Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 4.876242 | + | b1627 | b1627 | orf, hypothetical protein |
 |
|
| | b1628 | b1628 | orf, hypothetical protein |
EG13934 |
SIMILARITY: BELONGS TO THE 4FE4S BACTERIAL-TYPE FERREDOXIN FAMILY.
STRONG, TO H.INFLUENZAE HI1684.
|
| | b1629 | b1629 | putative membrane protein |
|
|
| | ydgO | b1630 | orf, hypothetical protein |
EG13936 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE RNFD FAMILY. STRONG, TO H.INFLUENZAE
HI1686.
|
| | b1631 | b1631 | orf, hypothetical protein |
EG13937 |
SIMILARITY: BELONGS TO THE RNFG FAMILY. STRONG, TO H.INFLUENZAE
HI1687.
|
| | ydgQ | b1632 | orf, hypothetical protein |
EG13938 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: STRONG, TO H.INFLUENZAE HI1688.
SIMILARITY: TO H.INFLUENZAE HI0168.
|
| | nth | b1633 | endonuclease III; specific for apurinic and/or apyrimidinic sites |
EG10662 |
FUNCTION: HAS BOTH AN APURINIC AND/OR APYRIMIDINIC ENDONUCLEASE
ACTIVITY AND A DNA N-GLYCOSYLASE ACTIVITY. INCISES DAMAGED DNA AT
CYTOSINES, THYMINES AND GUANINES. ACTS ON A DAMAGED STRAND, 5'
FROM THE DAMAGED SITE. REQUIRED FOR THE REPAIR OF BOTH OXIDATIVE
DNA DAMAGE AND SPONTANEOUS MUTAGENIC LESIONS.
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE NEAR APURINIC OR
APYRIMIDINIC SITES TO PRODUCTS WITH 5'-PHOSPHATE.
COFACTOR: BINDS A 4FE-4S CLUSTER WHICH IS NOT IMPORTANT FOR THE
CATALYTIC ACTIVITY, BUT WHICH IS PROBABLY INVOLVED IN THE PROPER
POSITIONING OF THE ENZYME ALONG THE DNA STRAND.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE NTH/MUTY FAMILY.
|
| 4.808952 | + | pheA | b2599 | chorismate mutase-P and prephenate dehydratase |
EG10707 |
CATALYTIC ACTIVITY: CHORISMATE = PREPHENATE.
CATALYTIC ACTIVITY: PREPHENATE = PHENYLPYRUVATE + H(2)O + CO(2).
PATHWAY: L-PHENYLALANINE BIOSYNTHESIS.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: TO OTHER PDT ENZYMES OR DOMAINS.
|
| 4.523742 | + | mutT | b0099 | 7,8-dihydro-8-oxoguanine-triphosphatase, prefers dGTP, causes AT-GC transversions |
EG10626 |
FUNCTION: INVOLVED IN THE GO SYSTEM RESPONSIBLE FOR REMOVING AN
OXIDATIVELY DAMAGED FORM OF GUANINE (7,8-DIHYDRO-8-OXOGUANINE)
FROM DNA AND THE NUCLEOTIDE POOL. 8-OXO-DGTP IS INSERTED OPPOSITE
DA AND DC RESIDUES OF TEMPLATE DNA WITH ALMOST EQUAL EFFICIENCY
THUS LEADING TO A.T TO G.C TRANSVERSIONS. MUTT SPECIFICALLY
DEGRADES 8-OXO-DGTP TO THE MONOPHOSPHATE.
CATALYTIC ACTIVITY: 8-OXO-DGTP + H(2)O = 8-OXO-DGMP +
PYROPHOSPHATE.
COFACTOR: REQUIRES MAGNESIUM.
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE NUDIX HYDROLASE FAMILY.
|
| 4.437419 | + | yihF | b3861 | putative GTP-binding protein |
EG11832 |
SIMILARITY: TO E.COLI YDGA AND H.INFLUENZAE HI1236.
|
| 4.309176 | - | 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.
|
| 4.280503 | + | 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.
|
| 4.268076 | + | gst | b1635 | glutathionine S-transferase |
EG12613 |
FUNCTION: CONJUGATION OF REDUCED GLUTATHIONE TO A WIDE NUMBER OF
EXOGENOUS AND ENDOGENOUS HYDROPHOBIC ELECTROPHILES. OPTIMA OF PH
AND TEMPERATURE ARE 7.5 AND 35 DEGREES CELSIUS.
CATALYTIC ACTIVITY: RX + GLUTATHIONE = HX + R-S-GLUTATHIONE.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE GST SUPERFAMILY. BETA SUBFAMILY.
|
| 3.545897 | + | 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.
|
| 3.263988 | + | yacL | b0119 | orf, hypothetical protein |
EG12605 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI1724.
|
| 3.199192 | + | thrA | b0002 | aspartokinase I, homoserine dehydrogenase I |
EG10998 |
CATALYTIC ACTIVITY: L-HOMOSERINE + NAD(P)(+) = L-ASPARTATE
BETA-SEMIALDEHYDE + NAD(P)H.
