Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 2.921986 | + | rbsD | b3748 | D-ribose high-affinity transport system; membrane-associated protein |
EG10817 |
FUNCTION: INVOLVED IN THE HIGH-AFFINITY RIBOSE MEMBRANE TRANSPORT
SYSTEM.
SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED (POTENTIAL).
|
 | | rbsA | b3749 | ATP-binding component of D-ribose high-affinity transport system |
EG10814 |
FUNCTION: PART OF THE BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM
FOR RIBOSE. PROBABLY RESPONSIBLE FOR ENERGY COUPLING TO THE
TRANSPORT SYSTEM.
SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED.
DOMAIN: COMPOSED OF TWO HOMOLOGOUS DOMAINS.
SIMILARITY: BELONGS TO THE ATP-BINDING TRANSPORT PROTEIN FAMILY
(ABC TRANSPORTERS). MGLA/RBSA SUBFAMILY.
|
| | rbsC | b3750 | D-ribose high-affinity transport system |
EG10816 |
FUNCTION: PART OF THE BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM
FOR RIBOSE. PROBABLY RESPONSIBLE FOR THE TRANSLOCATION OF THE
SUBSTRATE ACROSS THE MEMBRANE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: WITH INTEGRAL MEMBRANE COMPONENTS OF OTHER BINDING-
PROTEIN-DEPENDENT TRANSPORT SYSTEMS. BELONGS TO THE ARAH/RBSC
SUBFAMILY.
|
| | rbsB | b3751 | D-ribose periplasmic binding protein |
EG10815 |
FUNCTION: INVOLVED IN THE HIGH-AFFINITY D-RIBOSE MEMBRANE
TRANSPORT SYSTEM AND ALSO SERVES AS THE PRIMARY CHEMORECEPTOR FOR
CHEMOTAXIS.
SUBCELLULAR LOCATION: PERIPLASMIC.
SIMILARITY: BELONGS TO THE BACTERIAL EXTRACELLULAR SOLUTE-BINDING
RECEPTOR FAMILY 2.
|
| | rbsK | b3752 | ribokinase |
EG10818 |
CATALYTIC ACTIVITY: ATP + D-RIBOSE = ADP + D-RIBOSE 5-PHOSPHATE.
PATHWAY: FIRST STEP IN RIBOSE METABOLISM.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE PFKB FAMILY OF CARBOHYDRATE KINASES.
|
| | rbsR | b3753 | regulator for rbs operon |
EG10819 |
FUNCTION: TRANSCRIPTIONAL REPRESSOR FOR THE RIBOSE RBSDACBK
OPERON. RBSR BINDS TO A REGION OF PERFECT DYAD SYMMETRY SPANNING
THE RBS OPERON TRANSCRIPTIONAL START SITE. THE AFFINITY FOR THE
RBS OPERATOR IS REDUCED BY ADDITION OF RIBOSE, CONSISTENT WITH
RIBOSE BEING THE INDUCER OF THE OPERON.
SIMILARITY: BELONGS TO THE LACI FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 1.704770 | + | yjfH | b4180 | orf, hypothetical protein |
EG12483 |
SIMILARITY: BELONGS TO THE RNA METHYLTRANSFERASE TRMH FAMILY.
STRONG, TO H.INFLUENZAE HI0860.
|
| | yjfI | b4181 | orf, hypothetical protein |
EG12484 |
|
| | yjfJ | b4182 | putative alpha helical protein |
EG12485 |
|
| | yjfK | b4183 | orf, hypothetical protein |
EG12486 |
|
| | yjfL | b4184 | orf, hypothetical protein |
EG12487 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
|
| | yjfM | b4185 | orf, hypothetical protein |
EG12488 |
|
| | yjfC | b4186 | putative synthetase/amidase |
EG11812 |
SIMILARITY: STRONG, TO THE N-TERMINAL OF E.COLI GSP AND TO E.COLI
YGIC.
|
| | aidB | b4187 | putative acyl coenzyme A dehydrogenase |
EG11811 |
INDUCTION: BY ALKYLATING AGENTS.
