ID A0A1E7VF39_9BURK Unreviewed; 590 AA. AC A0A1E7VF39; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 07-APR-2021, entry version 18. DE RecName: Full=Histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN Name=dctB_3 {ECO:0000313|EMBL:OEZ59931.1}; GN ORFNames=DUGA6_35700 {ECO:0000313|EMBL:OEZ59931.1}; OS Duganella sp. HH105. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Oxalobacteraceae; Duganella; unclassified Duganella. OX NCBI_TaxID=1781067 {ECO:0000313|EMBL:OEZ59931.1, ECO:0000313|Proteomes:UP000175764}; RN [1] {ECO:0000313|EMBL:OEZ59931.1, ECO:0000313|Proteomes:UP000175764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH105 {ECO:0000313|EMBL:OEZ59931.1, RC ECO:0000313|Proteomes:UP000175764}; RA Haack F.S., Poehlein A., Kroger C., Voigt C.A., Piepenbring M., Bode H.B., RA Daniel R., Schafer W., Streit W.R.; RT "Molecular Keys to the Janthinobacterium and Duganella spp. Interaction RT with the Plant Pathogen Fusarium graminearum."; RL Front. Microbiol. 7:0-0(2016). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OEZ59931.1}. 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; LRHV01000011; OEZ59931.1; -; Genomic_DNA. DR RefSeq; WP_070359577.1; NZ_LRHV01000011.1. DR EnsemblBacteria; OEZ59931; OEZ59931; DUGA6_35700. DR PATRIC; fig|1781067.3.peg.3633; -. DR Proteomes; UP000175764; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; 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; IPR033479; dCache_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; IPR029151; Sensor-like_sf. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR017055; Sig_transdc_His_kinase_DctB. DR Pfam; PF02743; dCache_1; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PIRSF; PIRSF036431; STHK_DctB; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF103190; SSF103190; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000313|EMBL:OEZ59931.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 280..299 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 376..587 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT COILED 330..360 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 590 AA; 63896 MW; 94A91B9246D7C249 CRC64; MRAQKNLLLF AFTFACALGV IAGSYLAGTW RAREELRQQG QRQLQLMAPD LQSLLQKYET LPFVLGFQPD LIEALAHPSD ASAITRLNST LQTIQQQAKV GAIYVMDRDG LTIGASNWDQ PLGFVGKNFS YRPYFDAALH GRAGRFYGIG TSTSEAGYFI AQPVYRNGTA GGPVTGVVAV KISLADFERT WRSSDDTIAL ADSSGVVFLS NRPDWIYRSL HALDAATERQ LAHTQQYTGQ KITPLSGHSD LFVTQSVGQL GWQLMLFPGQ SRVLRAGAQW AAAATLLLAC AAVSSWALHQ RRRRLEERMA SAAALRQAAA ELDDKIVERT QQLRTTNQHL ESKYAKLQET EHLLRSTQNE LVQAGKLAML GQMAAGITHE LNQPLAAIRA FADNARVFLE RGQGEQVAGN LGHISEASAR MGAIIGQLKG FARKDETVAT VDLAASVRAS AFLLESEFRR HAVALEIAST DGLHVTGSSV RIEQVLINLL RNALDAVETA ERRVVVIALE RDGACALVSI SDSGEGIPEQ VVAHLFEPFF TTKPSGKGLG LGLAISSSIV QAMNGQLTAH NQAGGGARFE LRLPLQTEGV //