CATALYTIC ACTIVITY: ATP + L-ASPARTATE = ADP + 4-PHOSPHO-L-
ASPARTATE.
ENZYME REGULATION: THE ENZYME ACTIVITIES ARE REGULATED
ALLOSTERICALLY BY L-THREONINE.
PATHWAY: CATALYZES 2 NONCONSECUTIVE REACTIONS IN THE COMMON
BIOSYNTHETIC PATHWAY LEADING FROM ASP TO DIAMINOPIMELATE AND LYS,
TO MET, AND TO THR AND ILE.
SUBUNIT: HOMOTETRAMER.
MISCELLANEOUS: ASPARTOKINASE II-HOMOSERINE DEHYDROGENASE II AND
ASPARTOKINASE III ALSO CATALYZE THE SAME REACTION(S).
SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE
ASPARTOKINASE FAMILY.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE
HOMOSERINE DEHYDROGENASE FAMILY.
|
| | thrB | b0003 | homoserine kinase |
EG10999 |
CATALYTIC ACTIVITY: ATP + L-HOMOSERINE = ADP + O-PHOSPHO-L-
HOMOSERINE.
PATHWAY: THREONINE BIOSYNTHESIS FROM ASPARATE; FOURTH STEP.
SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
SIMILARITY: BELONGS TO THE GHMP KINASE FAMILY. HOMOSERINE
KINASE SUBFAMILY.
|
| | thrC | b0004 | threonine synthase |
EG11000 |
CATALYTIC ACTIVITY: O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE +
ORTHOPHOSPHATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: THREONINE BIOSYNTHESIS.
|
| 3.195848 | - | trpE | b1264 | anthranilate synthase component I |
EG11028 |
CATALYTIC ACTIVITY: CHORISMATE + L-GLUTAMINE = ANTHRANILATE +
PYRUVATE + L-GLUTAMATE.
PATHWAY: FIRST STEP IN BIOSYNTHESIS OF TRYPTOPHAN.
SUBUNIT: TETRAMER OF TWO COMPONENTS I AND TWO COMPONENTS II.
MISCELLANEOUS: COMPONENT I CATALYZES THE FORMATION OF ANTHRANILATE
USING AMMONIA RATHER THAN GLUTAMINE, WHEREAS COMPONENT II PROVIDES
GLUTAMINE AMIDOTRANSFERASE ACTIVITY.
SIMILARITY: BELONGS TO THE ANTHRANILATE SYNTHASE COMPONENT I
FAMILY.
|
| | trpD | b1263 | anthranilate synthase component II, glutamine amidotransferase and phosphoribosylanthranilate transferase |
EG11027 |
CATALYTIC ACTIVITY: CHORISMATE + L-GLUTAMINE = ANTHRANILATE +
PYRUVATE + L-GLUTAMATE.
CATALYTIC ACTIVITY: ANTHRANILATE + PHOSPHORIBOSYLPYROPHOSPHATE =
N-5'-PHOSPHORIBOSYL-ANTHRANILATE + PYROPHOSPHATE.
PATHWAY: FIRST AND SECOND STEPS IN BIOSYNTHESIS OF TRYPTOPHAN.
SUBUNIT: TETRAMER OF TWO COMPONENTS I AND TWO COMPONENTS II.
MISCELLANEOUS: COMPONENT I CATALYZES THE FORMATION OF ANTHRANILATE
USING AMMONIA RATHER THAN GLUTAMINE, WHEREAS COMPONENT II PROVIDES
GLUTAMINE AMIDOTRANSFERASE ACTIVITY.
SIMILARITY: TO OTHER TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAINS.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE ANTHRANILATE
PHOSPHORIBOSYLTRANSFERASE FAMILY.
|
| | trpC | b1262 | N-(5-phosphoribosyl)anthranilate isomerase and indole-3-glycerolphosphate synthetase |
EG11026 |
FUNCTION: BIFUNCTIONAL ENZYME THAT CATALYZES TWO SEQUENTIAL STEPS
OF TRYPTOPHAN BIOSYNTHETIC PATHWAY. THE FIRST REACTION IS
CATALYZED BY THE ISOMERASE, CODED BY THE TRPF DOMAIN; THE SECOND
REACTION IS CATALYZED BY THE SYNTHASE, CODED BY THE TRPC DOMAIN.
CATALYTIC ACTIVITY: N-5'-PHOSPHORIBOSYL-ANTHRANILATE =
1-(2-CARBOXYPHENYLAMINO)-1-DEOXY-D-RIBULOSE 5-PHOSPHATE.
CATALYTIC ACTIVITY: 1-(2-CARBOXYPHENYLAMINO)-1-DEOXY-D-RIBULOSE
5-PHOSPHATE = 1-(INDOL-3-YL)GLYCEROL 3-PHOSPHATE + CO(2) + H(2)O.