SIMILARITY: BELONGS TO THE ACYL-COA DEHYDROGENASES FAMILY.
|
| 1.375077 | + | malT | b3418 | positive regulator of mal regulon |
EG10562 |
FUNCTION: MALT IS THE POSITIVE REGULATOR OF THE E.COLI MALTOSE
REGULON. IT BINDS AND RECOGNIZES A DNA MOTIF (CALLED THE MALT
BOX): 5'-GGA[TG]GA-3'. IT ALSO BINDS MALTOTRIOSE AND ATP.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE LUXR/UHPA FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 1.060359 | - | yhhW | b3439 | orf, hypothetical protein |
EG12943 |
SIMILARITY: BELONGS TO THE PIRIN FAMILY.
|
| 1.024724 | + | ygfA | b2912 | putative ligase |
EG11158 |
|
| 0.840724 | + | b1432 | b1432 | putative virulence protein |
|
|
| 0.747138 | + | ykfC | b0258 | orf, hypothetical protein |
EG13341 |
SIMILARITY: TO MITOCHONDRIAL AND CHLOROPLAST AND GROUP II INTRON
MATURASES AND TO RHIZOBIUM NGR234.
|
| 0.661449 | + | fhlA | b2731 | formate hydrogen-lyase transcriptional activator for fdhF, hyc and hyp operons |
EG10301 |
FUNCTION: REQUIRED FOR INDUCTION OF EXPRESSION OF THE FORMATE
DEHYDROGENASE H AND HYDROGENASE-3 STRUCTURAL GENES.
SIMILARITY: THE CENTRAL REGION CONTAINS A SIGMA-54 FACTOR
INTERACTION ATP-BINDING DOMAIN.
|
| 0.649005 | - | ompT | b0565 | outer membrane protein 3b (a), protease VII |
EG10673 |
FUNCTION: PROTEASE THAT CAN CLEAVE T7 RNA POLYMERASE, FERRIC
ENTEROBACTIN RECEPTOR PROTEIN (FEP) AND OTHER PROTEINS. THIS
PROTEASE HAS A SPECIFICITY FOR PAIRED BASIC RESIDUES. IT SEEMS
TO BE A SERINE PROTEASE.
CATALYTIC ACTIVITY: PREFERENTIAL CLEAVAGE: XAA-|-YAA IN WHICH BOTH
XAA AND YAA ARE ARG OR LYS.
ENZYME REGULATION: INHIBITED BY ZINC IONS.
SUBUNIT: HOMOPENTAMER (POSSIBLE).
SUBCELLULAR LOCATION: OUTER MEMBRANE.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S18; ALSO KNOWN AS THE
OMPTIN FAMILY.
|
| 0.595611 | + | yeaP | b1794 | orf, hypothetical protein |
EG13502 |
SIMILARITY: BELONGS TO THE YEGE/YHDA/YHJK/YJCC FAMILY.
|
| 0.417095 | + | b1836 | b1836 | orf, hypothetical protein |
EG14024 |
|
| | b1837 | b1837 | orf, hypothetical protein |
EG14025 |
|
| 0.319451 | - | fdhF | b4079 | selenopolypeptide subunit of formate dehydrogenase H |
EG10285 |
FUNCTION: DECOMPOSES FORMIC ACID TO HYDROGEN AND CARBON DIOXIDE
UNDER ANAEROBIC CONDITIONS IN THE ABSENCE OF EXOGENOUS ELECTRON
ACCEPTORS.
CATALYTIC ACTIVITY: FORMATE + NAD(+) = CO(2) + NADH.
COFACTOR: MOLYBDENUM, TWO MOLYBDOPTERIN GUANINE DINUCLEOTIDE (MGD)
COFACTORS, A 4FE-4S, AND SELENOCYSTEINE. THE ACTIVE-SITE
SELENOCYSTEINE IS ENCODED BY THE OPAL CODON, UGA.
SUBUNIT: CONSISTS OF TWO SEPARABLE ENZYMATIC ACTIVITIES: A FORMATE
DEHYDROGENASE COMPONENT (FDH-H) AND HYDROGENASE-3.
