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PTQA_ECO57
ID   PTQA_ECO57              Reviewed;         116 AA.
AC   P69793; P17335; Q47092; Q47093; Q47094; Q57128;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=PTS system N,N'-diacetylchitobiose-specific EIIA component {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=EIIA-Chb {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=EIII-Chb {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=IIIcel {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69791};
GN   Name=chbA; Synonyms=celC; OrderedLocusNames=Z2766, ECs2442;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II ChbABC PTS system is involved in the transport of the chitin
CC       disaccharide N,N'-diacetylchitobiose (GlcNAc2).
CC       {ECO:0000250|UniProtKB:P69791}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P69791};
CC       Note=Can also use copper and nickel with lower efficiency.
CC       {ECO:0000250|UniProtKB:P69791};
CC   -!- SUBUNIT: Forms a complex with ChbB (EIIB). ChbA is a homotrimer.
CC       {ECO:0000250|UniProtKB:P69791}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By GlcNAc2, GlcNAc3 and beta-N,N'-diacetylchitobiose (Me-
CC       TCB). {ECO:0000250|UniProtKB:P69791}.
CC   -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR   EMBL; AE005174; AAG56722.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35865.1; -; Genomic_DNA.
DR   PIR; B90934; B90934.
DR   PIR; F85782; F85782.
DR   RefSeq; NP_310469.1; NC_002695.1.
DR   RefSeq; WP_000968919.1; NZ_SWKA01000004.1.
DR   AlphaFoldDB; P69793; -.
DR   BMRB; P69793; -.
DR   SMR; P69793; -.
DR   STRING; 155864.EDL933_2695; -.
DR   EnsemblBacteria; AAG56722; AAG56722; Z2766.
DR   EnsemblBacteria; BAB35865; BAB35865; ECs_2442.
DR   GeneID; 67415560; -.
DR   GeneID; 916949; -.
DR   KEGG; ece:Z2766; -.
DR   KEGG; ecs:ECs_2442; -.
DR   PATRIC; fig|386585.9.peg.2556; -.
DR   eggNOG; COG1447; Bacteria.
DR   HOGENOM; CLU_152490_3_0_6; -.
DR   OMA; MEQSRMA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00215; PTS_IIA_lac; 1.
DR   InterPro; IPR003188; PTS_IIA_lac/cel.
DR   InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR   PANTHER; PTHR34382; PTHR34382; 1.
DR   Pfam; PF02255; PTS_IIA; 1.
DR   PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR   SUPFAM; SSF46973; SSF46973; 1.
DR   TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..116
FT                   /note="PTS system N,N'-diacetylchitobiose-specific EIIA
FT                   component"
FT                   /id="PRO_0000186496"
FT   DOMAIN          15..113
FT                   /note="PTS EIIA type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT   ACT_SITE        89
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P69791"
FT   MOD_RES         89
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
SQ   SEQUENCE   116 AA;  12748 MW;  F2951DC6700FA8A9 CRC64;
     MMDLDNIPDT QTEAEELEEV VMGLIINSGQ ARSLAYAALK QAKQGDFAAA KAMMDQSRMA
     LNEAHLVQTK LIEGDAGEGK MKVSLVLVHA QDHLMTSMLA RELITELIEL HEKLKA
 
 
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