 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
|
| | yhfS | b3376 | orf, hypothetical protein |
EG12914 |
|
| 0.258052 | - | fepA | b0584 | outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D |
EG10293 |
FUNCTION: THIS PROTEIN IS INVOLVED IN THE INITIAL STEP OF IRON
UPTAKE BY BINDING FERRIENTEROBACTIN (FE-ENT), AN IRON CHELATIN
SIDEROPHORE THAT ALLOWS E.COLI TO EXTRACT IRON FROM THE
ENVIRONMENT. FEPA ALSO ACTS AS A RECEPTOR FOR COLICINS B AND D.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. OUTER MEMBRANE.
SIMILARITY: LOCAL TO OTHER TONB-DEPENDENT RECEPTOR PROTEINS.
|
| 0.257673 | + | b2866 | b2866 | orf, hypothetical protein |
|
|
| | ygeT | b2867 | putative dehydrogenase |
EG13050 |
SIMILARITY: SOME, TO VERTEBRATE XANTHINE DEHYDROGENASES.
|
| | b2868 | b2868 | putative dehydrogenase |
|
|
| 0.247270 | + | dgt | b0160 | deoxyguanosine triphosphate triphosphohydrolase |
EG10225 |
FUNCTION: DGTPASE PREFERENTIALLY HYDROLYZES DGTP OVER THE OTHER
CANONICAL NTPS.
CATALYTIC ACTIVITY: DGTP + H(2)O = DEOXYGUANOSINE + TRIPHOSPHATE.
SUBUNIT: HOMOTETRAMER.
SIMILARITY: BELONGS TO THE DGTPASE FAMILY.
CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN IN POSITIONS 89
TO 210 DUE TO A FRAMESHIFT.
|
| | htrA | b0161 | periplasmic serine protease Do; heat shock protein HtrA |
EG10463 |
FUNCTION: SERINE PROTEASE THAT IS REQUIRED AT HIGH TEMPERATURE.
INVOLVED IN THE DEGRADATION OF DAMAGED PROTEINS. IT CAN DEGRADES
ICIA, ADA, CASEIN AND GLOBIN. SHARED SPECIFICITY WITH DEGQ.
SUBUNIT: MULTIMERIC.
SUBCELLULAR LOCATION: PERIPLASMIC.
INDUCTION: HEAT SHOCK.
MISCELLANEOUS: HTRA IS INDISPENSABLE FOR BACTERIAL SURVIVAL AT
TEMPERATURES ABOVE 42 DEGREES CELSIUS.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S2C; ALSO KNOWN AS THE
DEGP/DEGQ/DEGS FAMILY.
SIMILARITY: CONTAINS 2 PDZ/DHR DOMAINS.
|
| | yaeG | b0162 | orf, hypothetical protein |
EG12335 |
FUNCTION: SEEMS TO REGULATE THE EXPRESSION OF THE OPERONS FOR THE
ENZYMES INVOLVED IN D-GALACTARATE, D-GLUCARATE AND D-GLYCERATE
UTILIZATION.
SIMILARITY: BELONGS TO THE CDAR FAMILY.
|
| 0.202385 | - | b2379 | b2379 | putative aminotransferase |
EG14198 |
COFACTOR: PYRIDOXAL PHOSPHATE (POTENTIAL).
SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| 0.199665 | + | sdaB | b2797 | L-serine dehydratase (deaminase), L-SD2 |
EG11623 |
FUNCTION: DEAMINATES ALSO THREONINE, PARTICULARLY WHEN IT IS
PRESENT IN HIGH CONCENTRATION.
CATALYTIC ACTIVITY: L-SERINE + H(2)O = PYRUVATE + NH(3) + H(2)O.
COFACTOR: IRON-SULFUR (4FE-4S) (PROBABLE).
PATHWAY: GLUCONEOGENESIS FROM SERINE.
INDUCTION: TRANSCRIBED IN RICH MEDIUM, PARTICULARLY IN THE
ABSENCE OF GLUCOSE, AND IS UNDER THE CONTROL OF CATABOLITE
ACTIVATOR PROTEIN. IT IS MADE AEROBICALLY AND ANAEROBICALLY.
