Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 5.736134 | + | nrdA | b2234 | ribonucleoside diphosphate reductase 1, alpha subunit, B1 |
EG10660 |
FUNCTION: CATALYZES THE BIOSYNTHESIS OF DEOXYRIBONUCLEOTIDES FROM
THE CORRESPONDING RIBONUCLEOTIDES, PRECURSORS THAT ARE NECESSARY
FOR DNA SYNTHESIS. R1 CONTAINS THE BINDING SITES FOR BOTH
SUBSTRATES AND ALLOSTERIC EFFECTORS AND CARRIES OUT THE ACTUAL
REDUCTION OF THE RIBONUCLEOTIDE.
CATALYTIC ACTIVITY: 2'-DEOXYRIBONUCLEOSIDE DIPHOSPHATE + OXIDIZED
THIOREDOXIN + H(2)O = RIBONUCLEOSIDE DIPHOSPHATE + REDUCED
THIOREDOXIN.
PATHWAY: FIRST REACTION IN THE DNA REPLICATION PATHWAY.
SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS. THE B1
PROTEIN IS A DIMER OF ALPHA CHAINS.
MISCELLANEOUS: E.COLI PRODUCES TWO SEPARATE CLASS I ENZYMES. THIS
ONE IS THE FUNCTIONAL ENZYME DURING GROWTH.
SIMILARITY: BELONGS TO THE RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE
LARGE CHAIN FAMILY.
CAUTION: REF.2 SEQUENCE WAS INCORRECT.
|
| 5.448395 | - | nrdD | b4238 | anaerobic ribonucleoside-triphosphate reductase |
EG11417 |
CATALYTIC ACTIVITY: 2'-DEOXYRIBONUCLEOSIDE TRIPHOSPHATE +
OXIDIZED THIOREDOXIN + H(2)O = RIBONUCLEOSIDE TRIPHOSPHATE +
REDUCED THIOREDOXIN.
COFACTOR: CONTAINS AN IRON-SULFUR CLUSTER. REQUIRES
S-ADENOSYLMETHIONINE, WHICH IS PROBABLY A GLYCINE RADICAL
GENERATOR.
INDUCTION: PROBABLY BY NRDD-ACTIVATING ENZYME UNDER ANAEROBIC
CONDITIONS BY GENERATION OF AN ORGANIC FREE RADICAL. EXPOSURE OF
ACTIVATED NRDD TO OXYGEN MAY RESULT IN CLEAVAGE AT THE GLYCINE
RESIDUE HARBORING ITS ORGANIC RADICAL WITH LOSS OF THE 31
C-TERMINAL AA.
SIMILARITY: STRONG, TO T4 AND H.INFLUENZAE NRDD.
|
| 4.345311 | + | yccE | b1001 | orf, hypothetical protein |
EG12196 |
 |
| 2.284771 | + | lpp | b1677 | murein lipoprotein |
EG10544 |
SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID
ANCHOR.
|
| 1.697709 | - | b2998 | b2998 | orf, hypothetical protein |
EG13007 |
 |
| 1.605840 | - | yiaW | b3587 | orf, hypothetical protein |
EG12291 |
SIMILARITY: STRONG, TO E.COLI YIBI.
|
 |  | yiaV | b3586 | putative membrane protein |
EG12290 |
SIMILARITY: STRONG, TO E.COLI YIBH; SOME, TO P.AERUGINOSA APRE.
|
| 1.474943 | + | slp | b3506 | outer membrane protein induced after carbon starvation |
EG11890 |
FUNCTION: THE INDUCTION OF SLP MAY HELP TO STABILIZE THE OUTER
MEMBRANE DURING CARBON STARVATION AND STATIONARY PHASE.
SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID
ANCHOR.
INDUCTION: INDUCED UPON STARVATION AND SLOWED GROWTH. CAMP/CRP-
INDEPENDENT.
|
| 1.456841 | + | atoS | b2219 | sensor protein AtoS for response regulator AtoC |
EG11667 |
FUNCTION: MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM ATOS/ATOC;
MAY ACTIVATE ATOC BY PHOSPHORYLATION.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: TO OTHER PROKARYOTIC SENSORY TRANSDUCTION HISTIDINE
KINASES.
|
 |  | atoC | b2220 | response regulator of ato, ornithine decarboxylase antizyme (sensor ATOS) |
EG11668 |
FUNCTION: MEMBER OF THE TWO-COMPONENT REGULATORY SYSTEM ATOS/ATOC
INVOLVED IN THE TRANSCRIPTIONAL REGULATION OF THE ATO GENES FOR
ACETOACETATE METABOLISM. ALSO AN INHIBITOR OF POLYAMINE
BIOSYNTHESIS.
SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
PTM: PHOSPHORYLATED BY ATOS (POTENTIAL).
PTM: THE N-TERMINUS IS BLOCKED.
SIMILARITY: THE N-TERMINAL REGION IS SIMILAR TO THAT OF OTHER
REGULATORY COMPONENTS OF SENSORY TRANSDUCTION SYSTEMS.
SIMILARITY: THE CENTRAL REGION CONTAINS A SIGMA-54 FACTOR
INTERACTION ATP-BINDING DOMAIN.
CAUTION: REF.4 SEQUENCE DIFFERS IN THE N-TERMINAL REGION DUE
TO A FRAMESHIFT.
|
| 1.324605 | + | b1643 | b1643 | orf, hypothetical protein |
EG13943 |
 |
 |  | b1644 | b1644 | putative membrane protein |
EG13944 |
 |
 |  | b1645 | b1645 | orf, hypothetical protein |
 |
 |
| 1.085098 | + | dnaK | b0014 | chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins |
EG10241 |
FUNCTION: PLAYS AN ESSENTIAL ROLE IN THE INITIATION OF PHAGE
LAMBDA DNA REPLICATION, WHERE IT ACTS IN AN ATP-DEPENDENT FASHION
WITH THE DNAJ PROTEIN TO RELEASE LAMBDA O AND P PROTEINS FROM THE
PREPRIMOSOMAL COMPLEX. DNAK IS ALSO INVOLVED IN CHROMOSOMAL DNA
REPLICATION, POSSIBLY THROUGH AN ANALOGOUS INTERACTION WITH THE
DNAA PROTEIN. ALSO PARTICIPATES ACTIVELY IN THE RESPONSE TO
HYPEROSMOTIC SHOCK.
PTM: AUTOPHOSPHORYLATED; GRPE INHIBITS THE AUTOPHOSPHORYLATION.
MISCELLANEOUS: THE MUTANTS DNAK756(TS), SEG-1 AND SEG-2 CONFER
TEMPERATURE SENSITIVITY.
SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY.
|
 |  | dnaJ | b0015 | chaperone with DnaK; heat shock protein |
EG10240 |
FUNCTION: INTERACTS WITH DNAK, TO DISASSEMBLE A PROTEIN COMPLEX
AT THE PHAGE LAMBDA ORIGIN OF REPLICATION. STIMULATES, JOINTLY
WITH GRPE, THE ATPASE ACTIVITY OF DNAK.
COFACTOR: BINDS TWO ZINC IONS PER MONOMER.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
INDUCTION: BY HEAT SHOCK UNDER THE CONTROL OF THE HTPR REGULATORY
PROTEIN.
SIMILARITY: BELONGS TO THE DNAJ FAMILY.
SIMILARITY: CONTAINS 1 J DOMAIN.
SIMILARITY: CONTAINS 1 CR DOMAIN.
|
 |  | yi81_1 | b0016 | IS186 hypothetical protein |
EG40012 |
FUNCTION: INVOLVED IN THE TRANSPOSITION OF THE INSERTION
SEQUENCE IS186.
SIMILARITY: BELONGS TO THE TRANSPOSASE FAMILY 11.
|
| 0.984947 | + | yaiB | b0382 | orf, hypothetical protein |
EG11256 |
 |
 |  | phoA | b0383 | alkaline phosphatase |
EG10727 |
CATALYTIC ACTIVITY: AN ORTHOPHOSPHORIC MONOESTER + H(2)O = AN
ALCOHOL + ORTHOPHOSPHATE (AT A HIGH PH OPTIMUM).
COFACTOR: METALLOENZYME CONTAINING TWO ZINC ATOMS AND A MAGNESIUM
ION.
SUBUNIT: ISOZYMES 1 & 3 ARE A DIMER OF IDENTICAL CHAINS, ISOZYME 2
IS A DIMER OF HETEROGENEOUS CHAINS, ONE OF EACH OF THE SUBUNITS
FROM ISOZYMES 1 AND 3.