PATHWAY: THIRD AND FOURTH STEPS IN BIOSYNTHESIS OF TRYPTOPHAN.
SUBUNIT: MONOMER.
SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE TRPC FAMILY.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE TRPF FAMILY.
|
| | trpB | b1261 | tryptophan synthase, beta protein |
EG11025 |
FUNCTION: THE BETA SUBUNIT IS RESPONSIBLE FOR THE SYNTHESIS
OF L-TRYPTOPHAN FROM INDOLE AND L-SERINE.
CATALYTIC ACTIVITY: L-SERINE + 1-(INDOL-3-YL)GLYCEROL 3-PHOSPHATE
= L-TRYPTOPHAN + GLYCERALDEHYDE 3-PHOSPHATE + H(2)O.
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: LAST (FIFTH) STEP IN BIOSYNTHESIS OF TRYPTOPHAN.
SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS.
SIMILARITY: BELONGS TO THE TRPB FAMILY.
|
| | trpA | b1260 | tryptophan synthase, alpha protein |
EG11024 |
FUNCTION: THE ALPHA SUBUNIT IS RESPONSIBLE FOR THE ALDOL CLEAVAGE
OF INDOLEGLYCEROL PHOSPHATE TO INDOLE AND GLYCERALDEHYDE 3-
PHOSPHATE.
CATALYTIC ACTIVITY: L-SERINE + 1-(INDOL-3-YL)GLYCEROL 3-PHOSPHATE
= L-TRYPTOPHAN + GLYCERALDEHYDE 3-PHOSPHATE + H(2)O.
PATHWAY: LAST (FIFTH) STEP IN BIOSYNTHESIS OF TRYPTOPHAN.
SUBUNIT: TETRAMER OF TWO ALPHA AND TWO BETA CHAINS.
SIMILARITY: BELONGS TO THE TRPA FAMILY.
|
| 3.130820 | - | 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.
|
| 3.005756 | - | 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.
|
| 2.950910 | + | hisG | b2019 | ATP phosphoribosyltransferase |
EG10449 |
CATALYTIC ACTIVITY: 1-(5-PHOSPHO-D-RIBOSYL)-ATP + PYROPHOSPHATE =
ATP + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE.
PATHWAY: FIRST STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. IS VERY
IMPORTANT IN THE REGULATION OF HISTIDINE METABOLISM.
SUBUNIT: HOMOHEXAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ATP PHOSPHORIBOSYLTRANSFERASE FAMILY.
|
| | hisD | b2020 | L-histidinal:NAD+ oxidoreductase; L-histidinol:NAD+ oxidoreductase |
EG10447 |
FUNCTION: THIS PROTEIN IS CONSIDERED AS A BIFUNCTIONAL ENZYME,
POSSESSING TWO ACTIVE SITES, ONE AN ALCOHOL DEHYDROGENASE AND
THE OTHER AN ALDEHYDE DEHYDROGENASE.
CATALYTIC ACTIVITY: L-HISTIDINOL + 2 NAD(+) = L-HISTIDINE +
2 NADH.
PATHWAY: TENTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: HOMODIMER.
SIMILARITY: TO OTHER PROKARYOTIC, FUNGAL AND PLANTS HDH.
|
| | hisC | b2021 | histidinol-phosphate aminotransferase |
EG10446 |
CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE =
3-(IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + GLUTAMATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: EIGHTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| | hisB | b2022 | imidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase |
EG10445 |
CATALYTIC ACTIVITY: D-ERYTHRO-1-(IMIDAZOL-4-YL)GLYCEROL
3-PHOSPHATE = 3-(IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + H(2)O.
CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + H(2)O = L-HISTIDINOL
+ ORTHOPHOSPHATE.
PATHWAY: SEVENTH & NINTH STEPS IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE
IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE FAMILY.
|
| | hisH | b2023 | glutamine amidotransferase subunit of heterodimer with HisF = imidazole glycerol phosphate synthase holoenzyme |
EG10450 |
FUNCTION: CATALYZES AN AMIDOTRANSFERASE REACTION THAT GENERATES
IMIDAZOLE-GLYCEROL PHOSPHATE AND 5-AMINOIMIDAZOL-4-CARBOXAMIDE
RIBONUCLEOTIDE, WHICH IS USED FOR PURINE SYNTHESIS.
PATHWAY: FIFTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HISH FAMILY.
SIMILARITY: CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN.
|
| | hisA | b2024 | N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'- phosphoribosyl)-4-imidazolecarboxamide isomerase |
EG10444 |
CATALYTIC ACTIVITY: N-(5'-PHOSPHO-D-RIBOSYLFORMIMINO)-5-AMINO-1-
(5''-PHOSPHORIBOSYL)-4-IMIDAZOLECARBOXAMIDE = N-(5'-PHOSPHO-D-1'-
RIBULOSYLFORMIMINO)-5-AMINO-1-(5''-PHOSPHORIBOSYL)-4-
IMIDAZOLECARBOXAMIDE.
