CHEZ_VIBC3
ID CHEZ_VIBC3 Reviewed; 239 AA.
AC A5F6J8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-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=VC0395_A1652, VC395_2179;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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 -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR EMBL; CP000627; ABQ20110.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10171.1; -; Genomic_DNA.
DR RefSeq; WP_000624259.1; NZ_JAACZH010000001.1.
DR AlphaFoldDB; A5F6J8; -.
DR SMR; A5F6J8; -.
DR STRING; 345073.VC395_2179; -.
DR EnsemblBacteria; ABQ20110; ABQ20110; VC0395_A1652.
DR GeneID; 57740689; -.
DR KEGG; vco:VC0395_A1652; -.
DR KEGG; vcr:VC395_2179; -.
DR PATRIC; fig|345073.21.peg.2106; -.
DR eggNOG; COG3143; Bacteria.
DR HOGENOM; CLU_080718_0_0_6; -.
DR OMA; EGPQIHA; -.
DR Proteomes; UP000000249; Chromosome 2.
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..239
FT /note="Protein phosphatase CheZ"
FT /id="PRO_0000410786"
FT SITE 168
FT /note="Enhances dephosphorylation of CheY-P"
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 27232 MW; CDF6959677C90C65 CRC64;
MISLEQAKEL VQLLEQGRQD DANRLFTYVY ESANNPMFKE IGMLTRDLHE ALKNFQIDER
FSEIATDEIP DARERLHYVI QKTEVAANKT MDAVDRCMPI ADKLHESLLL IRPEWNGLMN
GRIELMHFKS LCHRIDDLLS QVEGDSSELR GELTEILMAQ DFQDLTGQII KRVINLVNEV
EKRLVEILTV FGAAQKEQKA DKATVASIEP EGPILNPHER IDAVSSQDEV DDLLSSLGF