LUXQ_VIBHA
ID LUXQ_VIBHA Reviewed; 859 AA.
AC P54302;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Autoinducer 2 sensor kinase/phosphatase LuxQ;
DE EC=2.7.13.3;
DE EC=3.1.3.-;
GN Name=luxQ;
OS Vibrio harveyi (Beneckea harveyi).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB7;
RX PubMed=7984107; DOI=10.1111/j.1365-2958.1994.tb00422.x;
RA Bassler B.L., Wright M., Silverman M.R.;
RT "Multiple signalling systems controlling expression of luminescence in
RT Vibrio harveyi: sequence and function of genes encoding a second sensory
RT pathway.";
RL Mol. Microbiol. 13:273-286(1994).
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.
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.
CC -!- INTERACTION:
CC P54302; P54300: luxP; NbExp=5; IntAct=EBI-1101486, EBI-1101482;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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DR EMBL; U07069; AAA20838.1; -; Genomic_DNA.
DR PIR; S49046; S49046.
DR PDB; 1ZHH; X-ray; 1.94 A; B=39-278.
DR PDB; 2HJ9; X-ray; 2.34 A; C/D=53-271.
DR PDB; 2HJE; X-ray; 1.70 A; A=53-271.
DR PDBsum; 1ZHH; -.
DR PDBsum; 2HJ9; -.
DR PDBsum; 2HJE; -.
DR AlphaFoldDB; P54302; -.
DR SMR; P54302; -.
DR IntAct; P54302; 1.
DR STRING; 669.AL538_22575; -.
DR BRENDA; 2.7.13.3; 6632.
DR EvolutionaryTrace; P54302; -.
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; 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 Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..859
FT /note="Autoinducer 2 sensor kinase/phosphatase LuxQ"
FT /id="PRO_0000074783"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 489..711
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 736..851
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 492
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 785
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT HELIX 53..78
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 163..175
FT /evidence="ECO:0007829|PDB:2HJE"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2HJE"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:2HJE"
FT STRAND 260..270
FT /evidence="ECO:0007829|PDB:2HJE"
SQ SEQUENCE 859 AA; 96915 MW; AB2171F454C81060 CRC64;
MTTTRSNIKK RRSLATLITK IIILVLAPII LGIFIQSYYF SKQIIWQEVD RTKQQTSALI
HNIFDSHFAA IQIHHDSNSK SEVIRDFYTD RDTDVLNFFF LSIDQSDPSH TPEFRFLTDH
KGIIWDDGNA HFYGVNDLIL DSLANRVSFS NNWYYINVMT SIGSRHMLVR RVPILDPSTG
EVLGFSFNAV VLDNNFALME KLKSESNVDN VVLVANSVPL ANSLIGDEPY NVADVLQRKS
SDKRLDKLLV IETPIVVNAV TTELCLLTVQ DNQSVVTLQI QHILAMLASI IGMIMIALMS
REWIESKVSA QLESLMSYTR SAREEKGFER FGGSDIEEFD HIGSTLESTF EELEAQKKSF
RDLFNFALSP IMVWSEESVL IQMNPAARKE LVIEDDHEIM HPVFQGFKEK LTPHLKMAAQ
GATLTGVNVP IGNKIYRWNL SPIRVDGDIS GIIVQGQDIT TLIEAEKQSN IARREAEKSA
QARADFLAKM SHEIRTPING ILGVAQLLKD SVDTQEQKNQ IDVLCHSGEH LLAVLNDILD
FSKIEQGKFN IQKHPFSFTD TMRTLENIYR PICTNKGVEL VIENELDPNV EIFTDQVRLN
QILFNLVSNA VKFTPIGSIR LHAELEQFYG AENSVLVVEL TDTGIGIESD KLDQMFEPFV
QEESTTTREY GGSGLGLTIV KNLVDMLEGD VQVRSSKGGG TTFVITLPVK DRERVLRPLE
VSQRIKPEAL FDESLKVLLV EDNHTNAFIL QAFCKKYKMQ VDWAKDGLDA MELLSDTTYD
LILMDNQLPH LGGIETTHEI RQNLRLGTPI YACTADTAKE TSDAFMAAGA NYVMLKPIKE
NALHEAFVDF KQRFLVERT