PATHWAY: FOURTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HISA / HISF FAMILY.
|
| | hisF | b2025 | imidazole glycerol phosphate synthase subunit in heterodimer with HisH = imidazole glycerol phsphate synthase holoenzyme |
EG10448 |
FUNCTION: CATALYZES THE CYCLIZATION REACTION THAT PRODUCES
D-ERYTHRO-IMIDAZOLE GLYCEROL PHOSPHATE.
PATHWAY: SIXTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HISA / HISF FAMILY.
|
| | hisI | b2026 | phosphoribosyl-amp cyclohydrolase; phosphoribosyl-ATP pyrophosphatase |
EG10451 |
CATALYTIC ACTIVITY: 5-PHOSPHORIBOSYL-ATP + H(2)O =
5-PHOSPHORIBOSYL-AMP + PYROPHOSPHATE.
CATALYTIC ACTIVITY: 5-PHOSPHORIBOSYL-AMP + H(2)O =
5-(5-PHOSPHO-D-RIBOSYLAMINOFORMIMINO)-1-(5-PHOSPHO-RIBOSYL)
IMIDAZOLE-4-CARBOXAMIDE.
PATHWAY: SECOND AND THIRD STEPS IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBCELLULAR LOCATION: CYTOPLASMIC.
|
| 2.731044 | - | 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.
|
| 2.445815 | - | pyrE | b3642 | orotate phosphoribosyltransferase |
EG10808 |
CATALYTIC ACTIVITY: OROTIDINE-5'-PHOSPHATE + PYROPHOSPHATE =
OROTATE + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE.
PATHWAY: FIFTH STEP IN PYRIMIDINE BIOSYNTHESIS.
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO THE PURINE/PYRIMIDINE
PHOSPHORIBOSYLTRANSFERASE FAMILY.
|
| 2.429069 | - | rna | b0611 | RNase I, cleaves phosphodiester bond between any two nucleotides |
EG10856 |
FUNCTION: ONE OF THE FEW RNASES THAT CLEAVES THE PHOSPHODIESTER
BOND BETWEEN ANY TWO NUCLEOTIDE. SHOWS A PREFERENCE FOR
CYTIDYLIC OR GUANYLIC ACID.
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE TO 3'-
PHOSPHOMONONUCLEOTIDES AND 3'-PHOSPHOOLIGONUCLEOTIDES WITH
2',3'-CYCLIC PHOSPHATE INTERMEDIATES.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: PERIPLASMIC AND CYTOPLASMIC. RNASE I
(PERIPLASMIC) AND RNASE I* (CYTOPLASMIC) APPEAR TO BE ISOFORMS
APPARENTLY ENCODED BY THE SAME GENE. THE CYTOPLASMIC FORM IS LESS
ACTIVE TOWARDS NATURAL POLYMER RNA.
PTM: FOUR DISULFIDE BONDS ARE PRESENT (BY SIMILARITY).
SIMILARITY: BELONGS TO THE RNASE T2 FAMILY.
|
| 2.341552 | + | 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.
|
| 2.140983 | + | aslB | b3800 | putative arylsulfatase regulator |
EG10090 |
FUNCTION: POTENTIAL POSITIVE FACTOR FOR THE REGULATION OF
ARYLSULFATASE.
SIMILARITY: BELONGS TO THE ASLB/ATSB FAMILY.
|
| 2.132134 | - | 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.
|
| 2.104422 | + | tdcR | b3119 | threonine dehydratase operon activator protein |
EG10992 |
FUNCTION: PROBABLE TRANS-ACTING POSITIVE ACTIVATOR FOR THE TDC
OPERON.
|
| 2.045973 | + | degQ | b3234 | serine endoprotease |
EG12612 |
FUNCTION: PROTEASE WITH A SHARED SPECIFICITY WITH DEGP/DEGP.
SUBCELLULAR LOCATION: PERIPLASMIC.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S2C; ALSO KNOWN AS THE
DEGP/DEGQ/DEGS FAMILY.
SIMILARITY: CONTAINS 2 PDZ/DHR DOMAINS.
|
| | degS | b3235 | protease |
EG11652 |
SUBCELLULAR LOCATION: PERIPLASMIC (POTENTIAL).
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S2C; ALSO KNOWN AS THE
DEGP/DEGQ/DEGS FAMILY.
SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN.
|
| 1.969445 | + | thdF | b3706 | GTP-binding protein in thiophene and furan oxidation |
EG10997 |
FUNCTION: EXHIBITS A VERY HIGH INTRINSIC GTPASE HYDROLYSIS RATE.
