ID   CQSS_VIBC1              Reviewed;         681 AA.
AC   A7N6S2; Q693Z6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=CAI-1 autoinducer sensor kinase/phosphatase CqsS;
DE            EC=2.7.13.3;
DE            EC=3.1.3.-;
DE   AltName: Full=Cholerae quorum-sensing sensor;
GN   Name=cqsS; OrderedLocusNames=VIBHAR_06089;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS THE CAI-1 SENSOR.
RX   PubMed=15466044; DOI=10.1128/jb.186.20.6902-6914.2004;
RA   Henke J.M., Bassler B.L.;
RT   "Three parallel quorum-sensing systems regulate gene expression in Vibrio
RT   harveyi.";
RL   J. Bacteriol. 186:6902-6914(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Senses the quorum-sensing autoinducer CAI-1 ((S)-3-
CC       hydroxytridecan-4-one) which probably functions as an intragenus
CC       signal. The sensory signal is then relayed to LuxU and LuxO.
CC       {ECO:0000269|PubMed:15466044}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AY625893; AAT86007.1; -; Genomic_DNA.
DR   EMBL; CP000790; ABU73982.1; -; Genomic_DNA.
DR   RefSeq; WP_012129595.1; NC_022270.1.
DR   AlphaFoldDB; A7N6S2; -.
DR   SMR; A7N6S2; -.
DR   EnsemblBacteria; ABU73982; ABU73982; VIBHAR_06089.
DR   KEGG; vha:VIBHAR_06089; -.
DR   PATRIC; fig|338187.36.peg.4951; -.
DR   OrthoDB; 1755994at2; -.
DR   Proteomes; UP000008152; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Hydrolase; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Protein phosphatase; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..681
FT                   /note="CAI-1 autoinducer sensor kinase/phosphatase CqsS"
FT                   /id="PRO_0000316892"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          187..413
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          564..681
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         190
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         613
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   CONFLICT        484
FT                   /note="A -> R (in Ref. 1; AAT86007)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   681 AA;  77799 MW;  66EFACCF3F3DF932 CRC64;
     MDAIRKVYQY AEPNLSLVGW MGFIGFPIYY IVWEFMFPQP YENLPLRILC SVLFFGIIYR
     NRTPFEWRGF LPAYYQVVTT LCLPCFFFYM LLMNNWSNVW VMSFMSAIFL HILLVHITSV
     MFVQTFVGIG LATFFAWVAQ GFHLELTMDW THVPIFLFIY LFGNLFYFRN QVEHEAKVSI
     AKSFGAGIAH EMRNPLSGLL TSIDVIQSVL PNPKEGKKEQ YTLSDEDVTL LREVSSDAMK
     IIHSGNETID LLLTSIDENR VSRSTFKKHS AQSVVESAIE SFSYKRSTDR FAISLDVRSE
     FDFLGSDTLL KYVMYNLFKN AFHHRSSEDF HIHVTMYSDE FANQIVVTDN GSGIAPEVLQ
     SIFQDFYTTG KSGNYGLGLP FCKKVMRSFG GDIRCQSEVG EWSQFTMTFP TIGSSAVKEI
     KSELTKLKTI LFVSEQNILV SKVTDIARFM RFELTVLDVP AVLKNKEYEF EFDLILIDME
     SLDASGSHID KVESLLSFTE ARIVYMFEHH PIQRARSVSF EPIWVETQAW LLNTRATIDR
     LLYDANYVVP SMPAKPLDST NKRTIMVVDD NESLRKFTAM LLEKQGFEVI QTEDGLQAIN
     ALNENNVDLI LMDIEMPVMD GVEASRQIRG SNKAYASVPI IAHTGDSSPI TLDKIGSSGM
     SDFIVKPADK NRLFDKIANW I