ID A9WBS8_CHLAA Unreviewed; 739 AA. AC A9WBS8; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN OrderedLocusNames=Caur_1667 {ECO:0000313|EMBL:ABY34885.1}; OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl). OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae; OC Chloroflexaceae; Chloroflexus. OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY34885.1, ECO:0000313|Proteomes:UP000002008}; RN [1] {ECO:0000313|Proteomes:UP000002008} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl RC {ECO:0000313|Proteomes:UP000002008}; RX PubMed=21714912; DOI=10.1186/1471-2164-12-334; RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.; RT "Complete genome sequence of the filamentous anoxygenic phototrophic RT bacterium Chloroflexus aurantiacus."; RL BMC Genomics 12:334-334(2011). 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; CP000909; ABY34885.1; -; Genomic_DNA. DR RefSeq; WP_012257539.1; NC_010175.1. DR RefSeq; YP_001635274.1; NC_010175.1. DR AlphaFoldDB; A9WBS8; -. DR STRING; 324602.Caur_1667; -. DR EnsemblBacteria; ABY34885; ABY34885; Caur_1667. DR KEGG; cau:Caur_1667; -. DR PATRIC; fig|324602.8.peg.1906; -. DR eggNOG; COG0643; Bacteria. DR eggNOG; COG0745; Bacteria. DR HOGENOM; CLU_000650_2_1_0; -. DR InParanoid; A9WBS8; -. DR Proteomes; UP000002008; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006935; P:chemotaxis; IEA:InterPro. DR CDD; cd00088; HPT; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 1.20.120.160; HPT domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR004105; CheA-like_dim. DR InterPro; IPR037006; CheA-like_homodim_sf. DR InterPro; IPR036061; CheW-like_dom_sf. DR InterPro; IPR002545; CheW-lke_dom. 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; IPR036097; HisK_dim/P_sf. DR InterPro; IPR036641; HPT_dom_sf. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1. DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1. DR Pfam; PF01584; CheW; 1. DR Pfam; PF02895; H-kinase_dim; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01627; Hpt; 1. DR Pfam; PF00072; Response_reg; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00260; CheW; 1. DR SMART; SM01231; H-kinase_dim; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00073; HPT; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF50341; CheW-like; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR PROSITE; PS50851; CHEW; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50894; HPT; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}; KW Reference proteome {ECO:0000313|Proteomes:UP000002008}. FT DOMAIN 1..106 FT /note="HPt" FT /evidence="ECO:0000259|PROSITE:PS50894" FT DOMAIN 221..460 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT DOMAIN 462..598 FT /note="CheW-like" FT /evidence="ECO:0000259|PROSITE:PS50851" FT DOMAIN 618..734 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT REGION 131..156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 11..38 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 132..148 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 49 FT /note="Phosphohistidine" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110" FT MOD_RES 667 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 739 AA; 81709 MW; 4ED64849297978E4 CRC64; MDLTSFYDQF RDETAENVRV LNDALLNLEA QVDDGQRRAA LDRAFRAVHT IKGSARMLGF DPIAQLAHAL EHVLGDLREG RCIPERTLID LLLQGGDLVT RLTAEIPQLS AATLAHLPDF LQALRAISPA IPSVSPPTPQ PASPEPSSPI DTPLRTTRQT VRVRVDRLDR LFNLAGELTI EQQSLAELGT ELEQLYALVS RQQRALLALE QELARLRFSS TQRQALDARL STLRDVQVML VDRVQNQREN LDRYLSRQHL LVKDLEQEVM AVRLLPIATI FNSLPRLVRD LATATGKQAV LEIRGETTEL DRKVLELISD PLVHLIRNAV DHGLEPPDER IAQGKPPTGL IQVSAESSGN EVRISIQDDG RGIDPARIRT RAIELGLLTA GRADQLDTQE TLDLIFQPGF STATNVTEIS GRGVGMDIVR ANLLELGGQV RIDSTIGQGT TITLTIPLTL ITSRVVVVQV GQHHLALPAV TVRSILWVQR DQIQFIDGQP TFAHQQRTIS LLALAELLAI PAESPLTRYR RVPAVLLKTR QHRVALLVDD VIDEREAVIK PLGPLFARRP ALSGAVQSGD GRLVLLINPL YLVERNGYRP KPAATAIKPV AEPTRTARLL VVDDSFTTRE LLRSILQSAG YDVTVAIDGA DALDRLRSTP YDLVVSDIEM PRVDGFTLTT RIRNELALVD LPVILITSLA SEEHRRRGLE VGAQAYIVKS QFNQDSLLNV IQQLLGHEE //