INVOLVED IN THE BIOSYNTHESIS OF THE HYPERMODIFIED NUCLEOSIDE 5-
METHYLAMINOMETHYL-2-THIOURIDINE, WHICH IS FOUND IN THE WOBBLE
POSITION OF SOME TRNAS.
SUBUNIT: ABLE TO FORM SELF-ASSEMBLIES.
SUBCELLULAR LOCATION: CYTOPLASMIC; MAY ALSO BE ASSOCIATED WITH THE
INNER MEMBRANE.
SIMILARITY: BELONGS TO THE ERA/TRME FAMILY OF GTP-BINDING
PROTEINS. TRME SUBFAMILY.
CAUTION: REF.2 SEQUENCE WAS INCORRECT.
|
| 1.944946 | - | rem | b1561 | orf, hypothetical protein |
EG11129 |
|
| 1.804455 | - | yfbS | b2292 | putative transport protein |
EG14103 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(PROBABLE).
SIMILARITY: BELONGS TO THE NADC/P/PHO87 FAMILY OF TRANSPORTERS.
NADC SUBFAMILY.
|
| 1.770683 | + | yiiP | b3915 | putative transport system permease protein |
EG11873 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE UPF0018 FAMILY.
|
| 1.749027 | + | b1458 | b1458 | orf, hypothetical protein |
|
|
| | b1459 | b1459 | orf, hypothetical protein |
|
|
| 1.652681 | + | yjeI | b4144 | orf, hypothetical protein |
EG12471 |
|
| 1.648580 | - | glnD | b0167 | protein PII; uridylyltransferase acts on regulator of glnA |
EG11411 |
FUNCTION: MODIFIES, BY URIDYLYLATION OR DEURIDYLYLATION THE PII
(GLNB) REGULATORY PROTEIN.
CATALYTIC ACTIVITY: UTP + [PROTEIN-PII] = PYROPHOSPHATE +
URIDYLYL-[PROTEIN-PII].
SIMILARITY: BELONGS TO THE GLND FAMILY.
CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN FROM POSITION 703
ONWARD AND IS SHORTER (727 AA) DUE TO A FRAMESHIFT.
|
| | dapD | b0166 | 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase |
EG10207 |
CATALYTIC ACTIVITY: SUCCINYL-COA + 2,3,4,5-TETRAHYDROPYRIDINE-
2-CARBOXYLATE = COA + N-SUCCINYL-L-2-AMINO-6-OXOHEPTANEDIOATE.
PATHWAY: FOURTH STEP IN THE BIOSYNTHESIS OF DIAMINOPIMELATE AND
LYSINE FROM ASPARTATE SEMIALDEHYDE.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE CYSE/LACA/LPXA/NODL FAMILY OF
ACETYLTRANSFERASES. COMPOSED OF MULTIPLE REPEATS OF [LIV]-G-X(4).
|
| | b0165 | b0165 | orf, hypothetical protein |
|
|
| | yaeI | b0164 | orf, hypothetical protein |
EG12337 |
SIMILARITY: BELONGS TO THE UPF0151 FAMILY. SOME SIMILARITY TO
PHOSPHATASES.
|
| 1.589780 | + | yaeS | b0174 | orf, hypothetical protein |
EG13329 |
FUNCTION: GENERATES UNDECAPRENYL PYROPHOSPHATE (UPP) FROM
ISOPENTENYL PYROPHOSPHATE (IPP). UPP IS THE PRECURSOR OF THE
CARRIER LIPID FOR PEPTIDOGLYCAN SYNTHESIS.
CATALYTIC ACTIVITY: DI-TRANS-POLY-CIS-DECAPRENYL DIPHOSPHATE +
ISOPENTENYL DIPHOSPHATE = DIPHOSPHATE + DI-TRANS-POLY-CIS-
UNDECAPRENYL DIPHOSPHATE.
SIMILARITY: BELONGS TO THE UPP SYNTHETASE FAMILY.
|
| | cdsA | b0175 | CDP-diglyceride synthetase |
EG10139 |
CATALYTIC ACTIVITY: CTP + PHOSPHATIDATE = PYROPHOSPHATE +
CDP-DIACYLGLYCEROL.
PATHWAY: PHOSPHOLIPID BIOSYNTHESIS.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE CDS FAMILY.
|
| | yaeL | b0176 | orf, hypothetical protein |
EG12436 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE YAEL/HI0918/HP0258/SLR1821 FAMILY.
SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN.
|
| | yaeT | b0177 | orf, hypothetical protein |
EG12676 |
SUBCELLULAR LOCATION: OUTER MEMBRANE (POTENTIAL).
SIMILARITY: BELONGS TO THE SURFACE ANTIGEN D15 FAMILY.
|
| | hlpA | b0178 | histone-like protein, located in outer membrane or nucleoid |
EG10455 |
SUBUNIT: HOMOTETRAMER.
SUBCELLULAR LOCATION: EITHER IN THE NUCLEOID (CHROMATIN) OR IN
THE OUTER MEMBRANE.