INDUCTION: BY FORMATE. REPRESSED BY OXYGEN, NITRATE, NITRITE, AND
OTHER ELECTRON ACCEPTORS.
SIMILARITY: BELONGS TO THE PROKARYOTIC MOLYBDOPTERIN-CONTAINING
OXIDOREDUCTASE FAMILY.
|
| | yjcO | b4078 | orf, hypothetical protein |
EG11951 |
|
| 0.298033 | + | hyaA | b0972 | hydrogenase-1 small subunit |
EG10468 |
FUNCTION: THIS IS ONE OF THREE E.COLI HYDROGENASES SYNTHESIZED IN
RESPONSE TO DIFFERENT PHYSIOLOGICAL CONDITIONS. HYD1 IS BELIEVED
TO HAVE A ROLE IN HYDROGEN CYCLING DURING FERMENTATIVE GROWTH.
CATALYTIC ACTIVITY: 2 REDUCED FERREDOXIN + 2 H(+) = 2 OXIDIZED
FERREDOXIN + H(2).
COFACTOR: CONTAINS NICKEL AND IRON-SULFUR.
SUBUNIT: HETERODIMER OF A LARGE AND A SMALL SUBUNIT.
SUBCELLULAR LOCATION: MEMBRANE-BOUND; PERIPLASMIC SIDE.
SIMILARITY: TO OTHER UPTAKE HYDROGENASES SMALL SUBUNIT.
|
| | hyaB | b0973 | hydrogenase-1 large subunit |
EG10469 |
FUNCTION: THIS IS ONE OF THREE E.COLI HYDROGENASES SYNTHESIZED IN
RESPONSE TO DIFFERENT PHYSIOLOGICAL CONDITIONS. HYD1 IS BELIEVED
TO HAVE A ROLE IN HYDROGEN CYCLING DURING FERMENTATIVE GROWTH.
CATALYTIC ACTIVITY: 2 REDUCED FERREDOXIN + 2 H(+) = 2 OXIDIZED
FERREDOXIN + H(2).
COFACTOR: CONTAINS NICKEL AND IRON-SULFUR.
SUBUNIT: HETERODIMER OF A LARGE AND A SMALL SUBUNIT.
SUBCELLULAR LOCATION: MEMBRANE-BOUND.
SIMILARITY: BELONGS TO THE [NIFE]/[NIFESE] HYDROGENASE LARGE
SUBUNIT FAMILY.
|
| | hyaC | b0974 | probable Ni/Fe-hydrogenase 1 b-type cytochrome subunit |
EG10470 |
FUNCTION: PROBABLE B-TYPE CYTOCHROME.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: BELONGS TO THE HUPC/HYAC/HYDC FAMILY.
|
| | hyaD | b0975 | processing of HyaA and HyaB proteins |
EG10471 |
FUNCTION: PROTEASE INVOLVED IN THE C-TERMINAL PROCESSING OF HYAB,
THE LARGE SUBUNIT OF HYDROGENASE 1 (POTENTIAL).
SIMILARITY: BELONGS TO PEPTIDASE FAMILY M52. ALSO KNOWN AS THE
HUPD/HYAD FAMILY.
|
| | hyaE | b0976 | processing of HyaA and HyaB proteins |
EG10472 |
FUNCTION: NOT KNOWN. COULD FORM, ALONG WITH HYAD, A COMPLEX
INVOLVED IN THE PROCESSING OF THE HYDROGENASE 1 STRUCTURAL OPERON.
SIMILARITY: BELONGS TO THE HUPG/HYAE FAMILY.
|
| | hyaF | b0977 | nickel incorporation into hydrogenase-1 proteins |
EG10473 |
FUNCTION: NOT KNOWN. COULD ENHANCE THE INCORPORATION OF NICKEL
TO THE HYDROGENASE.
SIMILARITY: BELONGS TO THE HUPH/HYAF FAMILY.
|
| | appC | b0978 | probable third cytochrome oxidase, subunit I |
EG11380 |
FUNCTION: CYTOCHROME OXIDASE SUBUNIT.
PATHWAY: TERMINAL STEP IN THE RESPIRATORY CHAIN.
