QUIP_PSEPK
ID QUIP_PSEPK Reviewed; 813 AA.
AC Q88NU6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Acyl-homoserine lactone acylase QuiP;
DE Short=AHL acylase QuiP;
DE Short=Acyl-HSL acylase QuiP;
DE EC=3.5.1.97;
DE Contains:
DE RecName: Full=Acyl-homoserine lactone acylase QuiP subunit alpha;
DE Short=Acyl-HSL acylase QuiP subunit alpha;
DE Contains:
DE RecName: Full=Acyl-homoserine lactone acylase QuiP subunit beta;
DE Short=Acyl-HSL acylase QuiP subunit beta;
DE Flags: Precursor;
GN Name=quiP; OrderedLocusNames=PP_1108;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Catalyzes the deacylation of acyl-homoserine lactone (AHL or
CC acyl-HSL), releasing homoserine lactone (HSL) and the corresponding
CC fatty acid. Possesses a specificity for the degradation of long-chain
CC acyl-HSLs (side chains of seven or more carbons in length) (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-homoserine lactone + H2O = a carboxylate + L-
CC homoserine lactone; Xref=Rhea:RHEA:18937, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:55474, ChEBI:CHEBI:58633; EC=3.5.1.97;
CC -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC from the same precursor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: AHL-mediated signaling mediates quorum sensing in many
CC species of Proteobacteria, regulating hundreds of genes, including many
CC that code for extracellular virulence factors.
CC -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR EMBL; AE015451; AAN66733.1; -; Genomic_DNA.
DR RefSeq; NP_743269.1; NC_002947.4.
DR RefSeq; WP_010952271.1; NC_002947.4.
DR AlphaFoldDB; Q88NU6; -.
DR SMR; Q88NU6; -.
DR STRING; 160488.PP_1108; -.
DR MEROPS; S45.003; -.
DR EnsemblBacteria; AAN66733; AAN66733; PP_1108.
DR KEGG; ppu:PP_1108; -.
DR PATRIC; fig|160488.4.peg.1173; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_6; -.
DR OMA; EMDVRRH; -.
DR PhylomeDB; Q88NU6; -.
DR BioCyc; PPUT160488:G1G01-1181-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 1.10.439.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR043147; Penicillin_amidase_A-knob.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218; PTHR34218; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Quorum sensing; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..813
FT /note="Acyl-homoserine lactone acylase QuiP"
FT /id="PRO_0000253393"
FT CHAIN 27..?
FT /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT /id="PRO_0000253394"
FT PROPEP ?..261
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253395"
FT CHAIN 262..813
FT /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT /id="PRO_0000253396"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 813 AA; 88729 MW; E0BC1403A9F2AF6B CRC64;
MAAPAFPPFR LRFATAATLL GMLGLAGCQT GGYQDSVPPT SGVQPLKGLA QNVSVRRNAM
GAPLIESSSF HDALFSLGYV HAGDRIEQMV AMRLLAQGRL AELAGSEALD IDRLMRAANL
KQSAAQQYAD ASPRLKRFFE VYARGVNAYL FRYRDKLPAG LASSGYRPEY WKPEDSALIF
CLYAFSQSVN LQEELSALTL AQKAGSDKLA WLLPGAPDEP LAEMEVDKLK GLNLASQLPG
LPALAAASQK LADLDLLGSP GSANLALGPQ RSRSGKSLLA SDSRAAWALS PVQINTSKYQ
VAGLSLPGLP IVLAGYNGKL AWSSSAVMAD NQDLFLEQLR RQGSQLSYLA DGKWLPARAR
SETYFVRGQR PVREVMYDTR HGTLLAQPEN ASLGLALNLP QFKGDRSLDA LFDLTRAKNV
ERAFDSTREV TAAAVNFVFA EPEHIGWQVS GRYPNRREGQ GLLPSPGWDG RYDWDGYADP
MLHPYDQDPP AGWIGHANQR SLPRGYGMQL SSTWYYPERA ERLAQLAGNG RHDSRSLMAL
QNDQVTLLAN KLKQMFDAPG MAQPLKQAID ALPAGQRDKA RDTLARLKAF DGRLSPVSAD
AALYELFLQE VARQTFLDDL GPESGPAWQA FVGNARLSFS AQADHLLGRD DSPFWDDRNT
PQKEDKPAIL ARSLAGAMEA GIAQLGADRR TWQWGKLHQY RWPAPAYHGL GDAISRSPLA
AGGDFTTLAL TPFAWGSDFD THLPASARMI VDFGQAEPLQ ILTSSGQSGN PASAHYRDGL
DAWFKGRFMS LPLQQQNFGR AYGNQRLTLV PGR