SIMILARITY: TO OTHER SPECIES OMPH OUTER MEMBRANE PROTEIN.
|
| | lpxD | b0179 | UDP-3-O-(3-hydroxymyristoyl)-glucosamine N-acyltransferase; third step of endotoxin (lipidA) synthesis |
EG10316 |
CATALYTIC ACTIVITY: UDP-3-O-(3-HYDROXYTETRADECANOYL)GLUCOSAMINE
+ (R)-3-HYDROXYTETRADECANOYL-[ACYL-CARRIER PROTEIN] =
UDP-2,3-BIS(3-HYDROXYTETRADECANOYL)GLUCOSAMINE + [ACYL-CARRIER
PROTEIN].
PATHWAY: THIRD STEP IN LIPID A BIOSYNTHESIS.
MISCELLANEOUS: THE MUTANTS FIRA200, FIRA201 AND OMSA CONFER
TEMPERATURE SENSITIVITY. FIRA200 REVERSES THE RIFAMPIN RESISTANCE
OF RPOB MUTANTS.
SIMILARITY: BELONGS TO THE CYSE/LACA/LPXA/NODL FAMILY OF
ACETYLTRANSFERASES. COMPOSED OF MULTIPLE REPEATS OF [LIV]-G-X(4).
CAUTION: WAS ORIGINALLY THOUGHT TO BE INVOLVED IN TRANSCRIPTION.
|
| | fabZ | b0180 | (3R)-hydroxymyristol acyl carrier protein dehydratase |
EG11284 |
FUNCTION: INVOLVED IN SATURATED FATTY ACIDS BIOSYNTHESIS.
SUBUNIT: OLIGOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
PTM: THE N-TERMINUS IS BLOCKED.
SIMILARITY: BELONGS TO THE THIOESTER DEHYDRATASE FAMILY.
|
| | lpxA | b0181 | UDP-N-acetylglucosamine acetyltransferase; lipid A biosynthesis |
EG10545 |
FUNCTION: INVOLVED IN THE BIOSYNTHESIS OF LIPID A, A
PHOSPHORYLATED GLYCOLIPID THAT ANCHORS THE LIPOPOLYSACCHARIDE TO
THE OUTER MEMBRANE OF THE CELL.
CATALYTIC ACTIVITY: (R)-3-HYDROXYTETRADECANOYL-[ACYL-CARRIER
PROTEIN] + UDP-N-ACETYLGLUCOSAMINE = [ACYL-CARRIER PROTEIN] +
UDP-3-O-(3-HYDROXYTETRADECANOYL)-N-ACETYLGLUCOSAMINE.
PATHWAY: LIPID A BIOSYNTHESIS; FIRST STEP.
SUBUNIT: HOMOTRIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE TRANSFERASE HEXAPEPTIDE REPEAT FAMILY.
LPXA SUBFAMILY.
|
| | lpxB | b0182 | tetraacyldisaccharide-1-P; lipid A biosynthesis, penultimate step |
EG10546 |
FUNCTION: CONDENSATION OF UDP-2,3-DIACYLGLUCOSAMINE AND
2,3-DIACYLGLUCOSAMINE-1-PHOSPHATE TO FORM LIPID A DISACCHARIDE,
A PRECURSOR OF LIPID A, A PHOSPHORYLATED GLYCOLIPID THAT ANCHORS
THE LIPOPOLYSACCHARIDE TO THE OUTER MEMBRANE OF THE CELL.
CATALYTIC ACTIVITY: UDP-2,3-BIS(3-HYDROXYTETRADECANOYL)GLUCOSAMINE
+ 2,3-BIS(3-HYDROXYTETRADECANOYL)-BETA-D-GLUCOSAMINYL 1-PHOSPHATE
= UDP + 2,3-BIS(3-HYDROXYTETRADECANOYL)-D-GLUCOSAMINYL-1,6-BETA-
D-2,3-BIS(3-HYDROXYTETRADECANOYL)-BETA-D-GLUCOSAMINYL 1-PHOSPHATE.
PATHWAY: LIPID A BIOSYNTHESIS.
SIMILARITY: BELONGS TO THE LPXB FAMILY.
|
| | rnhB | b0183 | RNAse HII, degrades RNA of DNA-RNA hybrids |
EG10861 |
FUNCTION: DEGRADES THE RIBONUCLEOTIDE MOIETY ON RNA-DNA HYBRID
MOLECULES.
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE TO 5'-PHOSPHO-
MONOESTER.
COFACTOR: REQUIRES MANGANESE FOR ACTIVITY.
SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL).
SIMILARITY: BELONGS TO THE RNASE HII FAMILY.
|
| | dnaE | b0184 | DNA polymerase III, alpha subunit |
EG10238 |
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 ALPHA CHAIN IS THE DNA POLYMERASE.
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].