PTM: IT IS MADE BY THE CELL IN AN INACTIVE FORM, SUBJECT TO POST-
TRANSLATIONAL ACTIVATION BY A SYSTEM INVOLVING AT LEAST THREE GENE
PRODUCTS. THIS UNKNOWN IN VIVO SYSTEM IS MIMICKED IN VITRO BY IRON
AND DITHIOTHREITOL. THERE IS CONSIDERABLE EVIDENCE FOR A FREE-
RADICAL ACTIVATION MECHANISM.
SIMILARITY: BELONGS TO THE IRON-SULFUR DEPENDENT L-SERINE
DEHYDRATASE FAMILY.
|
| | exo | b2798 | 5'-3' exonuclease |
EG12372 |
FUNCTION: 3'-5' EXONUCLEASE ACTING PREFERENTIALLY ON SINGLE-
STRANDED DNA. ALSO HAS A 3'-PHOSPHODIESTERASE ACTIVITY THAT CAN
REMOVE THE 3'-UNSATURATED SUGAR-PHOSPHATE PRODUCT AT A 3'-INCISED
AP SITE. MAY PLAY AN IMPORTANT ROLE IN BASE EXCISION REPAIR AND
OTHER REPLICATIVE REPAIR AND RECOMBINATION PATHWAYS.
SIMILARITY: HIGH, TO THE EXONUCLEASE DOMAIN OF SOME BACTERIAL
DNA POLYMERASES OF FAMILY A.
|
| 0.194119 | + | ybaD | b0413 | orf, hypothetical protein |
EG11320 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0943.
SIMILARITY: TO C.ACETOBUTYLICUM HYPOTHETICAL PROTEIN IN SIGG
3'REGION (AC P33661) AND TO SYNECHOCOCCUS PCC 6301 HYPOTHETICAL
PROTEIN IN PSBB-RPS1 INTERGENIC REGION (AC P46227).
|
| | ribD | b0414 | bifunctional pyrimidine deaminase/reductase in pathway of riboflavin synthesis |
EG11321 |
FUNCTION: CONVERTS 2,5-DIAMINO-6-(RIBOSYLAMINO)-4(3H)-PYRIMIDINONE
5'-PHOSPHATE INTO 5-AMINO-6-(RIBOSYLAMINO)-2,4(1H,3H)-
PYRIMIDINEDIONE 5'-PHOSPHATE.
CATALYTIC ACTIVITY: 2,5-DIAMINO-6-HYDROXY-4-(5-
PHOSPHORIBOSYLAMINO)PYRIMIDINE + H(2)O = 5-AMINO-6-(5-
PHOSPHORIBOSYLAMINO)URACIL + NH(3).
CATALYTIC ACTIVITY: 5-AMINO-6-(5-PHOSPHORIBITYLAMINO)URACIL +
NADP(+) = 5-AMINO-6-(5-PHOSPHORIBOSYLAMINO)URACIL + NADPH.
COFACTOR: ZINC (BY SIMILARITY).
PATHWAY: SECOND AN THIRD STEPS OF RIBOFLAVIN BIOSYNTHESIS.
SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE CYTIDINE AND
DEOXYCYTIDYLATE DEAMINASES FAMILY.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE HTP
REDUCTASE FAMILY.
|
| | ribH | b0415 | riboflavin synthase, beta chain |
EG11322 |
FUNCTION: RIBOFLAVIN SYNTHASE IS A BIFUNCTIONAL ENZYME COMPLEX
CATALYZING THE FORMATION OF RIBOFLAVIN FROM 5-AMINO-6-(1'-D)-
RIBITYL-AMINO-2,4(1H,3H)-PYRIMIDINEDIONE AND L-3,4-DIHYDROHY-2-
BUTANONE-4-PHOSPHATE VIA 6,7-DIMETHYL-8-LUMAZINE. THE BETA
SUBUNIT CATALYZES THE CONDENSATION OF 5-AMINO-6-(1'-D)-RIBITYL-
AMINO-2,4(1H,3H)-PYRIMIDINEDIONE WITH L-3,4-DIHYDROHY-2-BUTANONE-
4-PHOSPHATE YIELDING 6,7-DIMETHYL-8-LUMAZINE.
CATALYTIC ACTIVITY: 2 6,7-DIMETHYL-8-(1-D-RIBITYL)LUMAZINE =
RIBOFLAVIN + 4-(1-D-RIBITYLAMINO)-5-AMINO-2,6-DIHYDROXYPYRIMIDINE.