SUBCELLULAR LOCATION: PERIPLASMIC.
SIMILARITY: BELONGS TO THE ALKALINE PHOSPHATASE FAMILY.
DATABASE: NAME=ProZyme technical fact sheet;
WWW="http://www.prozyme.com/technical/bap.html".
|
 |  | psiF | b0384 | induced by phosphate starvation |
EG11401 |
 |
 |  | yaiC | b0385 | orf, hypothetical protein |
EG11257 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE YAIC / YFIN (E.COLI), YHCK (B.SUBTILIS)
FAMILY.
|
| 0.879371 | + | b1527 | b1527 | orf, hypothetical protein |
EG13819 |
 |
| 0.867437 | + | b2659 | b2659 | orf, hypothetical protein |
EG13523 |
FUNCTION: MAY BE INVOLVED IN THE CONTROL OF UTILIZATION OF GAMA-
AMINOBUTYRIC ACID.
|
 |  | ygaF | b2660 | orf, hypothetical protein |
EG12387 |
 |
 |  | gabD | b2661 | succinate-semialdehyde dehydrogenase, NADP-dependent activity |
EG11329 |
CATALYTIC ACTIVITY: SUCCINATE SEMIALDEHYDE + NAD(P)(+) + H(2)O
= SUCCINATE + NAD(P)H.
PATHWAY: 4-AMINOBUTYRATE (GABA) DEGRADATION PATHWAY.
SIMILARITY: BELONGS TO THE ALDEHYDE DEHYDROGENASES FAMILY.
|
 |  | gabT | b2662 | 4-aminobutyrate aminotransferase activity |
EG10361 |
CATALYTIC ACTIVITY: 4-AMINOBUTANOATE + 2-OXOGLUTARATE = SUCCINATE
SEMIALDEHYDE + L-GLUTAMATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: 4-AMINOBUTYRATE (GABA) DEGRADATION PATHWAY.
SUBUNIT: HOMODIMER.
INDUCTION: CATABOLITE REPRESSION BY GLUCOSE (REPRESSION RELIEVED
BY GABA).
SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| 0.830540 | + | argR | b3237 | repressor of arg regulon; cer-mediated site specific recombination |
EG10070 |
FUNCTION: NEGATIVELY CONTROLS THE EXPRESSION OF THE FOUR OPERONS
OF ARGININE BIOSYNTHESIS IN ADDITION TO THE CARAB OPERON.
PREDOMINANTLY INTERACTS WITH A.T RESIDUES IN ARG BOXES.
IT ALSO BINDS TO A SPECIFIC SITE IN CER LOCUS. THUS IT IS
ESSENTIAL FOR CER-MEDIATED SITE-SPECIFIC RECOMBINATION IN
COLE1. IT IS NECESSARY FOR MONOMERIZATION OF THE PLASMID COLE1.
SUBUNIT: HOMOHEXAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ARGR FAMILY.
|
| 0.720395 | + | nrdH | b2673 | glutaredoxin-like protein; hydrogen donor |
EG13286 |
FUNCTION: ELECTRON TRANSPORT SYSTEM FOR RIBONUCLEOTIDE REDUCTASE
SYSTEM NRDEF.
SIMILARITY: BELONGS TO THE GLUTAREDOXIN FAMILY.
|
 |  | nrdI | b2674 | orf, hypothetical protein |
EG13287 |
FUNCTION: NOT KNOWN; PROBABLY INVOLVED IN RIBONUCLEOTIDE REDUCTASE
FUNCTION.
SIMILARITY: BELONGS TO THE NRDI FAMILY.
|
 |  | nrdE | b2675 | ribonucleoside-diphosphate reductase 2, alpha subunit |
EG20257 |
FUNCTION: CATALYZES THE BIOSYNTHESIS OF DEOXYRIBONUCLEOTIDES FROM
THE CORRESPONDING RIBONUCLEOTIDES, PRECURSORS THAT ARE NECESSARY
FOR DNA SYNTHESIS. R1E CONTAINS THE BINDING SITES FOR BOTH
SUBSTRATES AND ALLOSTERIC EFFECTORS AND CARRIES OUT THE ACTUAL
REDUCTION OF THE RIBONUCLEOTIDE.
CATALYTIC ACTIVITY: 2'-DEOXYRIBONUCLEOSIDE DIPHOSPHATE + OXIDIZED
THIOREDOXIN + H(2)O = RIBONUCLEOSIDE DIPHOSPHATE + REDUCED
THIOREDOXIN.
