ID   CHEY_CAMJ8              Reviewed;         130 AA.
AC   A8FMH1; P71129; Q0P9D6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Chemotaxis protein CheY homolog;
GN   Name=cheY; OrderedLocusNames=C8J_1059;
OS   Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS   11828).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=407148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Marchant J.E., Henderson J., Wren B.W., Ketley J.M.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9720026; DOI=10.1099/00221287-144-8-2049;
RA   Fry B.N., Korolik V., ten Brinke J.A., Pennings M.T.T., Zalm R.,
RA   Teunis B.J.J., Coloe P.J., van der Zeijst B.A.M.;
RT   "The lipopolysaccharide biosynthesis locus of Campylobacter jejuni 81116.";
RL   Microbiology 144:2049-2061(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81116 / NCTC 11828;
RX   PubMed=17873037; DOI=10.1128/jb.01404-07;
RA   Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA   van Vliet A.H.M.;
RT   "The complete genome sequence of Campylobacter jejuni strain 81116
RT   (NCTC11828).";
RL   J. Bacteriol. 189:8402-8403(2007).
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; U75208; AAB17571.1; -; Genomic_DNA.
DR   EMBL; Y11648; CAA72347.1; -; Genomic_DNA.
DR   EMBL; CP000814; ABV52658.1; -; Genomic_DNA.
DR   RefSeq; WP_002866134.1; NC_009839.1.
DR   AlphaFoldDB; A8FMH1; -.
DR   SMR; A8FMH1; -.
DR   KEGG; cju:C8J_1059; -.
DR   HOGENOM; CLU_000445_69_12_7; -.
DR   OMA; AAGAHEY; -.
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; Two-component regulatory system.
FT   CHAIN           1..130
FT                   /note="Chemotaxis protein CheY homolog"
FT                   /id="PRO_0000315387"
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