ID   CHEZ_VIBPA              Reviewed;         246 AA.
AC   Q9LB13;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=VP2230;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RX   PubMed=10648530; DOI=10.1128/jb.182.4.1035-1045.2000;
RA   Boles B.R., McCarter L.L.;
RT   "Insertional inactivation of genes encoding components of the sodium-type
RT   flagellar motor and switch of Vibrio parahaemolyticus.";
RL   J. Bacteriol. 182:1035-1045(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; AF069392; AAF32416.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC60493.1; -; Genomic_DNA.
DR   RefSeq; NP_798609.1; NC_004603.1.
DR   RefSeq; WP_005457755.1; NC_004603.1.
DR   AlphaFoldDB; Q9LB13; -.
DR   SMR; Q9LB13; -.
DR   STRING; 223926.28807223; -.
DR   EnsemblBacteria; BAC60493; BAC60493; BAC60493.
DR   GeneID; 1189743; -.
DR   KEGG; vpa:VP2230; -.
DR   PATRIC; fig|223926.6.peg.2133; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_0_0_6; -.
DR   OMA; EGPQIHA; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..246
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000410787"
FT   REGION          204..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            168
FT                   /note="Enhances dephosphorylation of CheY-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   246 AA;  27782 MW;  3E54BE3A2570F1C6 CRC64;
     MISLEQAKSL VQMLENGEQD QANMLVASLY EGTENPVLQE IGTLTRDLHD SLKQFNLDQR
     MTEIAKDEIP NARDRLHYVI EKTELAANKT MDAVDCCLPI ADNLHDCLQQ VRPQWNELMY
     GRIELSEFKA LCHRIDKLLV QVEGDSTELR GQLTEILMAQ DFQDLTGQII RRVITLVNEV
     EGRLVEILTV FSGQKPAEQV QVLSEPADKK IKQSSEAEGP ILHPELREDA VSSQDEVDDL
     LSSLGF