ID   LUXQ_VIBVU              Reviewed;         857 AA.
AC   Q8D5Z6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Autoinducer 2 sensor kinase/phosphatase LuxQ;
DE            EC=2.7.13.3;
DE            EC=3.1.3.-;
GN   Name=luxQ; OrderedLocusNames=VV2_0752;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: At low cell density, in absence of autoinducer has a kinase
CC       activity, and autophosphorylates on a histidine residue. The phosphoryl
CC       group is then transferred to an aspartate residue in the response
CC       regulator domain. The phosphoryl group is transferred to LuxU, and
CC       ultimately to LuxO. At high cell density, in the presence of
CC       autoinducer, the kinase activity is inactivated, and the response
CC       regulator domain has a phosphatase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBUNIT: Binds the complex formed by the autoinducer and LuxP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AE016796; AAO07683.1; -; Genomic_DNA.
DR   RefSeq; WP_011081679.1; NC_004460.2.
DR   AlphaFoldDB; Q8D5Z6; -.
DR   SMR; Q8D5Z6; -.
DR   EnsemblBacteria; AAO07683; AAO07683; VV2_0752.
DR   GeneID; 66967694; -.
DR   KEGG; vvu:VV2_0752; -.
DR   HOGENOM; CLU_000445_74_1_6; -.
DR   OMA; IYACTAD; -.
DR   Proteomes; UP000002275; Chromosome 2.
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; 3.30.450.220; -; 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; IPR015387; LuxQ-periplasm_dom.
DR   InterPro; IPR043056; LuxQ-periplasm_N.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029151; Sensor-like_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; PF00512; HisKA; 1.
DR   Pfam; PF09308; LuxQ-periplasm; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF103190; SSF103190; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..857
FT                   /note="Autoinducer 2 sensor kinase/phosphatase LuxQ"
FT                   /id="PRO_0000074785"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          490..712
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          735..850
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         493
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         784
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   857 AA;  96734 MW;  14ED0BE8C637C7F2 CRC64;
     MTNEQLQRKH QSLATLITRI IFLVLGLITI GIFIQSYYFS NKIIKQEVML TKQQTSALVK
     SLFNNHLSIL QIHHDSNSKN EAIRRFFLDG DDEKLEYYFL SMDQADPTHT PEFRFLTTGE
     GLLWDDGNAH FYGVNEVLLE KISQSVLFGN NWHFMSLHTL MGLRNMLVRR SPVIDTTTGE
     VLGQYYISVV LDNNFPLVEM LESGSNSDNI VMLVGDKVIS HSLSGNEPYD LDSLLAMRDE
     PSAFDDCLIS QTPIEINSTD TLVSILAIQE NSHVASLQRQ HYLGLATSVV LMLMLSLAIR
     SWIQNRVANA LESLMAYSRF AGTGEKYERF NGSDILEFAH IGHTLENTFE QLESQRRSFQ
     DLFNFALSPM MVWSESGLLI QMNPAAMKEL GIEHASPQDF SNPLFQLFKL KLSPHLKMAA
     QGATLTGINV PIGEKIFRWN LSPIVVENGI SGIIVQGQDI TTLIDAEKQS NLARREAEQS
     AKTRADFLAK MSHEIRTPLN GILGIAQLLK RSVNDAENLK QVDVLCNSGE HLLAVLNDIL
     DFSKIEQGKF NIKKRDFNFY DTLNTLENIY RPICREKGVS FEIHNQIPLD CQLHTDQVRL
     NQIMFNLISN AVKFTPAGRI EVSFKLEKFA RSEHSILSIQ VSDTGIGIDE SKLESIFEPF
     VQADSLSTRE YGGSGLGLTI VKNLVEMLEG EISVQSELCK GSTFYLSIPV EKGECEEQKT
     PTNPKPEQLF GQGLKVLLVE DNHTNAFILK AFCQKYQMSV EWVQDGTQAL EKLKEHAFDL
     ILMDNQLPKM GGIEATREIR ETLKLGTPIY ACTADAQEST KQEFLSAGAN RVIVKPIKEQ
     ELHDELLHFK AHYWVEH