Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 20.664829 | + | nadA | b0750 | quinolinate synthetase, A protein |
EG10630 |
PATHWAY: QUINOLINATE (PYRIDINE-2,3-DICARBOXYLATE) BIOSYNTHESIS
(NOTE: QUINOLINATE FORMATION OCCURS VIA 4 DIFFERENT PATHWAYS
DEPENDING ON THE ORGANISM). INVOLVED IN DE NOVO BIOSYNTHESIS OF
NAD.
SUBUNIT: HETERODIMER. THE QUINOLINATE SYNTHETASE COMPLEX CONSISTS
OF THE TWO ENZYMES QUINOLINATE SYNTHETASE A AND B.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: TO OTHER QUINOLINATE SYNTHETASE A.
CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO
FRAMESHIFTS.
|
 | | pnuC | b0751 | required for NMN transport |
EG11700 |
FUNCTION: REQUIRED FOR NMN TRANSPORT ACROSS THE CYTOPLASMIC
MEMBRANE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
INDUCTION: REPRESSED BY NADR.
|
| 20.057130 | - | 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.
|
| 18.891947 | - | leuA | b0074 | 2-isopropylmalate synthase |
EG11226 |
FUNCTION: CATALYZES CONDENSATION OF ACETYL-COA AND 2-
OXOISOVALERATE TO FORM 2-ISOPROPYLMALATE SYNTHASE.
CATALYTIC ACTIVITY: 3-CARBOXY-3-HYDROXY-4-METHYLPENTANOATE + COA =
ACETYL-COA + 3-METHYL-2-OXOBUTANOATE + H(2)O.
PATHWAY: FIRST STEP IN LEUCINE BIOSYNTHESIS.
SUBUNIT: HOMOTETRAMER.
SIMILARITY: BELONGS TO THE ALPHA-IPM SYNTHETASE / HOMOCITRATE
SYNTHASE FAMILY.
|
| | leuB | b0073 | 3-isopropylmalate dehydrogenase |
EG11577 |
CATALYTIC ACTIVITY: 3-CARBOXY-2-HYDROXY-4-METHYLPENTANOATE +
NAD(+) = 3-CARBOXY-4-METHYL-2-OXOPENTANOATE + NADH (THE PRODUCT
DECARBOXYLATES TO 4-METHYL-2-OXOPENTANOATE).
PATHWAY: THIRD STEP IN LEUCINE BIOSYNTHESIS.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ISOCITRATE AND ISOPROPYLMALATE
DEHYDROGENASES FAMILY.
|
| | leuC | b0072 | 3-isopropylmalate isomerase (dehydratase) subunit |
EG11576 |
CATALYTIC ACTIVITY: 3-ISOPROPYLMALATE = 2-ISOPROPYLMALEATE +
H(2)O (ALSO CATALYSES 2-ISOPROPYLMALEATE + H(2)O = 3-HYDROXY-
4-METHYL-3-CARBOXYPENTANONE).
PATHWAY: SECOND STEP IN LEUCINE BIOSYNTHESIS.
SUBUNIT: CONSISTS OF TWO DIFFERENT SUBUNITS: LEUC AND LEUD.
SIMILARITY: BELONGS TO THE ACONITASE/IPM ISOMERASE FAMILY.
|
| | leuD | b0071 | isopropylmalate isomerase subunit |
EG11575 |
CATALYTIC ACTIVITY: 3-ISOPROPYLMALATE = 2-ISOPROPYLMALEATE +
H(2)O (ALSO CATALYSES 2-ISOPROPYLMALEATE + H(2)O = 3-HYDROXY-
4-METHYL-3-CARBOXYPENTANONE).
PATHWAY: SECOND STEP IN LEUCINE BIOSYNTHESIS.
SUBUNIT: CONSISTS OF TWO DIFFERENT SUBUNITS: LEUC AND LEUD.
|
| 17.526725 | - | mutM | b3635 | formamidopyrimidine DNA glycosylase |
EG10329 |
FUNCTION: THIS ENZYME MAY PLAY A SIGNIFICANT ROLE IN PROCESSES
LEADING TO RECOVERY FROM MUTAGENESIS AND/OR CELL DEATH BY
ALKYLATING AGENTS. ALSO INVOLVED IN THE GO SYSTEM RESPONSIBLE FOR
REMOVING AN OXIDATIVELY DAMAGED FORM OF GUANINE (7,8-DIHYDRO-8-
OXOGUANINE = 7-OXOG) FROM DNA. CAN ALSO NICK DNA AT
APURINIC/APYRIMIDINIC SITES (AP SITES).
