CHEZ_ECO57
ID CHEZ_ECO57 Reviewed; 214 AA.
AC Q8XCG0; Q7AD54;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein phosphatase CheZ;
DE EC=3.1.3.-;
DE AltName: Full=Chemotaxis protein CheZ;
GN Name=cheZ; OrderedLocusNames=Z2935, ECs2591;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56871.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36014.1; -; Genomic_DNA.
DR PIR; C85801; C85801.
DR PIR; G90952; G90952.
DR RefSeq; NP_310618.1; NC_002695.1.
DR RefSeq; WP_000983602.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XCG0; -.
DR SMR; Q8XCG0; -.
DR STRING; 155864.EDL933_2856; -.
DR EnsemblBacteria; AAG56871; AAG56871; Z2935.
DR EnsemblBacteria; BAB36014; BAB36014; ECs_2591.
DR GeneID; 912565; -.
DR KEGG; ece:Z2935; -.
DR KEGG; ecs:ECs_2591; -.
DR PATRIC; fig|386585.9.peg.2717; -.
DR eggNOG; COG3143; Bacteria.
DR HOGENOM; CLU_080718_1_0_6; -.
DR OMA; EGPQIHA; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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..214
FT /note="Protein phosphatase CheZ"
FT /id="PRO_0000410776"
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; A3E29BF134D716D3 CRC64;
MMQPSIKPAD EHSAGDIIAR IGSLTRMLRD SLRELGLDQA IAEAAEAIPD ARDRLYYVVQ
MTAQAAERAL NSVEASQPHQ DQMEKSAKAL TQRWDDWFAD PIDLADAREL VTDTRKFLAD
VPAHTSFTNA QLLEIMMAQD FQDLTGQVIK RMMDVIQEIE RQLLMVLLEN IPEQESRPKR
ENQSLLNGPQ VDTSKAGVVA SQDQVDDLLD SLGF