PATHWAY: FIRST REACTION IN THE DNA REPLICATION PATHWAY.
SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS
(BY SIMILARITY).
SIMILARITY: BELONGS TO THE RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE
LARGE CHAIN FAMILY.
CAUTION: REF.2 DIFFERS FROM THAT SHOWN FROM POSITION 529 ONWARD
DUE TO A FRAMESHIFT.
|
 |  | nrdF | b2676 | ribonucleoside-diphosphate reductase 2, beta chain, frag |
EG12381 |
FUNCTION: CATALYZES THE BIOSYNTHESIS OF DEOXYRIBONUCLEOTIDES FROM
THE CORRESPONDING RIBONUCLEOTIDES, PRECURSORS THAT ARE NECESSARY
FOR DNA SYNTHESIS. R2F CONTAINS THE TYROSYL RADICAL REQUIRED FOR
CATALYSIS.
CATALYTIC ACTIVITY: 2'-DEOXYRIBONUCLEOSIDE DIPHOSPHATE + OXIDIZED
THIOREDOXIN + H(2)O = RIBONUCLEOSIDE DIPHOSPHATE + REDUCED
THIOREDOXIN.
COFACTOR: CONTAINS TWO IRON IONS (BY SIMILARITY).
PATHWAY: FIRST REACTION IN THE DNA REPLICATION PATHWAY.
SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS
(BY SIMILARITY).
SIMILARITY: BELONGS TO THE RIBONUCLEOSIDE DIPHOSPHATE REDUCTASE
SMALL CHAIN FAMILY.
|
| 0.691274 | + | yhcN | b3238 | orf, hypothetical protein |
EG12820 |
SIMILARITY: BELONGS TO THE YAHO/YBIJ/YBIM/YCFR/YHCN FAMILY.
|
| 0.618390 | + | b1587 | b1587 | putative oxidoreductase, major subunit |
EG13843 |
FUNCTION: TERMINAL REDUCTASE DURING ANAEROBIC GROWTH ON
VARIOUS SULFOXIDE AND N-OXIDE COMPOUNDS (BY SIMILARITY).
COFACTOR: MOLYBDENUM (MOLYBDOPTERIN); MAY BIND A 4FE-4S CLUSTER
(BY SIMILARITY).
SUBCELLULAR LOCATION: CYTOPLASMIC FACE OF THE MEMBRANE (BY
SIMILARITY).
SIMILARITY: BELONGS TO THE PROKARYOTIC MOLYBDOPTERIN-CONTAINING
OXIDOREDUCTASE FAMILY.
|
 |  | b1588 | b1588 | putative oxidoreductase, major subunit |
EG13844 |
FUNCTION: TERMINAL REDUCTASE DURING ANAEROBIC GROWTH ON
VARIOUS SULFOXIDE AND N-OXIDE COMPOUNDS (BY SIMILARITY).
COFACTOR: MOLYBDENUM (MOLYBDOPTERIN); MAY BIND A 4FE-4S CLUSTER
(BY SIMILARITY).
SUBCELLULAR LOCATION: CYTOPLASMIC FACE OF THE MEMBRANE (BY
SIMILARITY).
SIMILARITY: BELONGS TO THE PROKARYOTIC MOLYBDOPTERIN-CONTAINING
OXIDOREDUCTASE FAMILY.
|
 |  | b1589 | b1589 | putative oxidoreductase, Fe-S subunit |
 |
 |
 |  | b1590 | b1590 | putative DMSO reductase anchor subunit |
 |
 |
 |  | b1591 | b1591 | putative oxidoreductase component |
EG13847 |
SIMILARITY: TO H.INFLUENZAE HI1044.
SIMILARITY: BELONGS TO THE YCDY/YNFI FAMILY.
|
 |  | b1592 | b1592 | putative chloride channel |
 |
 |
| 0.615016 | - | ddlA | b0381 | D-alanine-D-alanine ligase A |
EG10213 |
FUNCTION: CELL WALL FORMATION.
CATALYTIC ACTIVITY: ATP + D-ALANINE + D-ALANINE = ADP +
ORTHOPHOSPHATE + D-ALANYL-D-ALANINE.
