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 27-MAR-2024, entry version 156. 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; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC 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) IN COMPLEX WITH MG(2+), COFACTOR, AND RP 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). CC {ECO:0000250|UniProtKB:P0AE67}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:9521117}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:9521117}; CC -!- INTERACTION: CC Q56312; Q9WZE6: fliM; NbExp=2; IntAct=EBI-1039694, EBI-6981685; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- PTM: Phosphorylated by CheA. {ECO:0000250|UniProtKB:P0AE67}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.TM_0700; -. DR PaxDb; 243274-THEMA_01165; -. DR EnsemblBacteria; AAD35782; AAD35782; TM_0700. DR KEGG; tma:TM0700; -. DR eggNOG; COG2201; Bacteria. DR InParanoid; Q56312; -. DR OrthoDB; 9793421at2; -. 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 CDD; cd17542; REC_CheY; 1. DR Gene3D; 3.40.50.2300; -; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR PANTHER; PTHR43228; TWO-COMPONENT RESPONSE REGULATOR; 1. DR PANTHER; PTHR43228:SF1; TWO-COMPONENT RESPONSE REGULATOR ARR22; 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 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 /evidence="ECO:0000250|UniProtKB:A0A0H3AMJ9" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:9521117, FT ECO:0007744|PDB:4TMY" FT BINDING 54 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:9521117, FT ECO:0007744|PDB:4TMY" FT BINDING 56 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:9521117, FT ECO:0007744|PDB:4TMY" 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 //