COFACTOR: FLAVOPROTEIN.
PATHWAY: FINAL STEP OF RIBOFLAVIN SYNTHESIS.
SUBUNIT: OLIGOMER THAT CONSIST OF 3 ALPHA SUBUNITS AND 60 BETA
SUBUNITS (BY SIMILARITY).
SIMILARITY: BELONGS TO THE DMRL SYNTHASE FAMILY.
|
| | nusB | b0416 | transcription termination; L factor |
EG10666 |
FUNCTION: THIS IS ONE OF THE PROTEINS ESSENTIAL FOR THE FORMATION
OF THE RNA POLYMERASE ANTITERMINATION COMPLEX IN THE PRESENCE OF
LAMBDA PHAGE N PROTEIN. HOWEVER, IT IS INVOLVED IN THE
TRANSCRIPTION TERMINATION PROCESS AT CERTAIN SITES DURING NORMAL
BACTERIAL GROWTH. BINDS TO THE BOXA RNA MOTIF.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE NUSB FAMILY.
|
| | thiL | b0417 | thiamin-monophosphate kinase |
EG20227 |
CATALYTIC ACTIVITY: ATP + THIAMINE PHOSPHATE = ADP + THIAMINE
DIPHOSPHATE.
PATHWAY: THIAMINE BIOSYNTHESIS.
SIMILARITY: BELONGS TO THE THIAMINE-MONOPHOSPHATE KINASE FAMILY.
|
| | pgpA | b0418 | phosphatidylglycerophosphatase |
EG10704 |
FUNCTION: ONE OF THE THREE PHOSPHOLIPID PHOSPHATASES, SPECIFICALLY
HYDROLYZES PHOSPHATIDYLGLYCEROPHOSPHATE.
CATALYTIC ACTIVITY: PHOSPHATIDYLGLYCEROPHOSPHATE + H(2)O =
PHOSPHATIDYLGLYCEROL + ORTHOPHOSPHATE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN BY A FRAMESHIFT
IN POSITION 42. IN ADDITION THE AUTHOR OF REF.1 HAS TRANSLATED
THE WRONG DNA STRAND THUS PRODUCING AN ORF WHICH HAS NOTHING TO
DO WITH THE ONE SHOWN HERE.
|
| 0.179324 | - | ygaU | b2665 | orf, hypothetical protein |
EG12675 |
SIMILARITY: SOME, TO B.SUBTILIS XKDP AND YQBP.
|
| 0.176746 | + | plsX | b1090 | glycerolphosphate auxotrophy in plsB background |
EG11437 |
FUNCTION: NOT KNOWN, PROBABLY INVOLVED IN FATTY ACID OR
PHOSPHOLIPID SYNTHESIS.
SIMILARITY: BELONGS TO THE PLSX FAMILY.
|
| | fabH | b1091 | 3-oxoacyl-[acyl-carrier-protein] synthase III; acetylCoA ACP transacylase |
EG10277 |
FUNCTION: CATALYZES THE CONDENSATION REACTION OF FATTY ACID
SYNTHESIS BY THE ADDITION TO AN ACYL ACCEPTOR OF TWO CARBONS
FROM MALONYL-ACP. KAS III CATALYZES THE FIRST CONDENSATION
REACTION WHICH INITIATES FATTY ACID SYNTHESIS AND MAY THEREFORE
PLAY A ROLE IN GOVERNING THE TOTAL RATE OF FATTY ACID PRODUCTION.
POSSESSES BOTH ACETOACETYL-ACP SYNTHASE AND ACETYL TRANSACYLASE
ACTIVITIES.
CATALYTIC ACTIVITY: ACYL-[ACYL-CARRIER PROTEIN] + MALONYL-[ACYL-
CARRIER PROTEIN] = 3-OXOACYL-[ACYL-CARRIER PROTEIN] + CO(2) +
[ACYL-CARRIER PROTEIN].
PATHWAY: FATTY ACID BIOSYNTHESIS.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE FABH FAMILY.
|
| | fabD | b1092 | malonyl-CoA-[acyl-carrier-protein] transacylase |
EG11317 |
CATALYTIC ACTIVITY: MALONYL-COA + [ACYL-CARRIER PROTEIN] = COA
+ MALONYL-[ACYL-CARRIER PROTEIN].
