ID   CHEY_CAMJJ              Reviewed;         130 AA.
AC   A1W0A5; P71129;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Chemotaxis protein CheY homolog;
GN   Name=cheY; OrderedLocusNames=CJJ81176_1136;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9076738; DOI=10.1046/j.1365-2958.1997.2861650.x;
RA   Yao R., Burr D.H., Guerry P.;
RT   "CheY-mediated modulation of Campylobacter jejuni virulence.";
RL   Mol. Microbiol. 23:1021-1032(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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).
CC       {ECO:0000250|UniProtKB:P0AE67}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P0AE67};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0AE67};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC44858.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U62038; AAC44858.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000538; EAQ72145.1; -; Genomic_DNA.
DR   RefSeq; WP_002866134.1; NC_008787.1.
DR   AlphaFoldDB; A1W0A5; -.
DR   SMR; A1W0A5; -.
DR   KEGG; cjj:CJJ81176_1136; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_000445_69_12_7; -.
DR   Proteomes; UP000000646; 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   CDD; cd19923; REC_CheY_CheY3; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR44591:SF3; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44591; STRESS RESPONSE REGULATOR PROTEIN 1; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 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_0000281899"
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|UniProtKB:A0A0H3AMJ9"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE67"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE67"
FT   BINDING         55
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE67"
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
//