ID A0A086WJ60_9VIBR Unreviewed; 628 AA. AC A0A086WJ60; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 07-OCT-2020, entry version 26. DE RecName: Full=Histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN ORFNames=IX95_22190 {ECO:0000313|EMBL:KFI09810.1}; OS Vibrio sp. B183. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=1526762 {ECO:0000313|EMBL:KFI09810.1, ECO:0000313|Proteomes:UP000029061}; RN [1] {ECO:0000313|EMBL:KFI09810.1, ECO:0000313|Proteomes:UP000029061} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B183 {ECO:0000313|EMBL:KFI09810.1, RC ECO:0000313|Proteomes:UP000029061}; RA Schreier H.J., Schott E.J.; RT "Draft Genome Sequence of the Shellfish Bacterial Pathogen Vibrio sp. RT B183."; RL Submitted (JUL-2014) 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:KFI09810.1}. 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; JPQB01000025; KFI09810.1; -; Genomic_DNA. DR RefSeq; WP_038163989.1; NZ_JPQB01000025.1. DR EnsemblBacteria; KFI09810; KFI09810; IX95_22190. DR Proteomes; UP000029061; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR CDD; cd01949; GGDEF; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 3.30.70.270; -; 1. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013767; PAS_fold. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR029151; Sensor-like_sf. DR Pfam; PF00990; GGDEF; 1. DR Pfam; PF00989; PAS; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF103190; SSF103190; 2. DR SUPFAM; SSF55073; SSF55073; 1. DR SUPFAM; SSF55785; SSF55785; 1. DR TIGRFAMs; TIGR00254; GGDEF; 1. DR TIGRFAMs; TIGR00229; sensory_box; 1. DR PROSITE; PS50887; GGDEF; 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 339..410 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT DOMAIN 412..465 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" FT DOMAIN 499..623 FT /note="GGDEF" FT /evidence="ECO:0000259|PROSITE:PS50887" FT COILED 561..581 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 628 AA; 72458 MW; AA29B0A944F02388 CRC64; MRQRKNIFWH LCITTVVLVS IAFAYYAQQY QNLEEETVES TAKQAMHQLA YSEREYQSVR SQLVSIIELL SHSRSLYDYI LSPSAENREV VEEVWSSMAI NQKWYSQIRF IDNAGKEQLR LNYLLSGNRV QMAEQLQDKS HRGYFRYAKL LRDEQIGAWG IDLEMENGEL VFPYKPALRL ITPVEVQGQR AGYLILNIDI WYLTSCLNYS PDKSFRPELV GETGFYMISD DPSKLFGHLL ASRSQHNLAR YYPETWQIMQ DQKSGYHLEK DHLIVFNQIY MEGRQKLYLV IDLSQEELKV RSERDYQILL KEASIVLLMV LAFTVPATSG VVYYRKRSLE SQLARAALSG MSAVVISDKK HQAVLVNDEF ERLTGYRQKD IASQNMIKAL VGEEQFATTL QLFEALSSNQ IWEGEITIHN QKTHTKVTAI MRVQCVLAKG RKVSYYITSL VDISERKELE ERLRILSEKD ELTQLWNRRK FELELRYSAK LSGRYPERHD TCLALLDIDF FKRVNDELGH DEGDRVISRV GAIITEALRE TDFIARIGGE EFAIIMPHTS IEEAEQALNR VRIAVEMAAD VPITVSVGLT DLTSNSTRCY KCADIALYES KTLGRNRVSV CQSCDEIA //