ID A0A0Q6KQC7_9BACI Unreviewed; 374 AA. AC A0A0Q6KQC7; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 19-JAN-2022, entry version 22. DE RecName: Full=Histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=ASG66_17490 {ECO:0000313|EMBL:KQU57545.1}; OS Bacillus sp. Leaf406. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1736368 {ECO:0000313|EMBL:KQU57545.1, ECO:0000313|Proteomes:UP000051502}; RN [1] {ECO:0000313|EMBL:KQU57545.1, ECO:0000313|Proteomes:UP000051502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf406 {ECO:0000313|EMBL:KQU57545.1, RC ECO:0000313|Proteomes:UP000051502}; RA Gilbert D.G.; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KQU57545.1, ECO:0000313|Proteomes:UP000051502} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Leaf406 {ECO:0000313|EMBL:KQU57545.1, RC ECO:0000313|Proteomes:UP000051502}; RA Schulze-Lefert P.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; RL Submitted (NOV-2015) 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 -!- 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:KQU57545.1}. 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; LMRU01000007; KQU57545.1; -; Genomic_DNA. DR RefSeq; WP_056540087.1; NZ_LMRU01000007.1. DR EnsemblBacteria; KQU57545; KQU57545; ASG66_17490. DR Proteomes; UP000051502; Unassembled WGS sequence. 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; IPR018984; Histidine_kinase_N. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF09385; HisK_N; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQU57545.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}. FT DOMAIN 163..369 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" SQ SEQUENCE 374 AA; 43892 MW; 04A03677D125731B CRC64; MTSPSEMMID FLKRHENEMI QNWLDDIVIS DTDKHKEEVE RNARRMFHLV IRAVERPLTE EEMLFLANKT AQERVDADVN ISEFVYNVNI GKSTIIKWLN HSFMEHGGFQ PKLDFVNELF DRFSYLAVRR YTEIKDQVLK EKELYIDQTH KERLTILGQM SSSFVHEFRN PLTSIVGFMK LLRNDYPDLP YMDIMQHELD QLNYRISQFL HVSRKELIES KQERMSLMSL LEELIEFLYP TLLDGDVSIQ SHCSPDVMIV GNKDEIRQVF LNLIMNSIDA LQEVQGYRHI NVSCEMLEDD VVVTFCNNGP RIEEEKIEAI FEPFFTTKDL GTGIGLYICR KLVEKHNGTL TCRSTDEKTT FTIRIPVEST VFQP //