ID B1KRN1_SHEWM Unreviewed; 996 AA. AC B1KRN1; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; DE Flags: Precursor; GN OrderedLocusNames=Swoo_3532 {ECO:0000313|EMBL:ACA87796.1}; OS Shewanella woodyi (strain ATCC 51908 / MS32). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA87796.1, ECO:0000313|Proteomes:UP000002168}; RN [1] {ECO:0000313|EMBL:ACA87796.1, ECO:0000313|Proteomes:UP000002168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella woodyi ATCC 51908."; RL Submitted (FEB-2008) 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; CP000961; ACA87796.1; -; Genomic_DNA. DR RefSeq; WP_012326129.1; NC_010506.1. DR AlphaFoldDB; B1KRN1; -. DR STRING; 392500.Swoo_3532; -. DR KEGG; swd:Swoo_3532; -. DR eggNOG; COG0784; Bacteria. DR eggNOG; COG2205; Bacteria. DR HOGENOM; CLU_000445_40_1_6; -. DR Proteomes; UP000002168; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 1.20.58.920; -; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 6.10.340.10; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 1.20.120.160; HPT domain; 1. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR003660; HAMP_dom. 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; IPR036641; HPT_dom_sf. DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom. DR InterPro; IPR014302; Sig_transdc_His_kinase_TorS. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR InterPro; IPR038188; TorS_sensor_sf. DR NCBIfam; TIGR02956; TMAO_torS; 1. DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1. DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR Pfam; PF01627; Hpt; 1. DR Pfam; PF00072; Response_reg; 1. DR PIRSF; PIRSF036437; HK_TorS; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SMART; SM00448; REC; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACA87796.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE- KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002168}; 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 364..386 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 391..443 FT /note="HAMP" FT /evidence="ECO:0000259|PROSITE:PS50885" FT DOMAIN 507..739 FT /note="Histidine kinase" FT /evidence="ECO:0000259|PROSITE:PS50109" FT DOMAIN 758..879 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT COILED 441..479 FT /evidence="ECO:0000256|SAM:Coils" FT MOD_RES 810 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 996 AA; 109059 MW; 6CA7F153BDEDD729 CRC64; MSALSLSRKS LVGRLMLAFG VLGLLLLLLV SLGNLSLYWV NQADAYLYDK ALPASEAARE LAQASNALAE NAQALGRVEE EHQRQFIGRK LSINSTNMLS AIAKLKTLQV QSDWRLELTA GEIIHDLSQL GKQVGNRLLV ASKLTAQGEA LALAASHSIE LLEAELAVVD SSVLAKLSLA YPEIVGQMKS AELLDTVIEH DIDIQERLNR ALKLIHDIAL IGQLLQSPEQ EKGLLTVLSN MSQQPSVVPP SSYQLQPLQA SMDPNAAGFQ SSIQVDLMAL ELLKGLVRDP VRAKELESEF SVLRQVSEGL TTQKNYVHLI KTQSKQLIML SNKLYELNQT VDHAMAMQQQ EAEGARLDYL QQIAWAKAGL MGTGVLMFIV ILFVVYRVIY KGIAVRLNEA TYALSRLSLG DTQVGINSHG DDELTAMASA IEAFKQKTAH NQKLQLELRE SADELSEHKA ALEIKVEART EELAIANKRL DSEAKGHAQA RTMAEQANQA KSLFLATMSH EIRTPLNGLL GTLTLLGHSN LPVAQKQMLA LSQYSGTLLQ TVLNDILDFS RLEQGKLANE PRPVAINDLL DEVVAIMLAG AGLAGLNLVL DSGKLPEWIN IDGPKLRQVL FNLIGNGIKF TPEGEVRLKV WVEDRALCFM VIDSGVGITD DAKKHLFKAY SAQLNQGRSR GTGLGLAISK ELVELMCQLP EYEAESIAGE LFEEGCKPLW VESEAGVGSR FGFSLPLVIC EQAHEGGQEP QRITNKKRVL VIEDNKVNAM VAQGFLAHLG HESVLADSCA EARNIYCTQS ANSFDAIMLD IQLGDGSGLA LLKELREVTL HASHQLDIAA FTAQIQADDM DHYREIGFDL VLGKPLNMQM LAAWIGVVNP LEEERVANTS PDDKQGELLD IGQIEQDIEY LGRDAVDEML MLYKESSQVQ LSALLQKSEN RNTLLHALKG SSASMGFIAL SKLCKLLETS EYKDGEYQGL QQLHKDSLAA FSQLLG //