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO DNA POLYMERASE TYPE-C FAMILY. DNAE
SUBFAMILY.
|
| | accA | b0185 | acetylCoA carboxylase, carboxytransferase component, alpha subunit |
EG11647 |
FUNCTION: THIS PROTEIN IS A COMPONENT OF THE ACETYL COENZYME A
CARBOXYLASE COMPLEX; FIRST, BIOTIN CARBOXYLASE CATALYZES THE
CARBOXYLATION OF THE CARRIER PROTEIN AND THEN THE TRANSCARBOXYLASE
TRANSFERS THE CARBOXYL GROUP TO FORM MALONYL-COA.
CATALYTIC ACTIVITY: CARBOXYBIOTIN CARBOXYL CARRIER PROTEIN +
ACETYL-COA = BIOTIN CARBOXYL CARRIER PROTEIN + MALONYL-COA.
PATHWAY: FIRST STEP IN LONG-CHAIN FATTY ACID SYNTHESIS.
SUBUNIT: ACETYL-COA CARBOXYLASE IS AN HETEROHEXAMER OF BIOTIN
CARBOXYL CARRIER PROTEIN, BIOTIN CARBOXYLASE AND THE TWO SUBUNITS
OF CARBOXYL TRANSFERASE IN A 2:2 COMPLEX.
SIMILARITY: TO THE C-TERMINUS OF MAMMALIAN PROPIONYL-COA
CARBOXYLASE BETA CHAIN.
|
| | ldcC | b0186 | lysine decarboxylase 2, constitutive |
EG13219 |
FUNCTION: LDC IS CONSTITUTIVELY BUT WEAKLY EXPRESSED UNDER VARIOUS
CONDITIONS. OPTIMUM ACTIVITY IS ACHIEVED BETWEEN PH 6.2 TO 8.0.
CATALYTIC ACTIVITY: L-LYSINE = CADAVERINE + CO(2).
COFACTOR: PYRIDOXAL PHOSPHATE.
SUBUNIT: HOMODECAMER.
SIMILARITY: BELONGS TO FAMILY 1 OF ORNITHINE, LYSINE, AND ARGININE
DECARBOXYLASES.
|
| | yaeR | b0187 | orf, hypothetical protein |
EG13224 |
SIMILARITY: STRONG, TO B.SUBTILIS YWKD.
|
| | mesJ | b0188 | cell cycle protein |
EG13220 |
SIMILARITY: BELONGS TO THE UPF0072 (MESJ/YCF62) FAMILY.
|
| 1.588448 | - | 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.
|
| 1.573531 | + | 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.
|
| 1.525787 | + | aceB | b4014 | malate synthase A |
EG10023 |
CATALYTIC ACTIVITY: L-MALATE + COA = ACETYL-COA + H(2)O +
GLYOXYLATE.
PATHWAY: SECOND STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE
TRICARBOXYLIC ACID CYCLE (IN BACTERIA, FUNGI AND PLANTS).
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE MALATE SYNTHASE FAMILY.
|
| | aceA | b4015 | isocitrate lyase |
EG10022 |
CATALYTIC ACTIVITY: ISOCITRATE = SUCCINATE + GLYOXYLATE.
COFACTOR: REQUIRES DIVALENT CATIONS.
ENZYME REGULATION: IS ACTIVATED BY PHOSPHORYLATION (ON HISTIDINE)
AND IS INHIBITED BY PEP, 3-PHOSPHOGLYCERATE AND SUCCINATE.
PATHWAY: FIRST STEP IN GLYOXYLATE BYPASS, AN ALTERNATIVE TO THE
TRICARBOXYLIC ACID CYCLE (IN BACTERIA, PLANTS, AND FUNGI).
SUBUNIT: HOMOTETRAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ISOCITRATE LYASE FAMILY.
|
| 1.505154 | + | clpP | b0437 | ATP-dependent proteolytic subunit of clpA-clpP serine protease, heat shock protein F21.5 |
EG10158 |
FUNCTION: CLEAVES PEPTIDES IN VARIOUS PROTEINS IN A PROCESS THAT
REQUIRES ATP HYDROLYSIS. HAS A CHYMOTRYPSIN-LIKE ACTIVITY. MAY BE
RESPONSIBLE FOR A FAIRLY GENERAL AND CENTRAL HOUSEKEEPING FUNCTION
RATHER THAN FOR THE DEGRADATION OF SPECIFIC SUBSTRATES. CLPP MAY
PLAY THE ROLE OF A MASTER PROTEASE WHICH IS ATTRACTED TO DIFFERENT
SUBSTRATES BY DIFFERENT SPECIFICITY FACTORS SUCH AS CLPA OR CLPX.
