ID A0A0F4IPV6_9ACTN Unreviewed; 517 AA. AC A0A0F4IPV6; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 22-JUL-2015, entry version 2. DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:KJY23503.1}; GN ORFNames=VR43_00140 {ECO:0000313|EMBL:KJY23503.1}; OS Streptomyces sp. NRRL S-104. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1609135 {ECO:0000313|EMBL:KJY23503.1, ECO:0000313|Proteomes:UP000033571}; RN [1] {ECO:0000313|EMBL:KJY23503.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NRRL S-104 {ECO:0000313|EMBL:KJY23503.1}; RA Ju K.-S., Doroghazi J.R., Metcalf W.; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N- CC phospho-L-histidine. {ECO:0000256|SAAS:SAAS00155570}. CC -!- SIMILARITY: Contains histidine kinase domain. CC {ECO:0000256|SAAS:SAAS00102782}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KJY23503.1}. 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; JZWW01000003; KJY23503.1; -; Genomic_DNA. DR RefSeq; WP_037847045.1; NZ_JZWW01000003.1. DR Proteomes; UP000033571; Unassembled WGS sequence. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR InterPro; IPR003661; EnvZ-like_dim/P. DR InterPro; IPR003660; HAMP_linker_domain. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR InterPro; IPR005467; Sig_transdc_His_kinase_core. DR InterPro; IPR009082; Sig_transdc_His_kinase_dimeric. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF47384; SSF47384; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|SAAS:SAAS00250970}; KW Complete proteome {ECO:0000313|Proteomes:UP000033571}; KW Kinase {ECO:0000256|RuleBase:RU003568, ECO:0000256|SAAS:SAAS00102739}; KW Membrane {ECO:0000256|SAAS:SAAS00155543}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00252523}; KW Phosphoprotein {ECO:0000256|RuleBase:RU003568, KW ECO:0000256|SAAS:SAAS00241301}; KW Transferase {ECO:0000256|RuleBase:RU003568, KW ECO:0000256|SAAS:SAAS00102940}; KW Transmembrane {ECO:0000256|RuleBase:RU003568, KW ECO:0000256|SAAS:SAAS00155742}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00155572}; KW Two-component regulatory system {ECO:0000256|SAAS:SAAS00108840}. SQ SEQUENCE 517 AA; 54221 MW; 89FE87834B620E60 CRC64; MAPRGSRRPG GRRPWSLRTR LVVSAVALIA VVGAAIGTVT TLALRSYLVT QLDERLDTSL RMAARVPGGK AARESGTGFA MPPGSPLDAV GIRLDHDGTV VGSARNTRRE GWSPDQVPPA LTEAQTTTLA EAAQEAVQGS SGRAVGAELP GLGTYRVLTS PDRTVVLAFP LSEVDSTVRA LVGVEVCVTL AGLIAASLAG QALVGVALRP LRRVAATATR VSELPLHEGE PALHERVPDA EADPRTEVGQ VGAAINRMLG HVSSALTARQ QSEMRVRQFV ADASHELRTP LASIRGYAEL TRRGREEPGP DTRHALGRIE SEATRMTGLV EDLLLLARLD AGRTPSTGDT DTDLAPLVVD AVSDARAAGP EHHWRLNLPE EPASVRADAA RIQQVLVNLL ANARTHTPPG TTVTAHVSRE TSAVRLRIED DGPGIAPELL PRVFERFARG DASRSRAAGS TGLGLAIVQA VVTAHGGSVN VQSEPGRTRF EVVLPLAGAT AAADPDSQTG HRLSTLG //