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Database: UniProt
Entry: Q87I43_VIBPA
LinkDB: Q87I43_VIBPA
Original site: Q87I43_VIBPA 
ID   Q87I43_VIBPA            Unreviewed;       524 AA.
AC   Q87I43;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=Putative sensor kinase CitA {ECO:0000313|EMBL:BAC62106.1};
GN   OrderedLocusNames=VPA0763 {ECO:0000313|EMBL:BAC62106.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC62106.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC62106.1, 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).
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DR   EMBL; BA000032; BAC62106.1; -; Genomic_DNA.
DR   RefSeq; NP_800273.1; NC_004605.1.
DR   RefSeq; WP_005481283.1; NC_004605.1.
DR   AlphaFoldDB; Q87I43; -.
DR   GeneID; 1191452; -.
DR   KEGG; vpa:VPA0763; -.
DR   PATRIC; fig|223926.6.peg.3696; -.
DR   eggNOG; COG3290; Bacteria.
DR   HOGENOM; CLU_020211_11_2_6; -.
DR   Proteomes; UP000002493; Chromosome 2.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR032834; NatK_C.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR40448; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR40448:SF1; TWO-COMPONENT SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF14501; HATPase_c_5; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAC62106.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Transferase {ECO:0000313|EMBL:BAC62106.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..523
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   524 AA;  57307 MW;  390198F288F18177 CRC64;
     MPFASFSFTK QLAVLLSGVM LLGMLSWWSY SAHQLDDILT HQISLRAQVQ SQQLSQLSSL
     IAAVGSGSAS KTSEIINAVQ AVSDADFITV SDRAGIRLAH PVAERVGLPV LGGDIERALE
     NGESYLSYGV GSLGPSVRYI SPIFSNEGDV IGMIKVGYLI DTLDLWTSER LLPLISFGII
     AVAICIWLSW KFSRYVRTQM QELEPWQLKQ ALKTHQGVLQ ATYEGLVAIN SEGSLYLIND
     SARAMLNYHQ ELGNVFTDGI DNPESFSLKG DDYINGLIRV NGKNLVMNRV TLRTSTGEPY
     GAVFSLRDQN EMHVLSEKIS QVTQYMENMR VARHEYQNKL STISGLLQMG AYDKALSVCL
     SQAKASQSQL DSLHALNSRP ALSALILAKA SKANELGVAL SIDCQSDLSA LSRRLSEEQL
     CGLIGNLAQN ALEAVKGQEN GHVHIGISES ACEYTIQVSN NGPLLESEFD VLCELGFTTK
     QNKADHGVGM YLVRSIVEQG NGHMELDSDE QETAFTIYFP KELG
//
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