PVDQ_PSEPF
ID PVDQ_PSEPF Reviewed; 778 AA.
AC Q3KD51;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=Pfl01_2563;
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 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; CP000094; ABA74304.1; -; Genomic_DNA.
DR RefSeq; WP_011333981.1; NC_007492.2.
DR AlphaFoldDB; Q3KD51; -.
DR SMR; Q3KD51; -.
DR STRING; 205922.Pfl01_2563; -.
DR MEROPS; S45.004; -.
DR EnsemblBacteria; ABA74304; ABA74304; Pfl01_2563.
DR KEGG; pfo:Pfl01_2563; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_6; -.
DR OMA; QGIPWVN; -.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..778
FT /note="Acyl-homoserine lactone acylase PvdQ"
FT /id="PRO_0000253361"
FT CHAIN 26..?195
FT /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT /id="PRO_0000253362"
FT PROPEP ?196..218
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253363"
FT CHAIN 219..778
FT /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT /id="PRO_0000253364"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 85671 MW; 4DBA6D2667321242 CRC64;
MTISRQFTGL TLAGLFLGLS LSAQAFSPSV QTGADIRRTG FGVPHIRAEN ERGLGFGIGY
AYAQDNLCLL ANEIVTVNGE RSRYFGPEQL TVEERENRIS DVFFQWLNTP QAVNAFWQAQ
PAEVRDLVEG YAAGYNRYLA ERRQQGLPQQ CQGEWVRDIA AEDLVKLTRR LLVEGGVGQF
AEALASATPP QAMANIENNA RAYQLADTRL QRFALDRGSN AVAVGSERSF NGRGMLLANP
HFPWVGGMRF YQMHLTIPGK LDVMGAALPG LPMINIGFNQ HLAWTHTVDS SKHFTLYRLQ
LDPKDPTRYL LDGQSLPLSK QTVTVQVKQT DGQVVPVSRD VYSSQFGPIV QWPGKLDWNN
QFAYSLRDAN LDNDRVLKQW YAMNRAGNLK DLQDSVHTIQ GIPWVNTLAV DDKGQTLYMN
LSVVPNVSTD KLARCSDPRA GLKMIVLDGS NSACAWDIDP HAAQKGIYAS SQLPQLLRKD
FVQHSNDSAW LANPAQPLTG FSPLISQDGQ PLGLRSRFAL DRLATLSKKG LVSVQDLQHM
VMDDQVFLAT QVVPDLLKFC TSQSEAALKS VCSSLKAWDG RANLESGVGL VHFQSIMQAM
QESPQAWRVA FDPKDAQHTP RGLAIEKPEV AKALREAMLA SAEIAAKMGL TEKTRWGDVQ
VVSSGGQQTP IHGGPGTLGI YNAIQSVPRE DGKLEVVSGT SYLQVVTFDD KGPHAQGLLA
FSLSSDPASK YSRDQTEAFS KKQWSVLPFT EQQIKADPQY QVQTVRDDLE KTGKVAAQ