PATHWAY: FATTY ACID BIOSYNTHESIS.
SIMILARITY: SIGNIFICANT, TO SEVERAL OTHER PROTEINS WITH
TRANSACYLASE ACTIVITY.
|
| | fabG | b1093 | 3-oxoacyl-[acyl-carrier-protein] reductase |
EG11318 |
CATALYTIC ACTIVITY: (3R)-3-HYDROXYACYL-[ACYL-CARRIER PROTEIN] +
NADP(+) = 3-OXOACYL-[ACYL-CARRIER PROTEIN] + NADPH.
PATHWAY: FIRST REDUCTION STEP IN THE FATTY ACID BIOSYNTHESIS
PATHWAY.
SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES
(SDR) FAMILY.
|
| 0.176289 | + | pspB | b1305 | phage shock protein |
EG10777 |
FUNCTION: THE PHAGE SHOCK PROTEIN (PSP) OPERON (PSPABCE) MAY PLAY
A SIGNIFICANT ROLE IN THE COMPETITION FOR SURVIVAL UNDER NUTRIENT-
OR ENERGY-LIMITED CONDITIONS. PSPB IS INVOLVED IN THE REGULATION
OF THE TRANSCRIPTION.
SUBCELLULAR LOCATION: INNER MEMBRANE.
INDUCTION: BY HEAT, ETHANOL, OSMOTIC SHOCK AND INFECTION BY
FILAMENTOUS BACTERIOPHAGES.
|
| | pspC | b1306 | phage shock protein: activates phage shock-protein expression |
EG10778 |
FUNCTION: THE PHAGE SHOCK PROTEIN (PSP) OPERON (PSPABCE) MAY PLAY
A SIGNIFICANT ROLE IN THE COMPETITION FOR SURVIVAL UNDER NUTRIENT-
OR ENERGY-LIMITED CONDITIONS. PSPC IS INVOLVED IN THE REGULATION
OF THE TRANSCRIPTION.
INDUCTION: BY HEAT, ETHANOL, OSMOTIC SHOCK AND INFECTION BY
FILAMENTOUS BACTERIOPHAGES.
|
| | pspD | b1307 | phage shock protein |
EG10779 |
INDUCTION: BY HEAT, ETHANOL, OSMOTIC SHOCK AND INFECTION BY
FILAMENTOUS BACTERIOPHAGES.
|
| | pspE | b1308 | phage shock protein |
EG10780 |
INDUCTION: BY HEAT, ETHANOL, OSMOTIC SHOCK AND INFECTION BY
FILAMENTOUS BACTERIOPHAGES.
|
| 0.174653 | + | ahpF | b0606 | alkyl hydroperoxide reductase, F52a subunit; detoxification of hydroperoxides |
EG11385 |
FUNCTION: SERVES TO PROTECT THE CELL AGAINST DNA DAMAGE BY ALKYL
HYDROPEROXIDES. IT CAN USE EITHER NADH OR NADPH AS ELECTRON DONOR
FOR DIRECT REDUCTION OF REDOX DYES OR OF ALKYL HYDROPEROXIDES WHEN
COMBINED WITH THE AHPC PROTEIN.
COFACTOR: FAD.
SUBUNIT: HOMODIMER.
MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND.
SIMILARITY: BELONGS TO THE PYRIDINE NUCLEOTIDE-DISULFIDE
OXIDOREDUCTASES CLASS-II.
|
| 0.168301 | + | ttk | b3641 | putative transcriptional regulator |
EG11191 |
FUNCTION: UNKNOWN.
SIMILARITY: BELONGS TO THE TETR/ACRR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.162095 | + | yhfP | b3373 | orf, hypothetical protein |
EG12911 |
|
| | yhfQ | b3374 | putative kinase |
EG12912 |
SIMILARITY: BELONGS TO THE PFKB FAMILY OF CARBOHYDRATE KINASES.
|
| | yhfR | b3375 | putative transcriptional regulator |
EG12913 |
SIMILARITY: BELONGS TO THE GNTR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.147073 | + | dapF | b3809 | diaminopimelate epimerase |
EG10209 |
CATALYTIC ACTIVITY: LL-2,6-DIAMINOHEPTANEDIOATE = MESO-
DIAMINOHEPTANEDIOATE.
