ID   CHEZ_PSEAB              Reviewed;         262 AA.
AC   Q02JU1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=PA14_45610;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ10638.1; -; Genomic_DNA.
DR   RefSeq; WP_003083075.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02JU1; -.
DR   SMR; Q02JU1; -.
DR   PRIDE; Q02JU1; -.
DR   EnsemblBacteria; ABJ10638; ABJ10638; PA14_45610.
DR   KEGG; pau:PA14_45610; -.
DR   HOGENOM; CLU_080718_0_0_6; -.
DR   OMA; EGPQIHA; -.
DR   BioCyc; PAER208963:G1G74-3826-MON; -.
DR   Proteomes; UP000000653; 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..262
FT                   /note="Protein phosphatase CheZ"
FT                   /id="PRO_0000410780"
FT   REGION          229..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            182
FT                   /note="Enhances dephosphorylation of CheY-P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  29622 MW;  A3605F5A4BD8B450 CRC64;
     MVLGNDSTGD EFESTLKKHA RELVDCLERG HFQQAVQLIQ ELSQARDRGL YQEVGKLTRE
     LHNAIVDFQI DPHSPHAQEM SQIADATDRL SYVVEMTEKA ANRTMDLVEQ SAPLVNQLGD
     DSRELHQEWQ RFMRREIDAD GFRELAKRIE QFLVRSGENA GQLSSQLNDI LLAQDYQDLT
     GQVIKRVTKL VTEVESNLVK LVWMAGQVDR YAGIEHDHVS MRHQAALERS AKGEGPQVAA
     EKREDVVSGQ DDVDDLLSSL GF