QUIP_PSEPF
ID QUIP_PSEPF Reviewed; 816 AA.
AC Q3KH00;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-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=Pfl01_1213;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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; CP000094; ABA72956.1; -; Genomic_DNA.
DR RefSeq; WP_011332772.1; NC_007492.2.
DR AlphaFoldDB; Q3KH00; -.
DR SMR; Q3KH00; -.
DR STRING; 205922.Pfl01_1213; -.
DR MEROPS; S45.003; -.
DR PRIDE; Q3KH00; -.
DR EnsemblBacteria; ABA72956; ABA72956; Pfl01_1213.
DR KEGG; pfo:Pfl01_1213; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_6; -.
DR OMA; EMDVRRH; -.
DR Proteomes; UP000002704; 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; Signal; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..816
FT /note="Acyl-homoserine lactone acylase QuiP"
FT /id="PRO_0000253389"
FT CHAIN 34..?
FT /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT /id="PRO_0000253390"
FT PROPEP ?..261
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253391"
FT CHAIN 262..816
FT /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT /id="PRO_0000253392"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 816 AA; 89025 MW; B3FCCBBACE0D7965 CRC64;
MASPALSHFL PRFGVAAAVA GVLSLTGCQT WNAQDTLPPT SGVQPLKGLA QNVSVRRNAM
GMPLIESNSF HDALFALGYV HASDRINQMV TLRLLAQGRL AEMSGSSMLD ADRYMRAVNL
KKSAGELYKA SSPRLKRFFE VYARGVNAYL FRYADKLPGD LASSGYKPEY WKPEDSALIF
CLLNFSQSAN LPEEIASLVL AQTVTNDKLA WLTPSAPDEN LPLAEADKLQ GIKLNGQIPG
LTELSNASEQ LAALNLLGTQ SSNNWAIAPQ RSRSGKSLLA SDSHGPLAAP SLWSFVQIRA
PKYQAAGVTV AGLPMVLGGF NGKVAWSLTS VLGDNQDLFL EKIRRQGSSL TYEVNGKWQP
VAVRNETYFV KGQRPIREAV YETRHGALLN STQAAAQGTG FGLALQTPSF TDDKSLDAFF
DLSRAQNVER ASDATREIRA IALNLVFADA SNIGWQVTGR FPNRREGEGL LPSPGWEGRY
DWDGYADPML HPYDQDPAQG WLGTANQRVI PHGYGMQLSN SWAAPERGER LAELAGSGKH
DSRSVIAMQY DQTTTFAAKL KKMFEAPGMA QPLKQAIDAL PEAERSKARE AYTRLMAFDG
KLSPTSADAA IYELFLQESM KQIFLDELGP QNSPAWKAFI ANGDLSYAAQ ADHLLGREDS
PFWDDARTPQ KEDKPAILAR SLAAAISAGD SQLGGDRRAW QWGKLHRYEW KNANGQSVRG
PIAAGGDHTT LNTAAFAWGQ DFNTTRAPSM RFIVDFGQSE PLMGQNGTGQ SGNPVSPNYL
NGIDPWLKGQ YIGLPMQPQN FDRVYGKTRL TLTPGK
