ID A0A1N7N277_9BACI Unreviewed; 617 AA. AC A0A1N7N277; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 16-JAN-2019, entry version 9. DE SubName: Full=PAS/PAC sensor signal transduction histidine kinase {ECO:0000313|EMBL:SIS92301.1}; 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; CC Evidence={ECO:0000256|SAAS:SAAS01126420}; 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 Proteomes; UP000199777; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR CDD; cd06225; HAMP; 1. DR CDD; cd00075; HATPase_c; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 3.30.565.10; -; 1. 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 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; SSF47384; SSF47384; 1. DR SUPFAM; SSF55785; SSF55785; 1. DR SUPFAM; SSF55874; SSF55874; 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|SAAS:SAAS00925949}; KW Complete proteome {ECO:0000313|Proteomes:UP000199777}; KW Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:SIS92301.1}; KW Membrane {ECO:0000256|SAAS:SAAS00925724, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310}; KW Transferase {ECO:0000256|SAAS:SAAS01003669}; KW Transmembrane {ECO:0000256|SAAS:SAAS00926038, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00926160, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 214 266 HAMP. {ECO:0000259|PROSITE:PS50885}. FT DOMAIN 271 327 PAS. {ECO:0000259|PROSITE:PS50112}. FT DOMAIN 335 389 PAC. {ECO:0000259|PROSITE:PS50113}. FT DOMAIN 393 610 Histidine kinase. {ECO:0000259|PROSITE: FT 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 //