ID Q9WYN0_THEMA Unreviewed; 225 AA. AC Q9WYN0; G4FHV8; DT 01-NOV-1999, integrated into UniProtKB/TrEMBL. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 167. DE SubName: Full=Response regulator {ECO:0000313|EMBL:AAD35484.1}; GN OrderedLocusNames=TM_0399 {ECO:0000313|EMBL:AAD35484.1}; 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 {ECO:0000313|EMBL:AAD35484.1, ECO:0000313|Proteomes:UP000008183}; RN [1] {ECO:0000313|EMBL:AAD35484.1, ECO:0000313|Proteomes:UP000008183} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8 RC {ECO:0000313|Proteomes:UP000008183}; 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., 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., Heidelberg J., RA Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O., RA 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 [2] {ECO:0007829|PDB:1KGS} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). RX PubMed=11839301; DOI=10.1016/S0969-2126(01)00706-7; RA Buckler D.R., Zhou Y., Stock A.M.; RT "Evidence of intradomain and interdomain flexibility in an OmpR/PhoB RT homolog from Thermotoga maritima."; RL Structure 10:153-164(2002). RN [3] {ECO:0007829|PDB:3NNN} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-122 IN COMPLEX WITH MAGNESIUM. RX PubMed=20702407; DOI=10.1074/jbc.M110.157164; RA Barbieri C.M., Mack T.R., Robinson V.L., Miller M.T., Stock A.M.; RT "Regulation of response regulator autophosphorylation through interdomain RT contacts."; RL J. Biol. Chem. 285:32325-32335(2010). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. 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; AE000512; AAD35484.1; -; Genomic_DNA. DR PIR; H72382; H72382. DR RefSeq; NP_228209.1; NC_000853.1. DR RefSeq; WP_004083233.1; NZ_CP011107.1. DR PDB; 1KGS; X-ray; 1.50 A; A=1-225. DR PDB; 3NNN; X-ray; 2.20 A; A/B=1-122. DR PDBsum; 1KGS; -. DR PDBsum; 3NNN; -. DR AlphaFoldDB; Q9WYN0; -. DR SMR; Q9WYN0; -. DR PaxDb; 243274-THEMA_02730; -. DR EnsemblBacteria; AAD35484; AAD35484; TM_0399. DR KEGG; tma:TM0399; -. DR PATRIC; fig|243274.5.peg.404; -. DR InParanoid; Q9WYN0; -. DR OrthoDB; 48397at2; -. DR EvolutionaryTrace; Q9WYN0; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd17625; REC_OmpR_DrrD-like; 1. DR CDD; cd00383; trans_reg_C; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 6.10.250.690; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR039420; WalR-like. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR48111; REGULATOR OF RPOS; 1. DR PANTHER; PTHR48111:SF22; TRANSCRIPTIONAL REGULATORY PROTEIN CIAR; 1. DR Pfam; PF00072; Response_reg; 1. DR Pfam; PF00486; Trans_reg_C; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00862; Trans_reg_C; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR PROSITE; PS51755; OMPR_PHOB; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1KGS, ECO:0007829|PDB:3NNN}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE- KW ProRule:PRU01091}; Metal-binding {ECO:0007829|PDB:3NNN}; KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}; KW Reference proteome {ECO:0000313|Proteomes:UP000008183}. FT DOMAIN 4..118 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 126..224 FT /note="OmpR/PhoB-type" FT /evidence="ECO:0000259|PROSITE:PS51755" FT DNA_BIND 126..224 FT /note="OmpR/PhoB-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01091" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:3NNN" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:3NNN" FT BINDING 53 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:3NNN" FT BINDING 55 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:3NNN" FT MOD_RES 53 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 225 AA; 26015 MW; 4CB1F2CC82A218F7 CRC64; MNVRVLVVED ERDLADLITE ALKKEMFTVD VCYDGEEGMY MALNEPFDVV ILDIMLPVHD GWEILKSMRE SGVNTPVLML TALSDVEYRV KGLNMGADDY LPKPFDLREL IARVRALIRR KSESKSTKLV CGDLILDTAT KKAYRGSKEI DLTKKEYQIL EYLVMNKNRV VTKEELQEHL WSFDDEVFSD VLRSHIKNLR KKVDKGFKKK IIHTVRGIGY VARDE //