SUBUNIT: HETERODIMER OF SUBUNITS I AND II (PROBABLE).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
INDUCTION: IS INDUCED WHEN BACTERIAL CULTURES REACH STATIONARY
PHASE; ITS SYNTHESIS IS TRIGGERED BY PHOSPHATE STARVATION OR A
SHIFT FROM AEROBIC TO ANAEROBIC CONDITIONS.
PTM: THE N-TERMINUS IS BLOCKED.
SIMILARITY: STRONG, TO E.COLI CYDA.
|
| | appB | b0979 | probable third cytochrome oxidase, subunit II |
EG11114 |
SIMILARITY: TO E.COLI YBGT.
|
| 0.288810 | + | frr | b0172 | ribosome releasing factor |
EG10335 |
FUNCTION: RESPONSIBLE FOR THE RELEASE OF RIBOSOMES FROM MESSENGER
RNA AT THE TERMINATION OF PROTEIN BIOSYNTHESIS. MAY INCREASE THE
EFFICIENCY OF TRANSLATION BY RECYCLING RIBOSOMES FROM ONE ROUND OF
TRANSLATION TO ANOTHER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE RRF FAMILY.
|
| | yaeM | b0173 | putative ATP-binding component of a transport system |
EG12715 |
FUNCTION: CATALYZES THE NADP-DEPENDENT REARRANGEMENT AND REDUCTION
OF 1-DEOXY-D-XYLULOSE-5-PHOSPHATE (DXP) TO 2-C-METHYL-D-
ERYTHRITOL 4-PHOSPHATE (MEP).
COFACTOR: REQUIRES A DIVALENT CATION: MAGNESIUM, MANGANESE OR
COBALT.
ENZYME REGULATION: INHIBITED BY FOSMIDOMYCIN.
PATHWAY: DEOXYXYLULOSE-5-PHOSPHATE PATHWAY (DXP) OF ISOPRENOID
BIOSYNTHESIS; SECOND STEP.
SUBUNIT: HOMOTETRAMER.
SIMILARITY: BELONGS TO THE DXR FAMILY.
|
| 0.286934 | - | gadB | b1493 | glutamate decarboxylase isozyme |
EG11490 |
FUNCTION: CATALYZES THE PRODUCTION OF GABA.
CATALYTIC ACTIVITY: L-GLUTAMATE = 4-AMINOBUTANOATE + CO(2).
COFACTOR: PYRIDOXAL PHOSPHATE.
SUBUNIT: HOMOHEXAMER.
SIMILARITY: BELONGS TO GROUP II DECARBOXYLASES (DDC, GAD, HDC AND
TYRDC).
|
| 0.284484 | - | ybdH | b0599 | putative oxidoreductase |
EG12692 |
SIMILARITY: BELONGS TO THE IRON-CONTAINING ALCOHOL DEHYDROGENASE
FAMILY. STRONG, TO BACTERIAL GLYCEROL DEHYDROGENASE.
|
| 0.274288 | - | thrS | b1719 | threonine tRNA synthetase |
EG11001 |
FUNCTION: THRS IS ALSO A TRANSLATIONAL REPRESSOR PROTEIN, IT
CONTROLS THE TRANSLATION OF ITS OWN GENE BY BINDING TO ITS MRNA.
CATALYTIC ACTIVITY: ATP + L-THREONINE + TRNA(THR) = AMP +
PYROPHOSPHATE + L-THREONYL-TRNA(THR).
COFACTOR: BINDS ONE ZINC ION.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
DOMAIN: THE C-TERMINAL DOMAIN RECOGNIZES THE ANTICODON BASES BUT
THE N-TERMINAL CONTRIBUTES ALSO TO THE PRECISE RECOGNITION OF
TRNA(THR) BY THRRS.