CATALYTIC ACTIVITY: HYDROLYSIS OF THE DEOXYRIBOSE N-GLYCOSIDIC
BOND TO EXCISE 2,6-DIAMINO-4-HYDROXY-5N-METHYLFORMAMIDOPYRIMIDINE
(FAPY) OR 4,6-DIAMINO-5-FORMAMIDOPYRIMIDINE.
COFACTOR: BINDS ONE ZINC ION PER MOLECULE.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE FPG FAMILY.
|
| 16.719958 | - | yhbC | b3170 | orf, hypothetical protein |
EG11179 |
SIMILARITY: BELONGS TO THE UPF0090 FAMILY.
CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A
FRAMESHIFT IN POSITION 9.
|
| | nusA | b3169 | transcription pausing; L factor |
EG10665 |
FUNCTION: NUSA PARTICIPATES IN BOTH THE TERMINATION AND
ANTITERMINATION OF TRANSCRIPTION. NUSA BINDS DIRECTLY TO THE CORE
ENZYME OF THE DNA-DEPENDENT RNA POLYMERASE. NUSA ALSO INTERACTS
WITH LAMBDA N PROTEIN, RNA, RHO FACTOR, AND PERHAPS NUSB.
INDUCTION: IN RESPONSE TO LOW TEMPERATURE.
SIMILARITY: BELONGS TO THE NUSA FAMILY.
|
| | infB | b3168 | protein chain initiation factor IF-2 |
EG10505 |
FUNCTION: IF-2, ONE OF THE ESSENTIAL COMPONENTS FOR THE INITIATION
OF PROTEIN SYNTHESIS IN VITRO, PROTECTS FORMYLMETHIONYL-TRNA FROM
SPONTANEOUS HYDROLYSIS AND PROMOTES ITS BINDING TO THE 30S
RIBOSOMAL SUBUNITS. IT IS ALSO INVOLVED IN THE HYDROLYSIS OF GTP
DURING THE FORMATION OF THE 70S RIBOSOMAL COMPLEX.
SUBCELLULAR LOCATION: CYTOPLASMIC.
ALTERNATIVE PRODUCTS: USING ALTERNATIVE INITIATION CODONS IN THE
SAME READING FRAME, THE GENE TRANSLATES INTO THREE ISOZYMES:
ALPHA, BETA AND BETA'.
SIMILARITY: BELONGS TO THE IF-2 FAMILY.
|
| 16.512731 | + | arsR | b3501 | transcriptional repressor of chromosomal ars operon |
EG12235 |
FUNCTION: TRANSCRIPTIONAL REPRESSOR FOR THE ARSEFG OPERON. ARSE IS
A TRANS-ACTING REGULATORY PROTEIN WHICH CONTROLS ITS OWN
EXPRESSION. THE REPRESSIVE EFFECT OF ARSE IS ALLEVIATED BY OXYIONS
OF +III OXIDATION STATE OF ARSENIC, ANTIMONY, AND BISMUTH, AS WELL
AS ARSENATE (AS(V)) (BY SIMILARITY).
SUBUNIT: BINDS DNA AS AN HOMODIMER (BY SIMILARITY).
SIMILARITY: BELONGS TO THE ARSR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| | arsB | b3502 | arsenical pump membrane protein |
EG12236 |
FUNCTION: INVOLVED IN ARSENICAL RESISTANCE. THOUGHT TO FORM THE
CHANNEL OF AN ARSENITE PUMP (BY SIMILARITY).
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
|
| | arsC | b3503 | arsenate reductase |
EG12237 |
FUNCTION: REDUCTION OF ARSENATE [AS(V)] TO ARSENITE [AS(III)].
THIS PROTEIN EXPANDS THE SUBSTRATE SPECIFICITY OF ARSAB PUMP WHICH
CAN EXTRUDE ARSENITE AND ANTIMONITE TO ALLOW FOR ARSENATE PUMPING
AND RESISTANCE (BY SIMILARITY).
