ID Q87QA5_VIBPA Unreviewed; 646 AA.
AC Q87QA5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=VP1245 {ECO:0000313|EMBL:BAC59508.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59508.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC59508.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; BA000031; BAC59508.1; -; Genomic_DNA.
DR RefSeq; NP_797624.1; NC_004603.1.
DR RefSeq; WP_005489098.1; NC_004603.1.
DR AlphaFoldDB; Q87QA5; -.
DR GeneID; 1188750; -.
DR KEGG; vpa:VP1245; -.
DR PATRIC; fig|223926.6.peg.1184; -.
DR eggNOG; COG0664; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_81_6; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
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; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 5..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 202..303
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 472..641
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 308..335
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 646 AA; 72657 MW; 657187E48209898D CRC64;
MNRYAVLCLD NNPISAEQFR LELSAFSSKF DIFSVESIEE AQSALEYLEE REQTVALVIA
SHHAHFNGVD FLIGLDKTPH TERARKILIS CSSDIDAILT AVNEGRLDHC LTKPLPDNVL
FNTAQKELTQ FILRNCKEDL LSYSQILDQH KLLRAHIENQ MSNYQAGFLH DYHSMSDNEL
AEQVISALQQ FFKENDETKA CRTYSPEHLL TVEGEPNSFL WFITSGEVAL YKRDEQGMQR
EVVRHTKGNI VGGMSFVTGE CSFSTALTLT ETEVIKLDRN VFRKVMQSDS NLLPLFTNLL
LRHFNRRLQR SINTKLQLQK TLESLESAHQ QLIEREKMAM LGQLVAGVAH ELNNPIAAIL
RGVENLTHTL EGLLTQLPTA EVQIKGVQLL TRAQTAKPAS TAELRSRVKE LNSTLPDRTI
AKKVVNLGLE SDSELVSQLA KKKDNASSTL ETLEQYHQAG ASLRSINVCA ARIADMVKSL
KGYARSDDER MHYADIHEGI EDTLVIFENK LKVHQVSTDY APLPRMLCQP IALQQVWTNL
ISNAIDAFPD KGSLKIQTRE VEKNQQRYAV ISFEDNGCGI PDSQKKAIFE LNFTTKKEGN
FGLGIGLSIC QQIVAAHKGW IDVQSELNAF TCMTVWLPVI EEGDET
//
