LUXQ_VIBVY
ID LUXQ_VIBVY Reviewed; 857 AA.
AC Q7MD16;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Autoinducer 2 sensor kinase/phosphatase LuxQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
GN Name=luxQ; OrderedLocusNames=VVA1220;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
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; BA000038; BAC97246.1; -; Genomic_DNA.
DR RefSeq; WP_011152473.1; NC_005140.1.
DR AlphaFoldDB; Q7MD16; -.
DR SMR; Q7MD16; -.
DR STRING; 672.VV93_v1c41460; -.
DR EnsemblBacteria; BAC97246; BAC97246; BAC97246.
DR KEGG; vvy:VVA1220; -.
DR PATRIC; fig|196600.6.peg.4375; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_74_1_6; -.
DR OMA; IYACTAD; -.
DR OrthoDB; 1755994at2; -.
DR Proteomes; UP000002675; 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; 3.30.450.220; -; 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 Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..857
FT /note="Autoinducer 2 sensor kinase/phosphatase LuxQ"
FT /id="PRO_0000074786"
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; 96743 MW; 9910D1356D5DA94D 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 HTPIEINSTD 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 EVSFKLEQFA RSEHSILSIQ VSDTGIGIDE SKLESIFEPF
VQADSLSTRE YGGSGLGLTI VKNLVEMLEG EISVQSELCK GSTFYLSIPV EKGECEEQKT
PTNPKPEQLF GQGLKVLLVE DNHTNAFILK AFCQKYQMSV EWVQDGTQAL EKLKEHAFDL
ILMDNQLPKM GGIEATREIR ETLKLGTPIY ACTADAQEST KQEFLSAGAN RVIVKPIKEQ
ELHDELLHFK AHYWVEH
