ID   PVDQ_PSEF5              Reviewed;         777 AA.
AC   Q4KCM5;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Acyl-homoserine lactone acylase PvdQ;
DE            Short=AHL acylase PvdQ;
DE            Short=Acyl-HSL acylase PvdQ;
DE            EC=3.5.1.97;
DE   Contains:
DE     RecName: Full=Acyl-homoserine lactone acylase PvdQ subunit alpha;
DE              Short=Acyl-HSL acylase PvdQ subunit alpha;
DE   Contains:
DE     RecName: Full=Acyl-homoserine lactone acylase PvdQ subunit beta;
DE              Short=Acyl-HSL acylase PvdQ subunit beta;
DE   Flags: Precursor;
GN   Name=pvdQ; OrderedLocusNames=PFL_2902;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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 11 to 14 carbons in length) (By similarity).
CC       {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:0000250}.
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; CP000076; AAY92174.1; -; Genomic_DNA.
DR   RefSeq; WP_011061191.1; NC_004129.6.
DR   AlphaFoldDB; Q4KCM5; -.
DR   SMR; Q4KCM5; -.
DR   STRING; 220664.PFL_2902; -.
DR   EnsemblBacteria; AAY92174; AAY92174; PFL_2902.
DR   KEGG; pfl:PFL_2902; -.
DR   PATRIC; fig|220664.5.peg.2958; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_017615_0_0_6; -.
DR   OMA; QGIPWVN; -.
DR   OrthoDB; 186419at2; -.
DR   Proteomes; UP000008540; 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; 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   SUPFAM; SSF56235; SSF56235; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Periplasm; Quorum sensing; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..777
FT                   /note="Acyl-homoserine lactone acylase PvdQ"
FT                   /id="PRO_0000253357"
FT   CHAIN           26..?195
FT                   /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT                   /id="PRO_0000253358"
FT   PROPEP          ?196..218
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000253359"
FT   CHAIN           219..777
FT                   /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT                   /id="PRO_0000253360"
FT   ACT_SITE        219
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   777 AA;  84990 MW;  7EFEC9D071448DBA CRC64;
     MIISRQLPSF CLAALFLSFS GGAHALAQPE QTRAEIRRTS FGVPHIRADD ERGLGYGIGY
     AYAQDNLCLM ANEVLTVNAQ RSQYFGAEGQ TLEQRDNLSS DLFFSWLNTP QAVAAFWQAQ
     TPAMRERMQG YVEGYNRQLA ERQVQGLPEQ CRGDWVRPLA TSDLVKLTRR LLVEGGAGQF
     AEALAGATPP GATAQAGLPA EHWQLAAARQ QRFALDRGSN AVAIGSERSF NGRGLLLANP
     HFPWVGGMRF YQMHLTIPGQ LDVMGAALPG LPLINIGFNQ HLAWTHTVDA SKHFTLYRLQ
     LDPKDPTRYL LDGRSLPLER QTLTVQSKGP DGQLQPRTRT LYSSVFGPIV QWPGELDWDH
     QYAYSLRDAN LDNSRVLAQW YAMNQASSVA GLQDSVHQLQ GIPWVNTLAV DDQGRALYMN
     QSVVPNVTQA KLAQCSDPRA GTRVIVLDGS RSACAWDIDP AAAQPGIFAA SQLPQLARND
     YLQHSNDSAW MVNPAAPLQG FSPVISEQDV PLKMRARFAL DRLSRMHKAQ VSDLQHLVTD
     DQVYLAGQVM PDLLQFCEQD LGADAQRLGP VCASLKAWDR SAGLQAGLGF VHFQGIMQPL
     LQDPSVWRVA FDPKDPQHTP RGLAIGRPAV ARALRESMLA SAQQVAEAGL GSDVRWGDIQ
     QVSQGGQPTP VPGGPESLGV YNAIQSVPAA DGKREVVSGT SYLNVVSFDE QGPRALGLLA
     FSLSSDPASA HFRDQTAAFA RNQWSVLPFT EAQIRADGQY QLQVIEEPRK GAVLARQ