CHEY_THEMA
ID CHEY_THEMA Reviewed; 120 AA.
AC Q56312;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Chemotaxis protein CheY;
GN Name=cheY; OrderedLocusNames=TM_0700;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=8550470; DOI=10.1128/jb.178.2.484-489.1996;
RA Swanson R.V., Sanna M.G., Simon M.I.;
RT "Thermostable chemotaxis proteins from the hyperthermophilic bacterium
RT Thermotoga maritima.";
RL J. Bacteriol. 178:484-489(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND PHOSPHORYLATION AT ASP-54.
RX PubMed=9521117; DOI=10.1002/pro.5560070221;
RA Usher K.C., de la Cruz A.F.A., Dahlquist F.W., Swanson R.V., Simon M.I.,
RA Remington S.J.;
RT "Crystal structures of CheY from Thermotoga maritima do not support
RT conventional explanations for the structural basis of enhanced
RT thermostability.";
RL Protein Sci. 7:403-412(1998).
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;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- INTERACTION:
CC Q56312; Q9WZE6: fliM; NbExp=2; IntAct=EBI-1039694, EBI-6981685;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated by CheA. {ECO:0000250}.
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DR EMBL; U30501; AAA96389.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35782.1; -; Genomic_DNA.
DR PIR; B72346; B72346.
DR RefSeq; NP_228509.1; NC_000853.1.
DR RefSeq; WP_004081049.1; NZ_CP011107.1.
DR PDB; 1TMY; X-ray; 1.90 A; A=1-120.
DR PDB; 1U0S; X-ray; 1.90 A; Y=2-119.
DR PDB; 2LLE; NMR; -; A=1-103.
DR PDB; 2TMY; X-ray; 2.30 A; A=1-120.
DR PDB; 3TMY; X-ray; 2.20 A; A/B=1-120.
DR PDB; 4IGA; X-ray; 1.73 A; A=1-120.
DR PDB; 4QWV; X-ray; 2.45 A; A=4-104.
DR PDB; 4QYW; X-ray; 1.60 A; A=2-120.
DR PDB; 4TMY; X-ray; 2.80 A; A/B=1-120.
DR PDB; 6C40; X-ray; 2.70 A; B/D=2-119.
DR PDBsum; 1TMY; -.
DR PDBsum; 1U0S; -.
DR PDBsum; 2LLE; -.
DR PDBsum; 2TMY; -.
DR PDBsum; 3TMY; -.
DR PDBsum; 4IGA; -.
DR PDBsum; 4QWV; -.
DR PDBsum; 4QYW; -.
DR PDBsum; 4TMY; -.
DR PDBsum; 6C40; -.
DR AlphaFoldDB; Q56312; -.
DR SMR; Q56312; -.
DR DIP; DIP-35249N; -.
DR IntAct; Q56312; 2.
DR STRING; 243274.THEMA_01165; -.
DR PRIDE; Q56312; -.
DR EnsemblBacteria; AAD35782; AAD35782; TM_0700.
DR KEGG; tma:TM0700; -.
DR eggNOG; COG2201; Bacteria.
DR InParanoid; Q56312; -.
DR OMA; AAGAHEY; -.
DR OrthoDB; 1630092at2; -.
DR EvolutionaryTrace; Q56312; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytoplasm; Flagellar rotation; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome;
KW Two-component regulatory system.
FT CHAIN 1..120
FT /note="Chemotaxis protein CheY"
FT /id="PRO_0000081055"
FT DOMAIN 4..119
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:9521117"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4QYW"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:4QYW"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4QYW"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:4QYW"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:4QYW"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4QYW"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4QYW"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4QYW"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4QYW"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:4QYW"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:4QYW"
SQ SEQUENCE 120 AA; 13217 MW; 195AC95641264E63 CRC64;
MGKRVLIVDD AAFMRMMLKD IITKAGYEVA GEATNGREAV EKYKELKPDI VTMDITMPEM
NGIDAIKEIM KIDPNAKIIV CSAMGQQAMV IEAIKAGAKD FIVKPFQPSR VVEALNKVSK
