LUXQ_VIBCH
ID LUXQ_VIBCH Reviewed; 857 AA.
AC Q9KLK7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Autoinducer 2 sensor kinase/phosphatase LuxQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
GN Name=luxQ; OrderedLocusNames=VC_A0736;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION.
RC STRAIN=El Tor C6706;
RX PubMed=12176318; DOI=10.1016/s0092-8674(02)00829-2;
RA Miller M.B., Skorupski K., Lenz D.H., Taylor R.K., Bassler B.L.;
RT "Parallel quorum sensing systems converge to regulate virulence in Vibrio
RT cholerae.";
RL Cell 110:303-314(2002).
RN [3]
RP AUTOINDUCER 2 (AI-2) SYNTHESIS IN V.CHOLERAE.
RX PubMed=9190823; DOI=10.1128/jb.179.12.4043-4045.1997;
RA Bassler B.L., Greenberg E.P., Stevens A.M.;
RT "Cross-species induction of luminescence in the quorum-sensing bacterium
RT Vibrio harveyi.";
RL J. Bacteriol. 179:4043-4045(1997).
CC -!- FUNCTION: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ
CC has a kinase activity and autophosphorylates on a histidine residue.
CC The phosphoryl group is then transferred to an aspartate residue in the
CC response regulator domain. The phosphoryl group is transferred to LuxU,
CC and ultimately to LuxO. At high cell density, in the presence of AI-2,
CC the kinase activity is inactivated, and the response regulator domain
CC has a phosphatase activity (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12176318}.
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 AI-2 and LuxP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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DR EMBL; AE003853; AAF96635.1; -; Genomic_DNA.
DR PIR; C82424; C82424.
DR RefSeq; NP_233123.1; NC_002506.1.
DR RefSeq; WP_001026306.1; NZ_LT906615.1.
DR PDB; 3C30; X-ray; 2.80 A; A=36-280.
DR PDB; 3C38; X-ray; 2.30 A; A=36-280.
DR PDBsum; 3C30; -.
DR PDBsum; 3C38; -.
DR AlphaFoldDB; Q9KLK7; -.
DR SMR; Q9KLK7; -.
DR STRING; 243277.VC_A0736; -.
DR PRIDE; Q9KLK7; -.
DR DNASU; 2611934; -.
DR EnsemblBacteria; AAF96635; AAF96635; VC_A0736.
DR KEGG; vch:VC_A0736; -.
DR PATRIC; fig|243277.26.peg.3359; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_74_0_6; -.
DR OMA; IYACTAD; -.
DR BioCyc; VCHO:VCA0736-MON; -.
DR EvolutionaryTrace; Q9KLK7; -.
DR Proteomes; UP000000584; 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; IBA:GO_Central.
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; 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; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Hydrolase;
KW Kinase; 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_0000074782"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 486..706
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 731..846
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 489
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 780
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT HELIX 53..78
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3C38"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3C38"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:3C38"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:3C38"
SQ SEQUENCE 857 AA; 96930 MW; 248000A038DA5A51 CRC64;
MNIRPSQIKH KQRIASFITH AVVVVMGVLI VSVLFQSYQI SSRLMAQEGQ RTSVQTSSLI
QSLFDFRLAA LRIHQDSTAK NASLINALVS RDSSRLDEFF SSVDELELSN APDLRFISSH
DNILWDDGNA SFYGIAQQEL NKLIRRVAIS GNWHLVQTPS EGKSVHILMR RSSLIEAGTG
QVVGYLYVGI VLNDNFALLE NIRSGSNSEN LVLAVDTTPL VSTLKGNEPY SLDYVVHSAK
DAMRDSFIVG QTFLEVESVP TYLCVYSIQT NQNVLTLRDN FYFWMAFALI SMIGVSIASR
WWLQKRIQRE IETLMNYTHK LMDLDTKSEF IGSKIYEFDY FGRTLEQSFR RLANKEKQFE
DLFNFALSPT MLWNTSGRLI RMNPSAQIQF LREDAQNHFL FEILERQLLP TITNAAQGNN
PSDVTTEVDG RVYRWNLSPI MVEGQIISII TQGQDITTIA EAEKQSQAAR REAEESARVR
AEFLAKMSHE LRTPLNGVLG VSQLLKRTPL NDEQREHVAV LCSSGEHLLA VLNDILDFSR
LEQGKFRIQK NEFRLKELVC AIDRIYRPLC NEKGLELVVN SNITTAAIVR SDQIRINQIL
FNLLNNAIKF THQGSIRVEL QLIEGDPLAQ LVIQVVDTGI GIREQDLTVI FEPFMQAEST
TTREYGGSGL GLTIVHSLVE MLSGQLHVSS EYGIGTRFEI QLPIELVEKP DAPQQLLPAP
DPQPLFDKTL RVLLVEDNHT NAFIAQAFCR KYGLDVSWVT DGLQAIEELK IHDYDLVLMD
NQLPYLDGVE TTRTIKKVLH LPVVVYACTA DGLEETRQAF FHAGAEYVLV KPLKEQTLHK
ALEHFKHHHG QKNAGLN
