ID W8Y7R0_BACTU Unreviewed; 424 AA. AC W8Y7R0; DT 14-MAY-2014, integrated into UniProtKB/TrEMBL. DT 14-MAY-2014, sequence version 1. DT 19-JAN-2022, entry version 35. DE RecName: Full=Histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=BTDB27_003866 {ECO:0000313|EMBL:CDN37524.1}; OS Bacillus thuringiensis DB27. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1431339 {ECO:0000313|EMBL:CDN37524.1}; RN [1] {ECO:0000313|EMBL:CDN37524.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DB27 {ECO:0000313|EMBL:CDN37524.1}; RA Iatsenko I., Pickard D., Corton C., Dougan G., Sommer R.J.; RT "Draft genome sequence of highly nematicidal Bacillus thuringiensis DB27."; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CDN37524.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DB27 {ECO:0000313|EMBL:CDN37524.1}; RA Aslett M.; RL Submitted (JAN-2014) 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 --------------------------------------------------------------------------- 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; HG810018; CDN37524.1; -; Genomic_DNA. DR RefSeq; WP_000420369.1; NZ_HG810018.1. DR EnsemblBacteria; CDN37524; CDN37524; BTDB27_003866. DR HOGENOM; CLU_000445_89_1_9; -. 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 CDD; cd00082; HisKA; 1. DR Gene3D; 3.30.565.10; -; 1. 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; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}; 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 7..24 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 39..63 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 75..96 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 102..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 131..154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 166..187 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 216..421 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT COILED 187..207 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 424 AA; 47848 MW; 17C957A24B880EF0 CRC64; MELIRDLLIQ IAIIILPLFL YEAIRLNRYQ EMPPKPNRYF IMFLSSVTLV LSMTYSICFG NVCGYNFHPI PIVSGFLYGG IVGLIPAVIF VAYEWLLKGM SFLPVLEVIF LLIVPLFLSK KWSLFSRDKK LILAFMISSF YVLVSLVLGM INVLLETGFT PYISQIYSGF IFASLIMVMT MVFQVYLTEY LNENALLRTE MQKSEKLNIV SELAASVAHE VRNPLTVVRG FIQLLESTED VKNKDYMRLV LAELDRAEQI ISDYLNLARP QIEKKEHICL SAQLIEMTTL MSSFAAMQGV YLQVEISESL YTIGDKTKLK QAIMNVVKNG IEAIQGNKGY LKVTAIQKDE TIIIRVKDSG VGMTKEQLAR LGQPYYSLKE KGTGLGLMVT FSILQAHNGT LEYKSESGKG TEAIIILPAV QNKE //