ID   CHEZ_ECOBD              Reviewed;         214 AA.
AC   C6EBU6; C5W5C5;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=ECBD_1757, ECD_01852, B21_01841;
OS   Escherichia coli (strain B / BL21-DE3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=469008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.;
RT   "Sequencing and gene expression analysis of Escherichia coli BL21.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT   "Complete sequence of Escherichia coli BL21(DE3).";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RX   PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA   Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H., Couloux A.,
RA   Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S., Segurens B.,
RA   Kim S.C., Oh T.K., Lenski R.E., Studier F.W., Daegelen P., Kim J.F.;
RT   "Genome sequences of Escherichia coli B strains REL606 and BL21(DE3).";
RL   J. Mol. Biol. 394:644-652(2009).
RN   [4]
RP   INDUCTION BY STRESS.
RC   STRAIN=B / BL21-DE3;
RX   PubMed=18363324; DOI=10.1021/pr700631c;
RA   Han K.Y., Park J.S., Seo H.S., Ahn K.Y., Lee J.;
RT   "Multiple stressor-induced proteome responses of Escherichia coli
RT   BL21(DE3).";
RL   J. Proteome Res. 7:1891-1903(2008).
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   -!- INDUCTION: Induced by heat shock and guanidine hydrochloride-derived
CC       protein denaturation stress. {ECO:0000269|PubMed:18363324}.
CC   -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR   EMBL; AM946981; CAQ32358.1; -; Genomic_DNA.
DR   EMBL; CP001665; ACT28808.1; -; Genomic_DNA.
DR   EMBL; CP001509; ACT43706.1; -; Genomic_DNA.
DR   RefSeq; WP_000983609.1; NZ_CP053602.1.
DR   AlphaFoldDB; C6EBU6; -.
DR   SMR; C6EBU6; -.
DR   STRING; 469008.B21_01841; -.
DR   GeneID; 66674228; -.
DR   KEGG; ebd:ECBD_1757; -.
DR   KEGG; ebe:B21_01841; -.
DR   KEGG; ebl:ECD_01852; -.
DR   PATRIC; fig|469008.15.peg.1880; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_1_0_6; -.
DR   OMA; EGPQIHA; -.
DR   Proteomes; UP000002032; 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   2: Evidence at transcript level;
KW   Chemotaxis; Cytoplasm; Flagellar rotation; Hydrolase; Protein phosphatase;
KW   Stress response.
FT   CHAIN           1..214
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000410775"
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