LUXP_VIBHA
ID LUXP_VIBHA Reviewed; 365 AA.
AC P54300;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Autoinducer 2-binding periplasmic protein LuxP;
DE Flags: Precursor;
GN Name=luxP;
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;
RA Schauder S., Bassler B.L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-365.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 24-365, AND FUNCTION.
RX PubMed=11823863; DOI=10.1038/415545a;
RA Chen X., Schauder S., Potier N., van Dorsselaer A., Pelczer I.,
RA Bassler B.L., Hughson F.M.;
RT "Structural identification of a bacterial quorum-sensing signal containing
RT boron.";
RL Nature 415:545-549(2002).
CC -!- FUNCTION: Binds to the signaling molecule autoinducer 2 (AI-2), a
CC furanosyl borate diester, (3a-methyl-5,6-dihydrofuro-
CC [2,3d][1,3,2]dioxaborole-2,2,6,6a-tetraol). This complex then interacts
CC with the LuxQ sensor protein. {ECO:0000269|PubMed:11823863}.
CC -!- INTERACTION:
CC P54300; P54302: luxQ; NbExp=5; IntAct=EBI-1101482, EBI-1101486;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {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; U07069; AAA20837.2; -; Genomic_DNA.
DR PIR; S49045; S49045.
DR PDB; 1JX6; X-ray; 1.50 A; A=24-365.
DR PDB; 1ZHH; X-ray; 1.94 A; A=22-365.
DR PDB; 2HJ9; X-ray; 2.34 A; A/B=27-365.
DR PDB; 4YP9; X-ray; 2.70 A; A/B=24-365.
DR PDB; 4YR7; X-ray; 2.53 A; A/B=24-365.
DR PDB; 4YRZ; X-ray; 2.57 A; A/B=24-365.
DR PDBsum; 1JX6; -.
DR PDBsum; 1ZHH; -.
DR PDBsum; 2HJ9; -.
DR PDBsum; 4YP9; -.
DR PDBsum; 4YR7; -.
DR PDBsum; 4YRZ; -.
DR AlphaFoldDB; P54300; -.
DR SMR; P54300; -.
DR IntAct; P54300; 1.
DR STRING; 669.AL538_22570; -.
DR BindingDB; P54300; -.
DR ChEMBL; CHEMBL6100; -.
DR EvolutionaryTrace; P54300; -.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Signal.
FT SIGNAL 1..23
FT CHAIN 24..365
FT /note="Autoinducer 2-binding periplasmic protein LuxP"
FT /id="PRO_0000031726"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4YP9"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4YP9"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4YP9"
FT HELIX 210..227
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 241..254
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1JX6"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:1JX6"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:1JX6"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:1JX6"
SQ SEQUENCE 365 AA; 41458 MW; EB2A19FB91E21E54 CRC64;
MKKALLFSLI SMVGFSPASQ ATQVLNGYWG YQEFLDEFPE QRNLTNALSE AVRAQPVPLS
KPTQRPIKIS VVYPGQQVSD YWVRNIASFE KRLYKLNINY QLNQVFTRPN ADIKQQSLSL
MEALKSKSDY LIFTLDTTRH RKFVEHVLDS TNTKLILQNI TTPVREWDKH QPFLYVGFDH
AEGSRELATE FGKFFPKHTY YSVLYFSEGY ISDVRGDTFI HQVNRDNNFE LQSAYYTKAT
KQSGYDAAKA SLAKHPDVDF IYACSTDVAL GAVDALAELG REDIMINGWG GGSAELDAIQ
KGDLDITVMR MNDDTGIAMA EAIKWDLEDK PVPTVYSGDF EIVTKADSPE RIEALKKRAF
RYSDN
