ID   CHEY_ENTCL              Reviewed;         129 AA.
AC   Q9FAD7;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Chemotaxis protein CheY;
GN   Name=cheY;
OS   Enterobacter cloacae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 7256 / NBRC 3320;
RX   PubMed=11302189; DOI=10.1271/bbb.65.456;
RA   Kato J., Nagata C., Yang L., Kuroda A., Ikeda T., Takiguchi N., Ohtake H.;
RT   "Isolation and characterization of the Enterobacter cloacae cheR mutant
RT   defective in phosphate taxis.";
RL   Biosci. Biotechnol. Biochem. 65:456-458(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;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB040876; BAB15841.1; -; Genomic_DNA.
DR   RefSeq; WP_008500431.1; NZ_WNXG01000101.1.
DR   AlphaFoldDB; Q9FAD7; -.
DR   SMR; Q9FAD7; -.
DR   STRING; 1399774.JDWH01000002_gene2957; -.
DR   GeneID; 63987531; -.
DR   GeneID; 67461649; -.
DR   eggNOG; COG0745; Bacteria.
DR   OMA; AAGAHEY; -.
DR   OrthoDB; 1630092at2; -.
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; 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_0000081043"
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;  14042 MW;  62C255BAC8B7A1D5 CRC64;
     MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG FGFVISDWNM
     PNMDGLELLK TIRADAGMAS MPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL
     GKIFEKLGM