ID A0A1N7N277_9BACI Unreviewed; 617 AA. AC A0A1N7N277; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 22-FEB-2023, entry version 19. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=SAMN05421758_11061 {ECO:0000313|EMBL:SIS92301.1}; OS Salimicrobium salexigens. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Salimicrobium. OX NCBI_TaxID=908941 {ECO:0000313|EMBL:SIS92301.1, ECO:0000313|Proteomes:UP000199777}; RN [1] {ECO:0000313|EMBL:SIS92301.1, ECO:0000313|Proteomes:UP000199777} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22782 {ECO:0000313|EMBL:SIS92301.1, RC ECO:0000313|Proteomes:UP000199777}; RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. 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; FTOK01000010; SIS92301.1; -; Genomic_DNA. DR RefSeq; WP_076572447.1; NZ_FTOK01000010.1. DR AlphaFoldDB; A0A1N7N277; -. DR EnsemblBacteria; SIS92301; SIS92301; SAMN05421758_11061. DR Proteomes; UP000199777; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd06225; HAMP; 1. DR CDD; cd00075; HATPase; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 2. DR InterPro; IPR003660; HAMP_dom. 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; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1. DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF00989; PAS; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF158472; HAMP domain-like; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SIS92301.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}. FT TRANSMEM 12..34 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 193..216 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 214..266 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 271..327 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT DOMAIN 335..389 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" FT DOMAIN 393..610 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" SQ SEQUENCE 617 AA; 69616 MW; 67DFD10C83BDC440 CRC64; MSKVGFFQSV RLKLIIVYIL LILLGLQVIG AYFVDRLEAQ LQNNFTESVE SRLDALAFNI QQAFEEDRTE EDPSLESDVQ SILNSFNEGY VRNEIRQLQV IEEGSNVVIA AYASGDATPQ ANVGKKTTNP DVLSAFLLQD QSSPETRVDS ETGQRLWVGT RTITNDVDET VAAIYFEADM SPVYEELQDI NTIFANGTVI SIIVTAILGI IVAGTITKPL IEMRRQAQIM ATGDFSQKVN VHGNDEIGQL GHTFNDLNDK LKISQATTEG ERRKLSSVLS HMSDGVIATD RLGIITLMNA PASHLIGQRF EQVQGKPLID VLGLEDQVSS AKEMEDLDSV IVDMSTNDQH LLLKANFSVV QDEHYEMNGF ITVISDVTEQ QRADQERREF VSNVSHELRT PLTTMRSYLE ALNDGAWRDE EIAPRFLDVT QNETDRMIRL VNDLLQLTKM DHKESSFYKE KVEFVSFLEQ IIERFEMNKR EDIQFSKQLP SDNVYVWLDK DKVTQVLDNV ISNATKYSPE GGTIHFAVKR VRQKLQVSIK DEGLGMPAHT VEKIFDRFYR VDKARSREIG GTGLGLAIAR EIIEAHHGEI WAESQEGKGT TVFFTLPLMR QKRRGNK //