SIMILARITY: BELONGS TO THE ARSC FAMILY.
|
| 12.113099 | - | sspA | b3229 | regulator of transcription; stringent starvation protein A |
EG10977 |
FUNCTION: FORMS AN EQUIMOLAR COMPLEX WITH THE RNA POLYMERASE
HOLOENZYME (RNAP) BUT NOT WITH THE CORE ENZYME, IT IS SYNTHESIZED
PREDOMINANTLY WHEN CELLS ARE EXPOSED TO AMINO ACID STARVATION, AT
WHICH TIME IT ACCOUNTS FOR OVER 50% OF THE TOTAL PROTEIN
SYNTHESIZED. IT IS INVOLVED IN THE TRANSITION FROM P1 EARLY TO P1
LATE GENE EXPRESSION. RNK AND SSPA CAN FUNCTIONALLY REPLACE
P.AERUGINOSA ALGINATE REGULATORY GENE ALGR2.
INDUCTION: BY AMINO ACID STARVATION.
SIMILARITY: BELONGS TO THE GST SUPERFAMILY. HSP26 FAMILY. STRONG,
TO OTHER BACTERIAL SSPA.
|
| | sspB | b3228 | stringent starvation protein B |
EG10978 |
FUNCTION: SEEMS TO ACT IN CONCERT WITH SSPA IN THE REGULATION
OF SEVERAL PROTEINS DURING EXPONENTIAL AND STATIONARY-PHASE
GROWTH. THE EXACT FUNCTION OF SSPB IS NOT YET KNOWN.
INDUCTION: BY AMINO ACID STARVATION.
|
| 9.631111 | + | yceK | b1050 | orf, hypothetical protein |
EG12689 |
SIMILARITY: TO E.COLI YIDQ.
|
| 9.442569 | - | insA_1 | b0022 | IS1 protein InsA |
|
|
| | insB_1 | b0021 | IS1 protein InsB |
EG40002 |
FUNCTION: ABSOLUTELY REQUIRED FOR TRANSPOSITION OF IS1.
SIMILARITY: TO INSB PROTEINS OF OTHER IS1 ELEMENTS.
|
| 9.389099 | + | htrC | b3989 | heat shock protein htrC |
EG11429 |
MISCELLANEOUS: INACTIVATION OF THE HTRC GENE RESULTS IN THE
INABILITY TO FORM COLONIES AT 42 DEGREES CELSIUS. AT 43 DEGREES
CELSIUS, HTRC MUTANT BACTERIA GRADUALLY LYSE, WHEREAS AT
INTERMEDIATE TEMPERATURES THEY FILAMENT EXTENSIVELY.
|
| 6.206825 | + | cdh | b3918 | CDP-diacylglycerol phosphotidylhydrolase |
EG10138 |
CATALYTIC ACTIVITY: CDP-DIACYLGLYCEROL + H(2)O = CMP +
PHOSPHATIDATE.
PATHWAY: PHOSPHOLIPID BIOSYNTHESIS.
SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED.
SIMILARITY: BELONGS TO THE CDH FAMILY.
CAUTION: REF.2 SEQUENCE WAS INCORRECT IN THE CENTRAL PART DUE
TO A FRAMESHIFT.
|
| 5.995466 | + | yhdT | b3257 | orf, hypothetical protein |
EG12831 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0974B.
CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A
FRAMESHIFT.
|
| | panF | b3258 | sodium/pantothenate symporter |
EG10685 |
FUNCTION: CATALYZES THE SODIUM-DEPENDENT UPTAKE OF EXTRACELLULAR
PANTOTHENATE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE SODIUM:SOLUTE SYMPORTER FAMILY (SSF).
|
| | prmA | b3259 | methylase for 50S ribosomal subunit protein L11 |
EG11497 |
FUNCTION: METHYLATES RIBOSOMAL PROTEIN L11.
SIMILARITY: TO OTHER METHYLTRANSFERASES.
|
| 5.470151 | - | btuC | b1711 | vitamin B12 transport permease protein |
EG10127 |
FUNCTION: PART OF THE BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM
FOR VITAMIN B12. PROBABLY RESPONSIBLE FOR THE TRANSLOCATION OF THE
SUBSTRATE ACROSS THE MEMBRANE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: WITH INTEGRAL MEMBRANE COMPONENTS OF OTHER BINDING-
PROTEIN-DEPENDENT TRANSPORT SYSTEMS. BELONGS TO THE FECCD
SUBFAMILY.
|
| | btuE | b1710 | vitamin B12 transport |
EG10129 |
FUNCTION: NOT ESSENTIAL FOR B12 TRANSPORT; HOWEVER, IT IS AN
AUXILIARY COMPONENT OF THE TRANSPORT SYSTEM.
SUBCELLULAR LOCATION: PERIPLASMIC (PROBABLE).
