ID   CHEY_ECO57              Reviewed;         129 AA.
AC   P0AE68; P06143;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Chemotaxis protein CheY;
GN   Name=cheY; OrderedLocusNames=Z2936, ECs2592;
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: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. In its active (phosphorylated
CC       or acetylated) form, CheY exhibits enhanced binding to a switch
CC       component, FliM, at the flagellar motor which induces a change from
CC       counterclockwise to clockwise flagellar rotation (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase,
CC       depending on which acetate metabolism pathway is available.
CC       {ECO:0000250}.
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DR   EMBL; AE005174; AAG56872.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36015.1; -; Genomic_DNA.
DR   PIR; D85801; D85801.
DR   PIR; H90952; H90952.
DR   RefSeq; NP_310619.1; NC_002695.1.
DR   RefSeq; WP_000763867.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AE68; -.
DR   BMRB; P0AE68; -.
DR   SMR; P0AE68; -.
DR   MINT; P0AE68; -.
DR   STRING; 155864.EDL933_2857; -.
DR   EnsemblBacteria; AAG56872; AAG56872; Z2936.
DR   EnsemblBacteria; BAB36015; BAB36015; ECs_2592.
DR   GeneID; 66674227; -.
DR   GeneID; 914203; -.
DR   KEGG; ece:Z2936; -.
DR   KEGG; ecs:ECs_2592; -.
DR   PATRIC; fig|386585.9.peg.2718; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_69_12_6; -.
DR   OMA; AAGAHEY; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; 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:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chemotaxis; Cytoplasm; Flagellar rotation; Magnesium;
KW   Metal-binding; Phosphoprotein; Reference proteome;
KW   Two-component regulatory system.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..129
FT                   /note="Chemotaxis protein CheY"
FT                   /id="PRO_0000081041"
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         92
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   129 AA;  14097 MW;  E4B60B8A73DA14DC CRC64;
     MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG YGFVISDWNM
     PNMDGLELLK TIRADGAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL
     NKIFEKLGM