SIMILARITY: BELONGS TO CLASS-II AMINOACYL-TRNA SYNTHETASE FAMILY.
|
| | infC | b1718 | protein chain initiation factor IF-3 |
EG10506 |
FUNCTION: IF-3 BINDS TO THE 30S RIBOSOMAL SUBUNIT AND SHIFTS THE
EQUILIBRUM BETWEEN 70S RIBOSOMES AND THEIR 50S AND 30S SUBUNITS IN
FAVOR OF THE FREE SUBUNITS, THUS ENHANCING THE AVAILABILITY OF 30S
SUBUNITS ON WHICH PROTEIN SYNTHESIS INITIATION BEGINS.
FUNCTION: IF-3 IS ALSO A TRANSLATIONAL REPRESSOR PROTEIN, IT
CONTROLS THE TRANSLATION OF ITS OWN GENE BY BINDING TO ITS MRNA.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
MISCELLANEOUS: EXISTS IN 2 MAIN FORMS, IF-3L AND IF-3S. THERE IS
AT LEAST ONE MINOR FORM THAT DIFFERS FROM IF-3L ONLY IN THE
ABSENCE OF THE FIRST RESIDUE.
SIMILARITY: BELONGS TO THE IF-3 FAMILY.
|
| | rpmI | b1717 | 50S ribosomal subunit protein A |
EG11231 |
MASS SPECTROMETRY: MW=7158.0; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L35P FAMILY OF RIBOSOMAL PROTEINS.
CAUTION: REF.2 SEQUENCE HAS AN EXTRA BASE (BETWEEN 3 AND 4) WHICH
WAS HIDDING THIS PROTEIN READING FRAME.
|
| | rplT | b1716 | 50S ribosomal subunit protein L20, and regulator |
EG10881 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 23S RIBOSOMAL RNA AND IS
NECESSARY TO THE IN VITRO ASSEMBLY PROCESS OF THE 50S RIBOSOMAL
SUBUNIT; IT IS NOT INVOLVED IN THE PROTEIN SYNTHESIZING FUNCTIONS
OF THAT SUBUNIT.
MASS SPECTROMETRY: MW=13366.9; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L20P FAMILY OF RIBOSOMAL PROTEINS.
|
| | pheM | b1715 | phenylalanyl-tRNA synthetase (pheST) operon leader peptide |
EG11272 |
|
| 0.274239 | + | yfiL | b2602 | orf, hypothetical protein |
EG12446 |
CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-14 IS THE INITIATOR.
|
| 0.261681 | + | pfkA | b3916 | 6-phosphofructokinase I |
EG10699 |
CATALYTIC ACTIVITY: ATP + D-FRUCTOSE 6-PHOSPHATE = ADP +
D-FRUCTOSE 1,6-BISPHOSPHATE.
ENZYME REGULATION: SUBJECT TO ALLOSTERIC ACTIVATION BY ADP AND
OTHER DIPHOSPHONUCLEOSIDES, AND INHIBITION BY PHOSPHOENOLPYRUVATE.
PATHWAY: KEY CONTROL STEP OF GLYCOLYSIS.
SUBUNIT: HOMOTETRAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
MISCELLANEOUS: E.COLI HAS TWO 6-PHOSPHOFRUCTOKINASES ENZYMES.
SIMILARITY: PHOSPHOFRUCTOKINASE-1 SHOWS NO HOMOLOGY TO
PHOSPHOFRUCTOKINASE-2, THE MINOR PHOSPHOFRUCTOKINASE FOUND IN
E.COLI. ALTHOUGH THE REACTION CATALYSED IS THE SAME, THE TWO
ENZYMES HAVE A DIFFERENT EVOLUTIONARY ORIGIN.
SIMILARITY: BELONGS TO THE PHOSPHOFRUCTOKINASE FAMILY.
|
| 0.255332 | + | yeaV | b1801 | putative transport protein |
EG13508 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
SIMILARITY: BELONGS TO THE BCCT (TC 2.33) FAMILY OF TRANSPORTERS.
|
| | yeaW | b1802 | orf, hypothetical protein |
EG13509 |
COFACTOR: PROBABLY BINDS A 2FE-2S GROUP AND AN IRON ATOM.
SUBUNIT: PROBABLE HETERODIMER OF YEAW AND YEAX.
