ID   CHEY_CAMJE              Reviewed;         130 AA.
AC   P0C635; P71129; Q0P9D6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Chemotaxis protein CheY homolog;
GN   Name=cheY; OrderedLocusNames=Cj1118c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. CheY seems to regulate the
CC       clockwise (CW) rotation (By similarity). {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:0000305}.
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DR   EMBL; AL111168; CAL35235.1; -; Genomic_DNA.
DR   PIR; A81316; A81316.
DR   RefSeq; WP_002866134.1; NC_002163.1.
DR   RefSeq; YP_002344511.1; NC_002163.1.
DR   AlphaFoldDB; P0C635; -.
DR   SMR; P0C635; -.
DR   IntAct; P0C635; 6.
DR   STRING; 192222.Cj1118c; -.
DR   PaxDb; P0C635; -.
DR   PRIDE; P0C635; -.
DR   EnsemblBacteria; CAL35235; CAL35235; Cj1118c.
DR   GeneID; 905409; -.
DR   KEGG; cje:Cj1118c; -.
DR   PATRIC; fig|192222.6.peg.1100; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_69_12_7; -.
DR   OMA; AAGAHEY; -.
DR   Proteomes; UP000000799; 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   Chemotaxis; Cytoplasm; Flagellar rotation; Magnesium; Metal-binding;
KW   Phosphoprotein; Reference proteome; Two-component regulatory system.
FT   CHAIN           1..130
FT                   /note="Chemotaxis protein CheY homolog"
FT                   /id="PRO_0000081049"
FT   DOMAIN          2..120
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         53
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   130 AA;  14437 MW;  41634D8ADE6C5081 CRC64;
     MKLLVVDDSS TMRRIIKNTL TRLGHDDVLE AEHGVEAWDL LTKNEDVKVL ITDWNMPEMN
     GLELVKKVRA EKKYEDMPII MVTTEGGKAE VITALKAGVN NYIVKPFTPQ VLKEKLEDVL
     GTGSGEGAAE