PATHWAY: SIXTH STEP IN THE BIOSYNTHESIS OF LYSINE FROM ASPARTATE
SEMIALDEHYDE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE DIAMINOPIMELATE EPIMERASE FAMILY.
|
| | yigA | b3810 | orf, hypothetical protein |
EG11201 |
|
| | xerC | b3811 | site-specific recombinase, acts on cer sequence of ColE1, effects chromosome segregation at cell division |
EG11069 |
FUNCTION: PARTICIPATES IN THE SITE-SPECIFIC RECOMBINATION AT
PLASMID COLE1 XER (OR CER) SITE AND AT THE DIF LOCI IN THE
CHOROMOSOME WHICH IS INVOLVED IN THE NORMAL PARTITION OF THE
E.COLI CHROMOSOME. ACTS BY CATALYZING THE CUTTING AND REJOINING
OF THE RECOMBINATING DNA MOLECULES. ACTS JOINTLY WITH XERD.
SIMILARITY: BELONGS TO THE "PHAGE" INTEGRASE FAMILY.
|
| | yigB | b3812 | putative phosphatase |
EG11202 |
SIMILARITY: TO E.COLI YJJG.
|
| | uvrD | b3813 | DNA-dependent ATPase I and helicase II |
EG11064 |
FUNCTION: HAS BOTH ATPASE AND HELICASE ACTIVITIES. UNWINDS DNA
DUPLEXES WITH 3' TO 5' POLARITY WITH RESPECT TO THE BOUND STRAND
AND INITIATES UNWINDING MOST EFFECTIVELY WHEN A SINGLE-STRANDED
REGION IS PRESENT. INVOLVED IN THE POSTINCISION EVENTS OF
NUCLEOTIDE EXCISION REPAIR AND METHYL-DIRECTED MISMATCH REPAIR.
SIMILARITY: BELONGS TO THE UVRD SUBFAMILY OF HELICASES.
|
| 0.124090 | - | glgS | b3049 | glycogen biosynthesis, rpoS dependent |
EG11381 |
FUNCTION: INVOLVED IN GLYCOGEN SYNTHESIS. MAY BE INVOLVED IN
GLYCOGEN PRIMING.
|
| 0.105796 | - | lysP | b2156 | lysine-specific permease |
EG11337 |
FUNCTION: PERMEASE THAT IS INVOLVED IN THE TRANSPORT ACROSS THE
CYTOPLASMIC MEMBRANE OF LYSINE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
INDUCTION: HIGH, IN ANAEROBIC MEDIA OF LOW PH, CONTAINING LYSINE.
SIMILARITY: BELONGS TO THE AMINO ACID PERMEASE FAMILY.
|
| 0.105562 | + | glnS | b0680 | glutamine tRNA synthetase |
EG10390 |
CATALYTIC ACTIVITY: ATP + L-GLUTAMINE + TRNA(GLN) = AMP +
PYROPHOSPHATE + L-GLUTAMINYL-TRNA(GLN).
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO CLASS-I AMINOACYL-TRNA SYNTHETASE FAMILY.
|
| 0.104454 | + | yegD | b2069 | putative heat shock protein |
EG12200 |
SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY.
|
| 0.103056 | + | b0817 | b0817 | putative toxin |
|
|
| | ybiR | b0818 | orf, hypothetical protein |
EG13323 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: TO M.JANNASCHII MJ0456.
|
| 0.102979 | + | bioB | b0775 | biotin synthesis, sulfur insertion? |
EG10118 |
CATALYTIC ACTIVITY: DETHIOBIOTIN + (S) = BIOTIN.
PATHWAY: LAST STEP IN BIOTIN BIOSYNTHESIS PATHWAY.
SIMILARITY: BELONGS TO THE BIOTIN AND LIPOIC ACID SYNTHETASES
FAMILY.
|
| | bioF | b0776 | 8-amino-7-oxononanoate synthase |
EG10121 |
CATALYTIC ACTIVITY: 6-CARBOXYHEXANOYL-COA + L-ALANINE =
8-AMINO-7-OXONONANOATE + COA + CO(2).
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: FIRST STEP IN BIOTIN BIOSYNTHESIS.