SIMILARITY: BELONGS TO THE BACTERIAL RING-HYDROXYLATING
DIOXYGENASE ALPHA SUBUNIT FAMILY.
|
| | yeaX | b1803 | putative diogenase beta subunit |
EG13510 |
COFACTOR: FMN (BY SIMILARITY).
SUBUNIT: PROBABLE HETERODIMER OF YEAW AND YEAX.
SIMILARITY: IN THE C-TERMINAL, BELONGS TO THE 2FE2S PLANT-TYPE
FERREDOXIN FAMILY.
SIMILARITY: BELONGS TO THE PDR/VANB FAMILY.
|
| 0.250394 | + | yjaA | b4011 | orf, hypothetical protein |
EG11206 |
|
| 0.247655 | + | yhcG | b3220 | orf, hypothetical protein |
EG12813 |
|
| 0.239744 | + | b1720 | b1720 | orf, hypothetical protein |
EG13983 |
SIMILARITY: CONTAINS 3 ANK REPEATS.
CAUTION: THIS IS A CONCEPTUAL TRANSLATION; A FRAMESHIFT HAD
TO BE INTRODUCED IN POSITION 142 TO PRODUCE THIS ORF.
|
| | b1721 | b1721 | orf, hypothetical protein |
|
|
| 0.225519 | + | pepQ | b3847 | proline dipeptidase |
EG10698 |
CATALYTIC ACTIVITY: HYDROLYSIS OF XAA-|-PRO DIPEPTIDES; ALSO
ACTS ON AMINOACYL-HYDROXYPROLINE ANALOGS. NO ACTION ON PRO-PRO.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY M24B.
CAUTION: REF.2 SEQUENCE WAS MUCH LONGER AND INCLUDED THE SEQUENCE
OF YIGZ DUE TO A FRAMESHIFT.
|
| | yigZ | b3848 | orf, hypothetical protein |
EG11484 |
SIMILARITY: BELONGS TO THE UPF0029 FAMILY. STRONG, TO H.INFLUENZAE
HI0722.
|
| | trkH | b3849 | potassium uptake, requires TrkE |
EG11021 |
FUNCTION: LOW-AFFINITY POTASSIUM TRANSPORT SYSTEM. INTERACTS WITH
TRK SYSTEM POTASSIUM UPTAKE PROTEIN TRKA AND REQUIRES TRKE FOR
TRANSPORT ACTIVITY.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
CAUTION: REF.2 AND REF.4 SEQUENCES DIFFER FROM THAT SHOWN IN
POSITION 418 ONWARD DUE TO FRAMESHIFTS.
|
| 0.217870 | + | pdhR | b0113 | transcriptional regulator for pyruvate dehydrogenase complex |
EG11088 |
FUNCTION: TRANSCRIPTIONAL REPRESSOR FOR THE PYRUVATE DEHYDROGENASE
COMPLEX GENES ACEEF AND LPD.
SIMILARITY: BELONGS TO THE GNTR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.212761 | + | sodB | b1656 | superoxide dismutase, iron |
EG10954 |
FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE
CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS.
CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2).
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO THE IRON/MANGANESE SUPEROXIDE DISMUTASE
FAMILY.
|
| 0.207935 | - | aroP | b0112 | aromatic amino acid transport protein |
EG10084 |
FUNCTION: PERMEASE THAT IS INVOLVED IN THE TRANSPORT ACROSS THE
CYTOPLASMIC MEMBRANE OF THE AROMATIC AMINO ACIDS (PHENYLALANINE,
TYROSINE, AND TRYPTOPHAN).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
INDUCTION: ITS ACTIVITY IS REGULATED BY PROTEIN TYRR.
SIMILARITY: BELONGS TO THE AMINO ACID PERMEASE FAMILY.
|
| 0.206549 | - | rnc | b2567 | RNase III, ds RNA |
EG10857 |
FUNCTION: DIGESTS DOUBLE-STRANDED RNA. INVOLVED IN THE PROCESSING
OF RIBOSOMAL RNA PRECURSORS AND OF SOME MRNAS.
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE TO 5'-PHOSPHO-
MONOESTER.