SIMILARITY: BELONGS TO THE GLUTATHIONE PEROXIDASE FAMILY.
|
| | btuD | b1709 | ATP-binding component of vitamin B12 transport system |
EG10128 |
FUNCTION: PART OF THE BINDING-PROTEIN-DEPENDENT TRANSPORT SYSTEM
FOR VITAMIN B12. PROBABLY RESPONSIBLE FOR ENERGY COUPLING TO
THE TRANSPORT SYSTEM.
SUBCELLULAR LOCATION: INNER MEMBRANE-ASSOCIATED.
SIMILARITY: BELONGS TO THE ATP-BINDING TRANSPORT PROTEIN FAMILY
(ABC TRANSPORTERS).
|
| | nlpC | b1708 | lipoprotein |
EG11133 |
SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID
ANCHOR (PROBABLE).
SIMILARITY: BELONGS TO THE E.COLI NLPC / LISTERIA P60 FAMILY.
|
| 5.269554 | - | lig | b2411 | DNA ligase |
EG10534 |
FUNCTION: THIS PROTEIN CATALYZES THE FORMATION OF PHOSPHODIESTER
LINKAGES BETWEEN 5'-PHOSPHORYL AND 3'-HYDROXYL GROUPS IN DOUBLE-
STRANDED DNA USING NAD AS A COENZYME AND AS THE ENERGY SOURCE FOR
THE REACTION. IT IS ESSENTIAL FOR DNA REPLICATION AND REPAIR OF
DAMAGED DNA.
CATALYTIC ACTIVITY: NAD(+) + (DEOXYRIBONUCLEOTIDE)(N) +
(DEOXYRIBONUCLEOTIDE)(M) = AMP + NICOTINAMIDE NUCLEOTIDE +
(DEOXYRIBONUCLEOTIDE)(N+M).
SIMILARITY: BELONGS TO THE NAD-DEPENDENT DNA LIGASE FAMILY.
CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A
FRAMESHIFT IN POSITIONS 289-313.
|
| 4.802867 | + | ybfM | b0681 | orf, hypothetical protein |
EG13659 |
|
| | ybfN | b0682 | orf, hypothetical protein |
EG13660 |
SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID
ANCHOR (PROBABLE).
|
| 4.346689 | - | b2531 | b2531 | orf, hypothetical protein |
EG13397 |
SIMILARITY: BELONGS TO THE UPF0074 (RFF2) FAMILY. STRONG,
TO H.INFLUENZAE HI0379.
SIMILARITY: BELONGS TO THE THERMONUCLEASE FAMILY.
|
| | yfhO | b2530 | putative aminotransferase |
EG12677 |
FUNCTION: CATALYZES THE REMOVAL OF ELEMENTAL SULFUR AND SELENIUM
ATOMS FROM CYSTEINE AND SELENOCYSTEINE TO PRODUCE ALANINE.
FUNCTIONS AS A SULFUR DELIVERY PROTEIN FOR NAD, BIOTIN AND FE-S
CLUSTER SYNTHESIS. TRANSFERS SULFUR ON CYS-456 OF THII IN A
TRANSPERSULFIDATION REACTION. FUNCTIONS ALSO AS A SELENIUM
DELIVERY PROTEIN IN THE PATHWAY FOR THE BIOSYNTHESIS OF
SELENOPHOSPHATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
SIMILARITY: BELONGS TO CLASS-V OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES. NIFS/ISCS SUBFAMILY.
|
| | b2529 | b2529 | orf, hypothetical protein |
EG13395 |
FUNCTION: MAY BE INVOLVED IN THE FORMATION OR REPAIR OF [FE-S]
CLUSTERS PRESENT IN IRON-SULFUR PROTEINS (POTENTIAL).
SIMILARITY: BELONGS TO THE NIFU FAMILY.
|
| | yfhF | b2528 | putative regulator |
EG12132 |
SIMILARITY: BELONGS TO THE HESB/YADR/YFHF FAMILY. STRONG, TO
H.INFLUENZAE HI0376.
CAUTION: REF.1 DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS.
|
| | yfhE | b2527 | orf, hypothetical protein |
EG12131 |
FUNCTION: CO-CHAPERONE THAT INTERACTS WITH HSCA AND STIMULATES
ITS ATPASE ACTIVITY.
SIMILARITY: CONTAINS 1 J DOMAIN.
|
| | hscA | b2526 | heat shock protein, chaperone, member of Hsp70 protein family |
EG12130 |
FUNCTION: PROBABLE CHAPERONE. HAS A LOW INTRINSIC ATPASE ACITIVITY
WHICH IS MARKEDLY STIMULATED BY HSCB.
