ID   QUIP_PSEAE              Reviewed;         847 AA.
AC   Q9I4U2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   AltName: Full=Quorum signal utilization and inactivation protein;
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=PA1032;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   FUNCTION, INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=16461666; DOI=10.1128/aem.72.2.1190-1197.2006;
RA   Huang J.J., Petersen A., Whiteley M., Leadbetter J.R.;
RT   "Identification of QuiP, the product of gene PA1032, as the second acyl-
RT   homoserine lactone acylase of Pseudomonas aeruginosa PAO1.";
RL   Appl. Environ. Microbiol. 72:1190-1197(2006).
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). Appears to
CC       be the acyl-HSL acylase that underlies the ability of P.aeruginosa to
CC       degrade and utilize certain acyl-HSLs as growth nutrients, including
CC       one of its own quorum signals, 3-oxo-C12-HSL. Is thought to have a role
CC       in quorum quenching. {ECO:0000269|PubMed:16461666}.
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   -!- INDUCTION: By long-chain acyl-HSLs, but not short-chain ones.
CC       {ECO:0000269|PubMed:16461666}.
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; AE004091; AAG04421.1; -; Genomic_DNA.
DR   PIR; F83517; F83517.
DR   RefSeq; NP_249723.1; NC_002516.2.
DR   RefSeq; WP_003112526.1; NZ_QZGE01000006.1.
DR   AlphaFoldDB; Q9I4U2; -.
DR   SMR; Q9I4U2; -.
DR   STRING; 287.DR97_912; -.
DR   MEROPS; S45.003; -.
DR   PaxDb; Q9I4U2; -.
DR   PRIDE; Q9I4U2; -.
DR   EnsemblBacteria; AAG04421; AAG04421; PA1032.
DR   GeneID; 880272; -.
DR   KEGG; pae:PA1032; -.
DR   PATRIC; fig|208964.12.peg.1067; -.
DR   PseudoCAP; PA1032; -.
DR   HOGENOM; CLU_011790_0_1_6; -.
DR   InParanoid; Q9I4U2; -.
DR   OMA; EMDVRRH; -.
DR   PhylomeDB; Q9I4U2; -.
DR   BioCyc; PAER208964:G1FZ6-1054-MON; -.
DR   BRENDA; 3.5.1.97; 5087.
DR   Proteomes; UP000002438; 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; IMP:PseudoCAP.
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   1: Evidence at protein level;
KW   Hydrolase; Periplasm; Quorum sensing; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..847
FT                   /note="Acyl-homoserine lactone acylase QuiP"
FT                   /id="PRO_0000253381"
FT   CHAIN           27..?
FT                   /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT                   /id="PRO_0000253382"
FT   PROPEP          ?..264
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000253383"
FT   CHAIN           265..847
FT                   /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT                   /id="PRO_0000253384"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   847 AA;  94070 MW;  141B2C463E3071C6 CRC64;
     MASPAFMRFL PRCGAAAAFG TLLGLAGCQS WLDDRYADSL PPTSGVQPIK GLAQNVSIRR
     NALGMPLIET GTFHDALFAL GYVHASDRLS QMVSLRLLAQ GRLAEMVGPG ALEIDRFMRT
     VNLRQAAEIQ YRNASPRLQR FFEVYARGVN AYLYRYRDKL PMDLAQSGYR PEYWKPEDSA
     LVFALLNFGL AVNLQEEIAS LTLAQKVGSD KLAWLTPTYP DENLPFDEAE KLKGLRLDGQ
     VPGLAGVEGA ARQVAALSML GVAASNNWAI APQRSRSGKS LMANDTHLPL SMPSVWNYVQ
     IRSPKYQAAG VSIAGLPGVV AGFNGKLAWG MTMVLGDNQD LYLEQLRRQG NRLYYLADGK
     WQPTRERQET FFIKGQRPIR EVIHETRHGP LLNSALGERK NILQPLPLKS GYGLAYRSIQ
     QEADKTLDGF FDLSRAKTIE QAFDATREIR AMPLNIVFAD EKHIGWQVTG RYPNRKEGRG
     LLPSPGWDGR YDWDGYADPI LHPSDQDPQQ GWLGTANHRT VQPGYGAQLS NSWYYPERAE
     RIAQLAGASK SHDTQSMIRM QYDQTSLFVA KLQAMFDNPG MALPLRQAID ALPEAQRSRA
     REAYDRLMAF DGKLTASSSD AALYGAFLHE SARQIFLDEL GPEDGPAWKA FVETANLSYS
     AQADHLLGRD DSPFWDDTRT PQKEDKPAIL ARSLAAAVEF CEQRLGSERK AWQWGKLHTY
     EWQSDSSKMA PYLGAGERAG LGAIKGYLDR GPYPAGGDHT TLDVSAYGWG QDFDTWLIPA
     MRLIVDFGQS EPMIGVNSSG QSGNPASPHY ADGIDAWLKG RYVSFPFQPQ NLDRVYGNKR
     LTLTPAR