ID A0A5S9F0S3_RHOMR Unreviewed; 1348 AA. AC A0A5S9F0S3; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 27-MAR-2024, entry version 15. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=RmaAA338_18730 {ECO:0000313|EMBL:BBM73008.1}; OS Rhodothermus marinus (Rhodothermus obamensis). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae; OC Rhodothermus. OX NCBI_TaxID=29549 {ECO:0000313|EMBL:BBM73008.1, ECO:0000313|Proteomes:UP000464918}; RN [1] {ECO:0000313|Proteomes:UP000464918} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AA3-38 {ECO:0000313|Proteomes:UP000464918}; RA Tomariguchi N., Miyazaki K.; RT "Complete Genome Sequences of Rhodothermus marinus Strains AA2-13 and AA3- RT 38, Isolated from Arima Onsen Hot Spring in Japan."; RL Microbiol. Resour. Announc. 9:e01475-19(2020). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085}; 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; AP019797; BBM73008.1; -; Genomic_DNA. DR Proteomes; UP000464918; Chromosome. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00890; Prefoldin; 1. DR CDD; cd00156; REC; 1. DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P. DR InterPro; IPR036097; HisK_dim/P_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011110; Reg_prop. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1. DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF07494; Reg_prop; 6. DR Pfam; PF00072; Response_reg; 2. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00448; REC; 2. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2. DR SUPFAM; SSF52172; CheY-like; 2. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 2. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE- KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..23 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 24..1348 FT /note="histidine kinase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5030137756" FT DOMAIN 822..1042 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT DOMAIN 1061..1183 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 1225..1343 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT REGION 1191..1228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 760..822 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 1191..1223 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1115 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" FT MOD_RES 1274 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 1348 AA; 152557 MW; 0984231B1C14AF7F CRC64; MLRRPCFHWF YGLALLIALP ALAQQHYFHT YTSADGLSQL VVQALLQDRE GYVWIGTQAG LNRFDGFGFE TFSLRDGLVG DFIWALAEGP DGSLWIGTRN GLSRREPNGR FTSFSLAEGL PSPDVRALTV TADGTVWIGT PRGLAYLKDD RIERVETLGT QAIYDFLIDR KRQLYVATQN GLYRWAPPRW VPVAPFTEQP VYRLLEDLEG RLWVSTADAL VVLAGGRRVA RYTEKDGLKG LPARDLAVDS LGVVWVVTLE GLGRIDATGV RWLTEANGLP TSVLNALMVD REGMLWLGSL KGVSQFRGRA FTNYTVRDGL ADNLVRPIVR DRQGYLWVGT RRGLNRFDGR RWAVYTEKDG LPSEFVRSLF LDSRGRLWIG TLRGLALYEN GRFHRVPGFP HEASVMSIVE DHQGRIWLAA QNLGVFRQNG ARFIPVEVPG QVFTDARLLV DRRGHVWISG DMGLSRWDGR HWRTFTSKDG LAGNNPYFLA EDLQGRIWFG YHAALGITVY DPEQNRFRTY TTADGLHNDA VYSIGVDHQN NIWIGTSRGV DRFDGERFVN YSPLEGYASY ESNAGGFFAD VDGTLWFGTM DGLSHYNPRE DLWNDRPPRV RLTYLQLGDR PVNPDSLVQV SYKANTLTAR VALLSFFGAE QIQLRYRLRS MDTDWNLTFQ PLQRNRSWLR KPISSEEGWR PLESPTIFLT NLPAGFYVLE VQARKPTSDW SRPAAARFEI TPPFWQTAWF AALVVTLLGL LVGGIHRYRI YRIEQQKEQL EALVQERTAE LQAQKRQLKA TLEDLRQTKE ELERANEELV RASRLKSEFL ANMSHEIRTP MNGVLGMTEL LLEMDLTKEQ RECVEIIHRS GETLLTILND ILDFSKIEAG RLELENIDFN LQETIEDVIT LFAPRAAAKQ LELICFIEER ALEVQGDPHR LRQVLSNLIG NAIKFTERGE VVVEAELERL NERRAYWRIS VRDTGIGIPP DRLSHLFQPF TQLDGSTTRR YGGTGLGLAI SKQLVEMMGG TIGVESEVGK GSTFTVRIPF RLSSQRKLNG DERRALLKDV RVLIVDDNET NREILRRQTL GWGMVPTLAR SGAEALELMR AAARQGHPFE LAILDMMMPE MDGIMLAREI KQDPALAATP LILLSSYLFT REDHRAMDET LFAAVLSKPT RQSYLFNTLV RVLQEMRSVA AEKQQPQRTE SATVPDQSDS SDAPSTTPRS TSRGHLLLAE DNPVNQKVAL YHLERLGYTC DVVSDGKQAV EAALRGGYDA ILMDVHMPVM DGFEATALIR EHEANLGRHT PIIAMTANAL RGERERCLEA GMDDYIAKPF KKDELKTVLE RWIQKAEA //