INDUCTION: BY COLD SHOCK.
SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 70 FAMILY.
|
| | fdx | b2525 | [2FE-2S] ferredoxin, electron carrer protein |
EG11328 |
FUNCTION: FERREDOXIN ARE IRON-SULFUR PROTEINS THAT TRANSFER
ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. ALTHOUGH THE
FUNCTION OF THIS FERREDOXIN IS UNKNOWN IT IS PROBABLE THAT IT
HAS A ROLE AS A CELLULAR ELECTRON TRANSFER PROTEIN.
COFACTOR: BINDS A 2FE-2S CLUSTER.
SIMILARITY: BELONGS TO THE ADRENODOXIN / PUTIDAREDOXIN FAMILY.
|
| | yfhJ | b2524 | orf, hypothetical protein |
EG12311 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0371.
|
| | pepB | b2523 | putative peptidase |
EG12310 |
COFACTOR: ACTIVATED BY MANGANESE (BY SIMILARITY).
SIMILARITY: BELONGS TO PEPTIDASE FAMILY M17; ALSO KNOWN AS THE
CYTOSOL AMINOPEPTIDASE FAMILY.
|
| | sseB | b2522 | enhanced serine sensitivity |
EG11601 |
FUNCTION: MAY BE INVOLVED IN THE ENHANCEMENT OF SERINE-
SENSITIVITY.
|
| 4.145297 | + | tra8_2 | b1404 | IS30 transposase |
|
|
| 4.134829 | + | yjgP | b4261 | orf, hypothetical protein |
EG12535 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: STRONG, TO H.INFLUENZAE HI1704.
|
| | yjgQ | b4262 | orf, hypothetical protein |
EG12536 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: STRONG, TO H.INFLUENZAE HI1703.
|
| 4.108628 | - | ychM | b1206 | orf, hypothetical protein |
EG12392 |
FUNCTION: POSSIBLE SULFATE TRANSPORTER.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE SULFATE PERMEASE FAMILY.
|
| 4.014387 | - | aspC | b0928 | aspartate aminotransferase |
EG10096 |
CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE +
L-GLUTAMATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| 3.802051 | - | tra8_3 | b4284 | IS30 transposase |
|
|
| 3.730640 | + | b1228 | b1228 | orf, hypothetical protein |
|
|
| 3.570955 | + | yeaD | b1780 | orf, hypothetical protein |
EG12679 |
SIMILARITY: BELONGS TO THE UPF0010 FAMILY. SIGNIFICANTLY RELATED
TO MUTAROTASE.
|
| 3.529706 | + | 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.
|
| 3.405009 | - | fumC | b1611 | fumarase C= fumarate hydratase Class II; isozyme |
EG10358 |
CATALYTIC ACTIVITY: L-MALATE = FUMARATE + H(2)O.
PATHWAY: TRICARBOXYLIC ACID CYCLE.
SUBUNIT: HOMOTETRAMER.
SIMILARITY: TO OTHER THERMOSTABLE CLASS II FUMARASES.
|
| 3.056883 | + | 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.
|
| 3.054628 | + | b1904 | b1904 | orf, hypothetical protein |
EG14036 |
|
| 2.877384 | + | aslB | b3800 | putative arylsulfatase regulator |
EG10090 |
FUNCTION: POTENTIAL POSITIVE FACTOR FOR THE REGULATION OF
ARYLSULFATASE.
SIMILARITY: BELONGS TO THE ASLB/ATSB FAMILY.
|
| 2.828107 | - | yeeO | b1985 | orf, hypothetical protein |
EG13383 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: BELONGS TO THE MULTI ANTIMICROBIAL EXTRUSION (MATE)
FAMILY.
|
| 2.758640 | + | csgC | b1043 | putative curli production protein |
EG13414 |
SIMILARITY: STRONG, TO SALMONELLA CSGC.
|
| | b1044 | b1044 | orf, hypothetical protein |
EG13873 |
SIMILARITY: SOME, TO THE N-TERMINAL OF THE FIMA/PAPA FAMILY OF
FIMBRIA PROTEINS.
|
| | b1045 | b1045 | putative polyprotein |
|
|
| | ymdC | b1046 | putative synthase |
EG13875 |
SIMILARITY: BELONGS TO THE PHOSPHOLIPDASE D FAMILY. CARDIOLIPIN
SYNTHASE SUBFAMILY. STRONG, TO H.PYLORI HP0190.
|
| 2.747913 | + | b2080 | b2080 | orf, hypothetical protein |
EG14059 |
SIMILARITY: STRONG, TO ORTHOLOG IN P.STUTZERI.
|
| | yegQ | b2081 | orf, hypothetical protein |
EG14060 |
SIMILARITY: BELONGS TO PEPTIDASE FAMILY U32.
