ID A0A7Y5ZGD8_9MICO Unreviewed; 592 AA. AC A0A7Y5ZGD8; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 24-JUL-2024, entry version 9. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=HNO83_14310 {ECO:0000313|EMBL:NUU07513.1}; OS Leifsonia sp. C5G2. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Leifsonia. OX NCBI_TaxID=2735269 {ECO:0000313|EMBL:NUU07513.1, ECO:0000313|Proteomes:UP000576379}; RN [1] {ECO:0000313|EMBL:NUU07513.1, ECO:0000313|Proteomes:UP000576379} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C5G2 {ECO:0000313|EMBL:NUU07513.1, RC ECO:0000313|Proteomes:UP000576379}; RA Nordstedt N.P., Jones M.L.; RT "Isolation of Rhizosphere Bacteria That Improve Quality and Water Stress RT Tolerance in Greenhouse Ornamentals."; RL Front. Plant Sci. 11:0-0(2020). 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:NUU07513.1}. 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; JABFMV010000011; NUU07513.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7Y5ZGD8; -. DR Proteomes; UP000576379; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR CDD; cd00075; HATPase; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 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; IPR001610; PAC. DR InterPro; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR050736; Sensor_HK_Regulatory. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1. DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF13426; PAS_9; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00086; PAC; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21..37 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 49..68 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 75..92 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..114 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 121..138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 150..169 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 226..274 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT DOMAIN 302..354 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" FT DOMAIN 358..577 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" SQ SEQUENCE 592 AA; 63551 MW; 154BB8FB5AC256FC CRC64; MTIDRWISRI PLDSPSAFMK QLPTLVGFGI VVLIALMPNG VPVTNWPEFV ASIVLVLIAT VLSLAVPWRR FAAEWAVIVP VLSLLAVGLM RLGTGSSASP FVVLTLLPFV WIASEEGRVN ILIAAVGTFI VLLAPLVVDG GGGSPADIVR AFFSPVLYLI VAVVINEIAH RMRVQLRVAR EAVEQQQQLL AQAVTAQDEL VLNEARLKTA NRLIQSIWNA VTEQSVIGTD LDGLIDVWNP GAAKMLGLTE KQVLDGKHHI IDFHDTQEIE QRLEDMDARV TTVSSVDEFS ALVDTVRAGS ADVRDWTYVR PDGKRVAVQV AATPRLDENG HRVGFIFVAT DMTQAREFAR LKDEFVGLIS HELRTPLSSI LGYLELMRDD DEAPLSEEQL QYLGVAERNA HRLLRLVGDL LFTAQVESGR FPLDIRDVEL GSVVSASIES ARPLAANAGV TIVGDLPDGP LQVRGDAVRL GQAVDNLVSN AIKFTPSGGT VTVALRADGE TAVIAVSDTG IGIPAVELSR LSQRFFRAST ATRNAVPGVG LGLTITKAIV TAHGGRLDIA SEEGVGTSIS IVLPVETPEP VTAAIPRVEV AP //