CHEY_CAMJJ
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 03-AUG-2022, entry version 80.
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; Proteobacteria; 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). {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}.
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 STRING; 354242.CJJ81176_1136; -.
DR EnsemblBacteria; EAQ72145; EAQ72145; CJJ81176_1136.
DR KEGG; cjj:CJJ81176_1136; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_69_12_7; -.
DR OMA; AAGAHEY; -.
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 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_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"
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