SIMILARITY: STRONG, TO H.INFLUENZAE HI0419.
|
| 2.701674 | + | pabC | b1096 | 4-amino-4-deoxychorismate lyase |
EG11493 |
FUNCTION: CONVERTS 4-AMINO-4-DEOXYCHORISMATE INTO 4-AMINOBENZOATE
(PABA) AND PYRUVATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: SECOND STEP IN FOLATE BIOSYNTHESIS PATHWAY.
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO CLASS-IV OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| | yceG | b1097 | putative thymidylate kinase (EC 2.7.4.9) |
EG11494 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0457.
|
| | tmk | b1098 | thymidylate kinase |
EG12302 |
FUNCTION: PHOSPHORYLATION OF DTMP TO FORM DTDP IN BOTH DE
NOVO AND SALVAGE PATHWAYS OF DTTP SYNTHESIS.
CATALYTIC ACTIVITY: ATP + THYMIDINE 5'-PHOSPHATE =
ADP + THYMIDINE 5'-DIPHOSPHATE.
SIMILARITY: BELONGS TO THE THYMIDYLATE KINASE FAMILY.
CAUTION: REF.4 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO
FRAMESHIFTS.
|
| | holB | b1099 | DNA polymerase III, delta prime subunit |
EG11500 |
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.
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].
|
| | ycfH | b1100 | orf, hypothetical protein |
EG12303 |
SIMILARITY: BELONGS TO THE TATD DNASE FAMILY. STRONG, TO
H.INFLUENZAE HI0454.
|
| 2.399646 | + | yfiM | b2586 | orf, hypothetical protein |
EG12857 |
|
| 2.329982 | - | celA | b1738 | PEP-dependent phosphotransferase enzyme IV for cellobiose, arbutin, and salicin |
EG10140 |
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.
SIMILARITY: CONTAINS A PTS EIIB DOMAIN.
|
| | celB | b1737 | PEP-dependent phosphotransferase enzyme II for cellobiose, arbutin, and salicin |
EG10141 |
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.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: CONTAINS A PTS EIIC DOMAIN.
|
| | celC | b1736 | PEP-dependent phosphotransferase enzyme III for cellobiose, arbutin, and salicin |
EG10142 |
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.
SIMILARITY: CONTAINS A PTS EIIA DOMAIN.
|
| | celD | b1735 | negative transcriptional regulator of cel operon |
EG10143 |
FUNCTION: REPRESSOR FOR THE CELABCF OPERON.
SIMILARITY: BELONGS TO THE ARAC/XYLS FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| | celF | b1734 | phospho-beta-glucosidase; cryptic |
EG10144 |
FUNCTION: HYDOLYZES A WIDE VARIETY OF P-BETA-GLUCOSIDES INCLUDING
CELLUBIOSE-6P, SALICIN-6P, ARBUTIN-6P, GENTIOBIOSE-6P, METHYL-
BETA-GLUCOSIDE-6P AND P-NITROPHENYL-BETA-D-GLUCOPYRANOSIDE-6P.
CATALYTIC ACTIVITY: 6-PHOSPHO-BETA-D-GLUCOSIDE-(1,4)-D-GLUCOSE +
H(2)O = D-GLUCOSE 6-PHOSPHATE + GLUCOSE.
COFACTOR: NAD AND A DIVALENT METAL ION. MANGANESE, COBALT AND
NICKEL IONS ENHANCE ACTIVITY WHEREAS MAGNESIUM, CALCIUM,
STRONTIUM AND ZINC IONS DO NOT.
PATHWAY: FERMENTATION OF THE BETA-GLUCOSIDES CELLOBIOSE,
ARBUTIN, AND SALICIN.
SIMILARITY: BELONGS TO FAMILY 4 OF GLYCOSYL HYDROLASES.
CAUTION: REF.1 AND REF.4 SEQUENCES DIFFER FROM THAT SHOWN IN
POSITIONS 371 ONWARD DUE TO NUMBER OF FRAMESHIFTS AS WELL AS OTHER
SEQUENCE ERRORS.
|
| | ydjC | b1733 | orf, hypothetical protein |
EG12198 |
INDUCTION: BY NICKEL.
|
| 2.320426 | - | 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.
|