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| | bioC | b0777 | biotin biosynthesis; reaction prior to pimeloyl CoA |
EG10119 |
FUNCTION: BIOC IS INVOLVED IN AN EARLY, BUT CHEMICALLY UNEXPLORED,
STEP IN THE CONVERSION OF PIMELIC ACID TO BIOTIN.
PATHWAY: BIOTIN BIOSYNTHESIS PATHWAY.
SIMILARITY: BELONGS TO THE METHYLTRANSFERASE SUPERFAMILY.
|
| | bioD | b0778 | dethiobiotin synthetase |
EG10120 |
CATALYTIC ACTIVITY: ATP + 7,8-DIAMINONONANOATE + CO(2) = ADP +
ORTHOPHOSPHATE + DETHIOBIOTIN.
COFACTOR: REQUIRES MAGNESIUM.
PATHWAY: BIOTIN BIOSYNTHESIS PATHWAY.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE DETHIOBIOTIN SYNTHETASE FAMILY.
|
| 0.102573 | + | yheE | b3324 | putative general secretion pathway for protein export (GSP) |
EG12889 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INNER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE EXEC/PULC/OUTC FAMILY.
|
| | yheF | b3325 | putative general protein secretion protein |
EG12890 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: OUTER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE EXED/OUTD/PULD/XPSD FAMILY.
|
| | yheG | b3326 | putative general secretion pathway for protein export (GSP) (TYPE II TRAFFIC WARDEN ATPASE) |
EG12891 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
SIMILARITY: BELONGS TO THE PULE/OUTE/EXEE/XPSE/XCPR FAMILY.
|
| | hofF | b3327 | putative general protein secretion protein |
EG12885 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
SIMILARITY: BELONGS TO THE PULF/OUTF/EXEF/XPSF/XCPS FAMILY.
|
| | hofG | b3328 | putative general protein secretion protein |
EG12886 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SIMILARITY: BELONGS TO THE PULG/OUTG/XPSG/EXEG/XCPT FAMILY.
|
| | hofH | b3329 | putative general protein secretion protein |
EG12887 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SIMILARITY: BELONGS TO THE PULH/OUTH/XPSH/EXEH/XCPU FAMILY.
|
| | yheH | b3330 | putative export protein for general secretion pathway (GSP) |
EG12892 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SIMILARITY: BELONGS TO THE PULI/OUTI/XPSI/EXEI/XCPV FAMILY.
|
| | yheI | b3331 | putative export protein I for general secretion pathway (GSP) |
EG12893 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SIMILARITY: BELONGS TO THE PULJ/OUTJ/XPSJ/EXEJ/XCPW FAMILY.
|
| | yheJ | b3332 | putative export protein J for general secretion pathway (GSP) |
EG12894 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INNER MEMBRANE (POTENTIAL).
SIMILARITY: BELONGS TO THE EXEK/PULK/OUTK/XCPX FAMILY.
|
| | yheK | b3333 | putative general protein secretion protein |
EG12895 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INNER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE EXEL/PULL/OUTL/XCPY FAMILY.
|
| | pshM | b3334 | putative general secretion |
EG12173 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INNER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE EXEM/PULM/OUTM/XCPZ FAMILY.
|
| | hofD | b3335 | leader peptidase, integral membrane protein |
EG11359 |
FUNCTION: CLEAVES TYPE-4 FIMBRIAL LEADER SEQUENCE AND METHYLATES
THE N-TERMINAL (GENERALLY PHE) RESIDUE (BY SIMILARITY).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
SIMILARITY: BELONGS TO PEPTIDASE FAMILY A24; ALSO KNOWN AS TYPE
III LEADER PEPTIDASE FAMILY.
|
| 0.099322 | + | yqjI | b3071 | orf, hypothetical protein |
EG12954 |
|
| 0.093827 | + | yhaB | b3120 | orf, hypothetical protein |
EG11173 |
|
| | yhaC | b3121 | orf, hypothetical protein |
EG11174 |
|
| | b3122 | b3122 | orf, hypothetical protein |
|
|
| 0.092608 | + | hyfR | b2491 | putative 2-component regulator, interaction with sigma 54 |
EG14219 |
FUNCTION: REQUIRED FOR INDUCTION OF EXPRESSION OF THE HYDROGENASE-
4 STRUCTURAL GENES.
SIMILARITY: THE CENTRAL REGION CONTAINS A SIGMA-54 FACTOR
INTERACTION ATP-BINDING DOMAIN.