PATHWAY: ALONG WITH ALANINE RACEMASE, IT MAKES UP THE D-ALANINE
BRANCH OF THE PEPTIDOGLYCAN BIOSYNTHETIC ROUTE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE D-ALANINE--D-ALANINE LIGASE FAMILY.
THERE ARE TWO RELATED D-ALANINE--D-ALANINE LIGASES IN E.COLI AND
S.TYPHIMURIUM.
|
| 0.608570 | + | yhfL | b3369 | orf, hypothetical protein |
EG12907 |
 |
| 0.564116 | + | ptsH | b2415 | PTS system protein HPr |
EG10788 |
FUNCTION: THIS IS A COMPONENT OF THE PHOSPHOENOLPYRUVATE-DEPENDENT
SUGAR PHOSPHOTRANSFERASE SYSTEM (PTS), A MAJOR CARBOHYDRATE ACTIVE
-TRANSPORT SYSTEM. THE PHOSPHORYL GROUP FROM PHOSPHOENOLPYRUVATE
(PEP) IS TRANSFERRED TO THE PHOSPHORYL CARRIER PROTEIN HPR BY
ENZYME I. PHOSPHO-HPR THEN TRANSFERS IT TO THE PERMEASE (ENZYMES
II/III). HPR IS COMMON TO ALL PTS.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HPR FAMILY.
|
 |  | ptsI | b2416 | PEP-protein phosphotransferase system enzyme I |
EG10789 |
FUNCTION: THIS IS A COMPONENT OF THE PHOSPHOENOLPYRUVATE-DEPENDENT
SUGAR PHOSPHOTRANSFERASE SYSTEM (PTS), A MAJOR CARBOHYDRATE ACTIVE
-TRANSPORT SYSTEM. ENZYME I TRANSFERS THE PHOSPHORYL GROUP FROM
PHOSPHOENOLPYRUVATE (PEP) TO THE PHOSPHORYL CARRIER PROTEIN (HPR).
ENZYME I IS COMMON TO ALL PTS.
CATALYTIC ACTIVITY: PHOSPHOENOLPYRUVATE + PROTEIN HISTIDINE =
PYRUVATE + PROTEIN N-PHOSPHOHISTIDINE.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE PEP-UTILIZING ENZYMES FAMILY.
|
 |  | crr | b2417 | PTS system, glucose-specific IIA component |
EG10165 |
FUNCTION: THIS IS A COMPONENT OF THE PHOSPHOENOLPYRUVATE-DEPENDENT
SUGAR PHOSPHOTRANSFERASE SYSTEM (PTS), A MAJOR CARBOHYDRATE ACTIVE
-TRANSPORT SYSTEM. THE IICD DOMAINS CONTAIN THE SUGAR BINDING SITE
AND THE TRANSMEMBRANE CHANNEL; THE IIA DOMAIN CONTAINS THE PRIMARY
PHOSPHORYLATION SITE (THE DONOR IS PHOSPHO-HPR); IIA TRANSFERS ITS
PHOSPHORYL GROUP TO THE IIB DOMAIN WHICH FINALLY TRANSFERS IT TO
THE SUGAR.
CATALYTIC ACTIVITY: PROTEIN N-PHOSPHOHISTIDINE + SUGAR =
PROTEIN HISTIDINE + SUGAR PHOSPHATE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
MISCELLANEOUS: THE NONPHOSPHORYLATED FACTOR III IS AN INHIBITOR
FOR UPTAKE OF CERTAIN SUGARS SUCH AS MALTOSE, MELIBIOSE, LACTOSE,
& GLYCEROL. PHOSPHORYLATED FACTOR III, HOWEVER, MAY BE AN
ACTIVATOR FOR ADENYLATE CYCLASE. IT IS AN IMPORTANT REGULATORY
PROTEIN FOR CELL METABOLISM.
SIMILARITY: CONTAINS A PTS EIIA DOMAIN.
|
| 0.482343 | + | gltF | b3214 | regulator of gltBDF operon, induction of Ntr enzymes |
EG11514 |
FUNCTION: INVOLVED IN INDUCTION OF THE SO-CALLED NTR ENZYMES IN
RESPONSE TO NITROGEN DEPRIVATION, AS WELL AS IN GLUTAMATE
BIOSYNTHESIS. MAY MEDIATE THE GLUTAMATE-DEPENDENT REPRESSION OF
THE GLT OPERON.