SUBUNIT: ORGANIZED INTO A STRUCTURE (PROCESSOME) CONTAINING A
NUMBER OF RNA-PROCESSING ENZYMES.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: CONTAINS 1 DRBM (DOUBLE-STRANDED RNA-BINDING) DOMAIN.
SIMILARITY: BELONGS TO THE RNASE III FAMILY.
|
| | era | b2566 | GTP-binding protein |
EG10270 |
FUNCTION: BINDS BOTH GDP AND GTP, HAS AN INTRINSIC GTPASE ACTIVITY
AND IS ESSENTIAL FOR CELL GROWTH.
SUBCELLULAR LOCATION: MEMBRANE-BOUND.
PTM: AUTOPHOSPHORYLATED.
SIMILARITY: BELONGS TO THE ERA/TRME FAMILY OF GTP-BINDING
PROTEINS. ERA SUBFAMILY.
SIMILARITY: CONTAINS 1 KH DOMAIN.
|
| | recO | b2565 | protein interacts with RecR and possibly RecF proteins |
EG10832 |
FUNCTION: INVOLVED IN DNA REPAIR AND RECF PATHWAY RECOMBINATION.
SIMILARITY: BELONGS TO THE RECO FAMILY.
|
| | pdxJ | b2564 | pyridoxine biosynthesis |
EG10693 |
FUNCTION: CATALYZES THE CONDENSATION OF 1-DEOXY-D-XYLULOSE-5-
PHOSPHATE (DXP) AND 1-AMINO-3-OXO-4-(PHOSPHOHYDROXY)PROPAN-2-ONE
TO FORM PYRIDOXINE 5'-PHOSPHATE (PNP).
PATHWAY: DE NOVO SYNTHESIS OF PYRIDOXINE (VITAMIN B6) AND
PYRIDOXAL PHOSPHATE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE PDXJ FAMILY.
CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO NUMEROUS
FRAMESHIFTS.
|
| | acpS | b2563 | CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase |
EG10247 |
FUNCTION: TRANSFERS THE 4'-PHOSPHOPANTETHEINE MOIETY FROM COENZYME
A TO THE SER-36 OF ACYL-CARRIER PROTEIN.
CATALYTIC ACTIVITY: COA + APO-[ACYL-CARRIER PROTEIN] = ADENOSINE
3',5'-BISPHOSPHATE + HOLO-[ACYL-CARRIER PROTEIN].
COFACTOR: REQUIRES MAGNESIUM.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
MASS SPECTROMETRY: MW=13950; METHOD=ELECTROSPRAY.
SIMILARITY: BELONGS TO THE ACPS FAMILY.
|
| 0.204924 | + | b2889 | b2889 | putative enzyme |
EG13072 |
FUNCTION: CATALYZES THE 1,3-ALLYLIC REARRANGEMENT OF THE
HOMOALLYLIC SUBSTRATE ISOPENTENYL (IPP) TO ITS ALLYLIC ISOMER,
DIMETHYLALLYL DIPHOSPHATE (DMAPP).
CATALYTIC ACTIVITY: ISOPENTENYL DIPHOSPHATE = DIMETHYLALLYL
DIPHOSPHATE.
COFACTOR: REQUIRES MAGNESIUM OR MANGANESE FOR ACTIVITY.
PATHWAY: ISOPRENOID BIOSYNTHESIS.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE IPP ISOMERASE TYPE 1 FAMILY.
|
| 0.198186 | + | b2603 | b2603 | orf, hypothetical protein |
EG14225 |
|
| | yfiN | b2604 | orf, hypothetical protein |
EG12880 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE YAIC / YFIN (E.COLI), YHCK (B.SUBTILIS)
FAMILY.
|
| | yfiB | b2605 | putative outer membrane protein |
EG11152 |
SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID
ANCHOR (POTENTIAL).
|
| 0.197429 | + | yicE | b3654 | putative transport protein |
EG11194 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (PROBABLE).
