ID   CHEZ_BORPE              Reviewed;         210 AA.
AC   Q7VZ92;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=BP1034;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., 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., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   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:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR   EMBL; BX640414; CAE41334.1; -; Genomic_DNA.
DR   RefSeq; NP_879822.1; NC_002929.2.
DR   RefSeq; WP_003817162.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VZ92; -.
DR   SMR; Q7VZ92; -.
DR   STRING; 257313.BP1034; -.
DR   GeneID; 45388796; -.
DR   KEGG; bpe:BP1034; -.
DR   PATRIC; fig|257313.5.peg.1105; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_1_0_4; -.
DR   OMA; EGPQIHA; -.
DR   Proteomes; UP000002676; 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;
KW   Chemotaxis; Cytoplasm; Flagellar rotation; Hydrolase; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..210
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000410773"
FT   SITE            145
FT                   /note="Enhances dephosphorylation of CheY-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23268 MW;  CD1AB485B223856A CRC64;
     MNATDTGMQA DPTDLIQRIA SLTRMLRDSM RELGLDQAIK DAAEAIPDAR DRLRYVAQMT
     EQAANRVLNA TEAAGPIQDG MARGAQALDE RWQQWYDQPL ELPQARALVQ DTRAFLAAVP
     QHTQQTQAKL MEIVMAQDFQ DLTGQVIMRM MDVVGAIERE LLQVLLDNVP QERRDEANSL
     LNGPQVNPGG KADVVTSQDQ VDDLLASLGF