SIMILARITY: TO E.COLI YHCF.
|
| 0.434965 | + | yabH | b0055 | putative DNA binding protein |
EG11570 |
FUNCTION: CHAPERONE THAT MAY PLAY A ROLE IN THE CORRECT ASSEMBLY,
ACTIVITY AND/OR MAINTENANCE OF A NUMBER OF MEMBRANE PROTEINS,
INCLUDING TWO-COMPONENT SIGNAL-TRANSDUCTION SYSTEMS. MIGHT CO-
OPERATE WITH DNAK TO ACTIVATE THE RCS TWO-COMPONENT SYSTEM.
SUBCELLULAR LOCATION: TYPE III MEMBRANE PROTEIN.
SIMILARITY: CONTAINS 1 J DOMAIN.
|
| 0.427181 | + | pspA | b1304 | phage shock protein, inner membrane protein |
EG10776 |
FUNCTION: THE PHAGE SHOCK PROTEIN (PSP) OPERON (PSPABCE) MAY PLAY
A SIGNIFICANT ROLE IN THE COMPETITION FOR SURVIVAL UNDER NUTRIENT-
OR ENERGY-LIMITED CONDITIONS. PSPA HAS A ROLE AS A NEGATIVE
REGULATOR, IS REQUIRED FOR EFFICIENT TRANSLOCATION AND HAS AN
UNKNOWN FUNCTION IN THE MAINTENANCE OF THE PROTON MOTIVE FORCE.
SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED.
INDUCTION: BY HEAT, ETHANOL, OSMOTIC SHOCK AND INFECTION BY
FILAMENTOUS BACTERIOPHAGES.
SIMILARITY: BELONGS TO THE PSPA/IM30 FAMILY.
|
 |  | 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.
|
| 0.411918 | - | b1696 | b1696 | putative ARAC-type regulatory protein |
EG13975 |
SIMILARITY: BELONGS TO THE ARAC/XYLS FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.396467 | + | emrR | b2684 | regulator of plasmid mcrB operon (microcin B17 synthesis) |
EG10603 |
FUNCTION: NEGATIVE REGULATOR OF THE MULTIDRUG OPERON EMRAB.
INDUCTION: AUTOREGULATED.
SIMILARITY: BELONGS TO THE MARR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
 |  | emrA | b2685 | multidrug resistance secretion protein |
EG11354 |
FUNCTION: THE EMR LOCUS CONFERS RESISTANCE TO SUBSTANCES OF HIGH
HYDROPHOBICITY. EMRA PROBABLY PARTICIPATE IN A TRANSPORT SYSTEM
TO EXTRUDE TOXINS AND DRUGS FROM THE CELL.
SUBCELLULAR LOCATION: INNER MEMBRANE-BOUND.
SIMILARITY: BELONGS TO THE HLYD FAMILY OF SECRETION PROTEINS.
|
 |  | emrB | b2686 | multidrug resistance; probably membrane translocase |
EG11439 |
FUNCTION: TRANSLOCASE THAT CONFERS RESISTANCE TO SUBSTANCES OF
HIGH HYDROPHOBICITY.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE MAJOR FACILITATOR FAMILY (ALSO KNOWN
AS THE DRUG RESISTANCE TRANSLOCASE FAMILY).
|
| 0.380726 | + | pckA | b3403 | phosphoenolpyruvate carboxykinase |
EG10688 |
CATALYTIC ACTIVITY: ATP + OXALOACETATE = ADP + PHOSPHOENOLPYRUVATE
+ CO(2).
ENZYME REGULATION: ALLOSTERICALLY ACTIVATED BY CALCIUM.
POSITIVELY REGULATED BY CAMP.
PATHWAY: RATE-LIMITING GLUCONEOGENIC ENZYME.
SUBUNIT: MONOMER.
MASS SPECTROMETRY: MW=59656; METHOD=ELECTROSPRAY.
MISCELLANEOUS: MUTANT PCK51 IS AN ALTERED-ACTIVITY MUTANT THAT
CATALYZES THE CONVERSION FROM OXALOACETATE TO PYRUVATE (OAA
DECARBOXYLASE ACTIVITY) AND THE MUTANT PCK53 IS A REDUCED-ACTIVITY
MUTANT.
SIMILARITY: BELONGS TO THE PHOSPHOENOLPYRUVATE CARBOXYKINASE [ATP]
FAMILY.
CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN FROM POSITION 456
ONWARD AND IS SHORTER (464 AA) DUE TO A FRAMESHIFT.
|
| 0.371789 | + | ybhH | b0769 | orf, hypothetical protein |
EG13664 |
SIMILARITY: TO B.SUBTILIS YRAM.
|
 |  | ybhI | b0770 | putative membrane pump protein |
EG13665 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
SIMILARITY: BELONGS TO THE NADC/P/PHO87 FAMILY OF TRANSPORTERS.
SODIT1 SUBFAMILY. STRONG, TO H.INFLUENZAE HI0020.
|
| 0.362626 | + | yhfM | b3370 | putative amino acid/amine transport protein |
EG12908 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: BELONGS TO THE ARCD/CADB/GERAB/LYSI FAMILY OF
PERMEASES.
|
 |  | yhfN | b3371 | putative transport protein |
EG12909 |
SIMILARITY: STRONG, TO THE C-TERMINAL PART OF GLUCOSAMINE--
FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE (GFAT).
|
 |  | yhfO | b3372 | orf, hypothetical protein |
EG12910 |
 |
 |  | 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.
|
| 0.362418 | - | recA | b2699 | DNA strand exchange and renaturation, DNA-dependent ATPase, DNA- and ATP-dependent coprotease |
EG10823 |
FUNCTION: CAN CATALYZE THE HYDROLYSIS OF ATP IN THE PRESENCE OF
SINGLE-STRANDED DNA, THE ATP-DEPENDENT UPTAKE OF SINGLE-STRANDED
DNA BY DUPLEX DNA, AND THE ATP-DEPENDENT HYBRIDIZATION OF
HOMOLOGOUS SINGLE-STRANDED DNAS. IT INTERACTS WITH LEXA CAUSING
ITS ACTIVATION AND LEADING TO ITS AUTOCATALYTIC CLEAVAGE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
INDUCTION: IN RESPONSE TO LOW TEMPERATURE. SENSITIVE TO
TEMPERATURE THROUGH CHANGES IN THE LINKING NUMBER OF THE DNA.
SIMILARITY: BELONGS TO THE RECA FAMILY.
DATABASE: NAME=E.coli recA Web page;
WWW="http://monera.ncl.ac.uk:80/protein/final/reca.htm".
|
 |  | oraA | b2698 | regulator, OraA protein |
EG12080 |
FUNCTION: MAY PLAY A REGULATORY ROLE POSSIBLY BY INTERACTING WITH
RECA.
SIMILARITY: BELONGS TO THE RECX FAMILY.
|
 |  | alaS | b2697 | alanyl-tRNA synthetase |
EG10034 |
CATALYTIC ACTIVITY: ATP + L-ALANINE + TRNA(ALA) = AMP +
PYROPHOSPHATE + L-ALANYL-TRNA(ALA).
COFACTOR: BINDS ONE ZINC ION.
SUBUNIT: HOMOTETRAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO CLASS-II AMINOACYL-TRNA SYNTHETASE FAMILY.
|
| 0.351224 | + | ycbW | b0946 | orf, hypothetical protein |
EG13715 |
 |
| 0.343858 | - | speB | b2937 | agmatinase |
EG10960 |
CATALYTIC ACTIVITY: AGMATINE + H(2)O = PUTRESCINE + UREA.
COFACTOR: MANGANESE (POTENTIAL).
ENZYME REGULATION: THE EXPRESSION OF AUH ACTIVITY IS
ANTAGONISTICALLY REGULATED BY CYCLIC AMP AND AGMATINE. IN THE
PRESENCE OF THE CAMP RECEPTOR PROTEIN, CAMP REPRESSES THE
EXPRESSION OF AUH, WHILE AGMATINE INDUCES IT.
PATHWAY: PUTRESCINE AND SPERMIDINE BIOSYNTHESIS.
SIMILARITY: BELONGS TO THE ARGINASE FAMILY.
|
| 0.331082 | + | yecI | b1902 | ferritin-like protein |
EG13175 |
SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL).
