(data stored in ACNUC1104 zone)

SWISSPROT: Q7WAA2_BORPA

ID   Q7WAA2_BORPA            Unreviewed;       210 AA.
AC   Q7WAA2;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Protein phosphatase CheZ {ECO:0000256|PIRNR:PIRNR002884};
DE            EC=3.1.3.- {ECO:0000256|PIRNR:PIRNR002884};
DE   AltName: Full=Chemotaxis protein CheZ {ECO:0000256|PIRNR:PIRNR002884};
GN   Name=cheZ {ECO:0000313|EMBL:CAE36780.1};
GN   OrderedLocusNames=BPP1478 {ECO:0000313|EMBL:CAE36780.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Plays an important role in bacterial chemotaxis signal
CC       transduction pathway by accelerating the dephosphorylation of
CC       phosphorylated CheY (CheY-P). {ECO:0000256|PIRNR:PIRNR002884}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR002884}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR002884}.
CC   -!- SIMILARITY: Belongs to the CheZ family.
CC       {ECO:0000256|PIRNR:PIRNR002884}.
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DR   EMBL; BX640427; CAE36780.1; -; Genomic_DNA.
DR   RefSeq; WP_010928058.1; NC_002928.3.
DR   EnsemblBacteria; CAE36780; CAE36780; BPP1478.
DR   KEGG; bpa:BPP1478; -.
DR   HOGENOM; HOG000254724; -.
DR   KO; K03414; -.
DR   OMA; GPQIHAD; -.
DR   BioCyc; BPAR257311:G1GSY-1518-MONOMER; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0050920; P:regulation of chemotaxis; IEA:InterPro.
DR   InterPro; IPR007439; Chemotax_Pase_CheZ.
DR   Pfam; PF04344; CheZ; 1.
DR   PIRSF; PIRSF002884; CheZ; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WAA2.
DR   SWISS-2DPAGE; Q7WAA2.
KW   Chemotaxis {ECO:0000256|PIRNR:PIRNR002884};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR002884};
KW   Flagellar rotation {ECO:0000256|PIRNR:PIRNR002884};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR002884};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR002884}.
FT   SITE        145    145       Enhances dephosphorylation of CheY-P.
FT                                {ECO:0000256|PIRSR:PIRSR002884-1}.
SQ   SEQUENCE   210 AA;  23294 MW;  D9B02A44AB48166A CRC64;
     MNATDTGMQA DPTDLIQRIA SLTRMLRDSM RELGLDQAIK DAAEAIPDAR DRLRYLAQMT
     EQAANRVLNA IEAAGPIQDG MARGAQALDE RWQQWYDQPL ELPQARALVQ DTRAFLAAVP
     QHTQQTQAKL MEIVMAQDFQ DLTGQVIMRM MDVVGAIERE LLQVLLDNVP QERRDEANSL
     LNGPQVNPGG KADVVTSQDQ VDDLLASLGF
//

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