ID   CHEZ_ECOL6              Reviewed;         214 AA.
AC   P0A9I0; P07366;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, 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=c2296;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN80755.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN80755.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000983609.1; NC_004431.1.
DR   AlphaFoldDB; P0A9I0; -.
DR   SMR; P0A9I0; -.
DR   STRING; 199310.c2296; -.
DR   EnsemblBacteria; AAN80755; AAN80755; c2296.
DR   GeneID; 66674228; -.
DR   KEGG; ecc:c2296; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_1_0_6; -.
DR   OMA; EGPQIHA; -.
DR   Proteomes; UP000001410; 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.
FT   CHAIN           1..214
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000089640"
FT   REGION          174..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            147
FT                   /note="Enhances dephosphorylation of CheY-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  23976 MW;  42308F5AC0685D27 CRC64;
     MMQPSIKPAD EHSAGDIIAR IGSLTRMLRD SLRELGLDQA IAEAAEAIPD ARDRLYYVVQ
     MTAQAAERAL NSVEASQPHQ DQMEKSAKAL TQRWDDWFAD PIDLADAREL VTDTRQFLAD
     VPAHTSFTNA QLLEIMMAQD FQDLTGQVIK RMMDVIQEIE RQLLMVLLEN IPEQESRPKR
     ENQSLLNGPQ VDTSKAGVVA SQDQVDDLLD SLGF