SIMILARITY: BELONGS TO THE FERRITIN FAMILY. PROKARYOTIC SUBFAMILY.
|
 |  | b1903 | b1903 | orf, hypothetical protein |
EG13242 |
 |
| 0.323243 | - | b1481 | b1481 | orf, hypothetical protein |
EG14301 |
 |
 |  | rpsV | b1480 | 30S ribosomal subunit protein S22 |
EG11508 |
MASS SPECTROMETRY: MW=5095.9; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S22P FAMILY OF RIBOSOMAL PROTEINS.
|
 |  | sfcA | b1479 | NAD-linked malate dehydrogenase (malic enzyme) |
EG10948 |
CATALYTIC ACTIVITY: (S)-MALATE + NAD(+) = PYRUVATE + CO(2) + NADH.
SUBUNIT: HOMOTETRAMER (PROBABLE).
SIMILARITY: BELONGS TO THE MALIC ENZYMES FAMILY.
|
 |  | adhP | b1478 | alcohol dehydrogenase |
EG12622 |
FUNCTION: PREFERRED SPECIFICITY IS TOWARDS 1-PROPANOL.
CATALYTIC ACTIVITY: ALCOHOL + NAD(+) = ALDEHYDE OR KETONE + NADH.
COFACTOR: REQUIRES ZINC FOR ITS ACTIVITY.
SIMILARITY: BELONGS TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE
FAMILY.
|
 |  | yddM | b1477 | orf, hypothetical protein |
EG13784 |
SIMILARITY: BELONGS TO THE VAPA/VAPI FAMILY.
|
| 0.322969 | + | hyfA | b2481 | hydrogenase 4 Fe-S subunit |
EG11150 |
FUNCTION: PROBABLE ELECTRON TRANSFER PROTEIN FOR HYDROGENASE 4.
SIMILARITY: TO E.COLI DMSO REDUCTASE B SUBUNIT (DMSB).
SIMILARITY: THE IRON-SULFUR CENTERS ARE SIMILAR TO THOSE OF
'BACTERIAL-TYPE' 4FE-4S FERREDOXINS.
|
 |  | hyfB | b2482 | hydrogenase 4 membrane subunit |
EG11282 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(BY SIMILARITY).
SIMILARITY: TO POLYPEPTIDE 5 OF THE NADH-UBIQUINOL OXIDOREDUCTASE
OF CHLOROPLASTS OR MITOCHONDRIA.
|
 |  | hyfC | b2483 | hydrogenase 4 membrane subunit |
EG14211 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE COMPLEX I SUBUNIT 1 FAMILY.
|
 |  | hyfD | b2484 | hydrogenase 4 membrane subunit |
EG14212 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(BY SIMILARITY).
SIMILARITY: TO POLYPEPTIDE 5 OF THE NADH-UBIQUINOL OXIDOREDUCTASE
OF CHLOROPLASTS OR MITOCHONDRIA.
|
 |  | hyfE | b2485 | hydrogenase 4 membrane subunit |
EG14213 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
|
 |  | hyfF | b2486 | hydrogenase 4 membrane subunit |
EG14214 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(BY SIMILARITY).
SIMILARITY: TO POLYPEPTIDE 5 OF THE NADH-UBIQUINOL OXIDOREDUCTASE
OF CHLOROPLASTS OR MITOCHONDRIA.
|
 |  | hyfG | b2487 | hydrogenase 4 subunit |
EG14215 |
COFACTOR: BINDS A 4FE-4S CLUSTER.
SIMILARITY: BELONGS TO THE COMPLEX I 49 KDA SUBUNIT FAMILY.
|
 |  | hyfH | b2488 | hydrogenase 4 Fe-S subunit |
EG14216 |
FUNCTION: PROBABLE ELECTRON TRANSFER PROTEIN FOR HYDROGENASE 4.
SIMILARITY: THE IRON-SULFUR CENTERS ARE SIMILAR TO THOSE OF
'BACTERIAL-TYPE' 4FE-4S FERREDOXINS.
|
 |  | hyfI | b2489 | hydrogenase 4 Fe-S subunit |
EG14217 |
COFACTOR: MAY CONTAIN AN IRON-SULFUR 4FE-4S CLUSTER.
SIMILARITY: BELONGS TO THE COMPLEX I 20 KDA SUBUNIT FAMILY.
|
 |  | b2490 | b2490 | putative protein processing element |
EG14218 |
SIMILARITY: TO E.COLI HYCH.
|
 |  | 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.
|
| 0.315240 | + | ygjR | b3087 | orf, hypothetical protein |
EG12729 |
SIMILARITY: BELONGS TO THE GFO/IDH/MOCA FAMILY. STRONG, TO
B.SUBTILIS YULF.
|