|
| | focB | b2492 | probable formate transporter (formate channel 2) |
EG14220 |
FUNCTION: INVOLVED IN THE BIDIRECTIONAL TRANSPORT OF FORMATE
(BY SIMILARITY).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
SIMILARITY: BELONGS TO THE FNT (TC 2.44) FAMILY OF TRANSPORTERS.
|
| 0.092005 | + | gltB | b3212 | glutamate synthase, large subunit |
EG10403 |
CATALYTIC ACTIVITY: 2 L-GLUTAMATE + NADP(+) = L-GLUTAMINE +
2-OXOGLUTARATE + NADPH.
COFACTOR: BINDS A 3FE-4S CLUSTER; FAD AND FMN.
PATHWAY: NITROGEN METABOLISM, GLUTAMATE BIOSYNTHESIS.
THE CATALYZED REACTION BRINGS TOGETHER THE NITROGEN AND
CARBON METABOLISM.
SUBUNIT: AGGREGATE OF 4 CATALYTICAL ACTIVE HETERODIMERS,
CONSISTING OF A LARGE AND A SMALL SUBUNIT.
MISCELLANEOUS: GLUTAMINE BINDS TO THE LARGE SUBUNIT AND TRANSFERS
THE AMIDO GROUP TO 2-OXO-GLUTAMATE THAT APPARENTLY BINDS TO THE
SMALL SUBUNIT.
SIMILARITY: TO OTHER GLUTAMATE SYNTHASES.
|
| | gltD | b3213 | glutamate synthase, small subunit |
EG10404 |
CATALYTIC ACTIVITY: 2 L-GLUTAMATE + NADP(+) = L-GLUTAMINE +
2-OXOGLUTARATE + NADPH.
COFACTOR: BINDS A 4FE-4S CLUSTER.
PATHWAY: NITROGEN METABOLISM, GLUTAMATE BIOSYNTHESIS.
THE CATALYZED REACTION BRINGS TOGETHER THE NITROGEN AND
CARBON METABOLISM.
SUBUNIT: AGGREGATE OF 4 CATALYTICAL ACTIVE HETERODIMERS,
CONSISTING OF A LARGE AND A SMALL SUBUNIT.
MISCELLANEOUS: GLUTAMINE BINDS TO THE LARGE SUBUNIT AND TRANSFERS
THE AMIDO GROUP TO 2-OXO-GLUTAMATE THAT APPARENTLY BINDS TO THE
SMALL SUBUNIT.
SIMILARITY: THE IRON-SULFUR CENTERS ARE SIMILAR TO THOSE OF
'BACTERIAL-TYPE' 4FE-4S FERREDOXINS.
SIMILARITY: STRONG, TO E.COLI AEGA AND YGFT.
|
| 0.091713 | + | b1045 | b1045 | putative polyprotein |
|
|
| | ymdC | b1046 | putative synthase |
EG13875 |
SIMILARITY: BELONGS TO THE PHOSPHOLIPDASE D FAMILY. CARDIOLIPIN
SYNTHASE SUBFAMILY. STRONG, TO H.PYLORI HP0190.
|
| 0.089571 | + | yjiI | b4331 | orf, hypothetical protein |
EG12570 |
FUNCTION: REMOVES THE 2'-PHOSPHATE FROM RNA VIA AN INTERMEDIATE IN
WHICH THE PHOSPHATE IS ADP-RIBOSYLATED BY NAD FOLLOWED BY A
PRESUMED TRANSESTERIFICATION TO RELEASE THE RNA AND GENERATE ADP-
RIBOSE 1"-2"-CYCLIC PHOSPHATE (APPR>P). MAY FUNCTION AS AN ADP-
RIBOSYLASE.
SIMILARITY: BELONGS TO THE KPTA / TPT1 FAMILY.
|
| 0.088875 | + | sfa | b0991 | suppresses fabA and ts growth mutation |
EG13233 |
SIMILARITY: STRONG, TO E.COLI YDFY.
|
| 0.088821 | + | b0392 | b0392 | orf, hypothetical protein |
EG14282 |
SIMILARITY: TO THE C-TERMINAL OF E.COLI YDBD.
|