ID   CHEZ_PSEPK              Reviewed;         262 AA.
AC   Q88EW3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=PP_4339;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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}.
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DR   EMBL; AE015451; AAN69918.1; -; Genomic_DNA.
DR   RefSeq; NP_746454.1; NC_002947.4.
DR   RefSeq; WP_010955069.1; NC_002947.4.
DR   AlphaFoldDB; Q88EW3; -.
DR   SMR; Q88EW3; -.
DR   STRING; 160488.PP_4339; -.
DR   EnsemblBacteria; AAN69918; AAN69918; PP_4339.
DR   KEGG; ppu:PP_4339; -.
DR   PATRIC; fig|160488.4.peg.4613; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_0_0_6; -.
DR   OMA; EGPQIHA; -.
DR   PhylomeDB; Q88EW3; -.
DR   BioCyc; PPUT160488:G1G01-4617-MON; -.
DR   Proteomes; UP000000556; 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..262
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000410781"
FT   REGION          218..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            181
FT                   /note="Enhances dephosphorylation of CheY-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  29533 MW;  00F686B072600370 CRC64;
     MDSSQTSLGE FESTLKKHAQ ELVESLERGR FGEAVQLIHE LNQTRDRGLY QEVGKLTREL
     HSAIVSFQID PTMPQAEEVS QITDATERLS YVVKLTEGAA NRTMDLVEES TPVLNELANE
     AKALSTDWQR FMRREVAAPE FRDLVKRVDS FLTHSAEGNR KVSGHLNDIL LAQDYQDLTG
     QVIKRVTTLV TEVESNLLKL VLMASQVDRF AGIKHDHDQL RAEKDREKHP TRGEGPQIHA
     DKREDVVSGQ DDVDDLLSSL GF