SIMILARITY: BELONGS TO THE XANTHINE/URACIL PERMEASES FAMILY.
|
| | yicH | b3655 | orf, hypothetical protein |
EG11684 |
|
| 0.194149 | + | b1978 | b1978 | putative factor |
|
|
| 0.193301 | + | holD | b4372 | DNA polymerase III, psi subunit |
EG11414 |
FUNCTION: DNA POLYMERASE III IS A COMPLEX, MULTICHAIN ENZYME
RESPONSIBLE FOR MOST OF THE REPLICATIVE SYNTHESIS IN BACTERIA.
THIS DNA POLYMERASE ALSO EXHIBITS 3' TO 5' EXONUCLEASE ACTIVITY.
THE EXACT FUNCTION OF THE PSI SUBUNIT IS UNKNOWN.
CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE =
N PYROPHOSPHATE + DNA(N).
SUBUNIT: CONTAINS A CORE (COMPOSED OF ALPHA, EPSILON, AND THETA
CHAINS) THAT ASSOCIATES WITH A TAU SUBUNIT WHICH ALLOW THE CORE
DIMERIZATION TO FORM THE POLIII' COMPLEX. POLIII' ASSOCIATES WITH
THE GAMMA COMPLEX (COMPOSED OF CHAINS GAMMA, DELTA, DELTA', PSI,
AND CHI) AND WITH THE BETA CHAIN. THE FINAL COMPOSITION OF THE
COMPLEX IS: (ALPHA,EPSILON,THETA)[2]-TAU[2]-(GAMMA,DELTA,DELTA',
PSI,CHI)[2]-BETA[4].
|
| | rimI | b4373 | acyltransferase for 30S ribosomal subunit protein S18; acetylation of N-terminal alanine |
EG10850 |
FUNCTION: THIS ENZYME ACETYLATES THE N-TERMINAL ALANINE OF
RIBOSOMAL PROTEIN S18.
CATALYTIC ACTIVITY: ACETYL-COA + RIBOSOMAL-PROTEIN L-ALANINE =
COA + RIBOSOMAL-PROTEIN N-ACETYL-L-ALANINE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ACETYLTRANSFERASE FAMILY. RIMI
SUBFAMILY.
|
| | yjjG | b4374 | putative phosphatase |
EG12115 |
SIMILARITY: TO E.COLI YIGB.
|
| | prfC | b4375 | peptide chain release factor RF-3 |
EG12114 |
FUNCTION: INCREASES THE FORMATION OF RIBOSOMAL TERMINATION
COMPLEXES AND STIMULATES ACTIVITIES OF RF-1 AND RF-2. IT BINDS
GUANINE NUCLEOTIDES AND HAS STRONG PREFERENCE FOR UGA STOP CODONS.
IT MAY INTERACT DIRECTLY WITH THE RIBOSOME. THE STIMULATION OF RF-
1 AND RF-2 IS SIGNIFICANTLY REDUCED BY GTP AND GDP, BUT NOT BY
GMP.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE GTP-BINDING ELONGATION FACTOR FAMILY.
PRFC SUBFAMILY.
|
| 0.191836 | + | ansA | b1767 | cytoplasmic L-asparaginase I |
EG10045 |
CATALYTIC ACTIVITY: L-ASPARAGINE + H(2)O = L-ASPARTATE + NH(3).
SUBUNIT: HOMOTETRAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
MISCELLANEOUS: KM = 3.5 X 10(-3) M.
MISCELLANEOUS: E.COLI CONTAINS TWO L-ASPARAGINASE ISOENZYMES:
L-ASPARAGINASE I, A LOW-AFFINITY ENZYME LOCATED IN THE CYTOPLASM,
AND L-ASPARAGINASE II, A HIGH-AFFINITY SECRETED ENZYME.
SIMILARITY: BELONGS TO THE ASPARAGINASE 1 FAMILY.
|
| | ydjB | b1768 | orf, hypothetical protein |
EG11135 |
CATALYTIC ACTIVITY: NICOTINAMIDE + H(2)O = NICOTINATE + NH(3).
PATHWAY: PYRIDINE NUCLEOTIDE CYCLE.
SIMILARITY: TO YEAST YGL037C.
|
| 0.191539 | + | yhhK | b3459 | orf, hypothetical protein |
EG12211 |
|