CATALYTIC ACTIVITY: HYDROLYSIS OF PROTEINS TO SMALL PEPTIDES IN
THE PRESENCE OF ATP AND MAGNESIUM. ALPHA-CASEIN IS THE USUAL TEST
SUBSTRATE. IN THE ABSENCE OF ATP, ONLY OLIGOPEPTIDES SHORTER THAN
FIVE RESIDUES ARE CLEAVED (SUCH AS SUCCINYL-LEU-TYR-|-NHMEC; AND
LEU-TYR-LEU-|-TYR-TRP, IN WHICH THE CLEAVAGE OF THE -TYR-|-LEU-
AND -TYR-|-TRP- BOND ALSO OCCURS).
SUBUNIT: TWELVE CLPP SUBUNITS ASSEMBLE INTO A DISK-LIKE STRUCTURE
WITH A CENTRAL CAVITY, RESEMBLING THE STRUCTURE OF EUKARYOTIC
PROTEASOMES. IN THE PRESENCE OF ATP, CLPA OR CLPX SUBUNITS
INTERACT WITH THE CLPP STRUCTURE TO FORM A 750 KDA COMPLEX THAT
EXHIBITS ATP-DEPENDENT PROTEOLYTIC ACTIVITY.
INDUCTION: BY HEAT SHOCK.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S14; ALSO KNOWN AS CLPP
FAMILY.
|
| | clpX | b0438 | ATP-dependent specificity component of clpP serine protease, chaperone |
EG10159 |
FUNCTION: ATP-DEPENDENT SPECIFICITY COMPONENT OF THE CLP PROTEASE.
IT DIRECTS THE PROTEASE TO SPECIFIC SUBSTRATES. IT MAY BIND TO THE
LAMBDA O SUBSTRATE PROTEIN AND PRESENT IT TO THE CLPP PROTEASE IN
A FORM THAT CAN BE RECOGNIZED AND READILY HYDROLYZED BY CLPP. CAN
PERFORM CHAPERONE FUNCTIONS IN THE ABSENCE OF CLPP.
SUBUNIT: HETERODIMER OF CLPP AND CLPX.
INDUCTION: BY HEAT SHOCK.
SIMILARITY: BELONGS TO THE CLPX CHAPERONE FAMILY.
|
| 1.502258 | - | bglG | b3723 | positive regulation of bgl operon |
EG10116 |
FUNCTION: MEDIATES THE POSITIVE REGULATION OF THE BETA-GLUCOSIDE
(BGL) OPERON BY FUNCTIONING AS A TRANSCRIPTIONAL ANTITERMINATOR.
THIS IS A RNA-BINDING PROTEIN THAT RECOGNIZES A SPECIFIC SEQUENCE
LOCATED JUST UPSTREAM OF TWO TERMINATION SITES WITHIN THE OPERON.
PTM: PHOSPHORYLATED AND INACTIVATED BY BGLF (II-BGL). THE DEGREE
OF PHOSPHORYLATION IS DEPENDENT ON THE PRESENCE OR ABSENCE OF
BETA-GLUCOSIDES WHICH ACT AS INDUCERS OF THE OPERON EXPRESSION.
ADDITION OF INDUCER RESULT IN THE RAPID DEPHOSPHORYLATION OF BGLG.
SIMILARITY: BELONGS TO THE TRANSCRIPTIONAL ANTITERMINATOR BGLG
FAMILY.
|
| | bglF | b3722 | PTS system beta-glucosides, enzyme II, cryptic |
EG10115 |
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.
FUNCTION: ACTS AS BOTH A KINASE AND A PHOSPHATASE ON BGLG.
CATALYTIC ACTIVITY: PROTEIN N-PHOSPHOHISTIDINE + SUGAR =
PROTEIN HISTIDINE + SUGAR PHOSPHATE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: CONTAINS A PTS EIIA DOMAIN.
SIMILARITY: CONTAINS A PTS EIIB DOMAIN.
SIMILARITY: CONTAINS A PTS EIIC DOMAIN.
|
| | bglB | b3721 | phospho-beta-glucosidase B; cryptic |
EG10114 |
FUNCTION: CAN HYDROLYZE SALICIN AND ARBUTIN.
CATALYTIC ACTIVITY: 6-PHOSPHO-BETA-D-GLUCOSIDE-(1,4)-D-GLUCOSE +
H(2)O = D-GLUCOSE 6-PHOSPHATE + GLUCOSE.
SIMILARITY: BELONGS TO FAMILY 1 OF GLYCOSYL HYDROLASES.
|
| | yieC | b3720 | putative receptor protein |
EG11364 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. OUTER MEMBRANE
(POTENTIAL).
SIMILARITY: BELONGS TO THE LAMB FAMILY OF PORINS. STRONG, TO
E.CHRYSANTHEMI YIEC.
|
| | yieL | b3719 | putative xylanase |
EG11729 |
|
| | yieK | b3718 | putative isomerase |
EG11728 |
SIMILARITY: BELONGS TO THE GLUCOSAMINE/GALACTOSAMINE-6-PHOSPHATE
ISOMERASE FAMILY.
|