ID PVDQ_PSEPK Reviewed; 772 AA.
AC Q88IU8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=PP_2901;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; 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 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; AE015451; AAN68509.1; -; Genomic_DNA.
DR RefSeq; NP_745045.1; NC_002947.4.
DR AlphaFoldDB; Q88IU8; -.
DR SMR; Q88IU8; -.
DR STRING; 160488.PP_2901; -.
DR MEROPS; S45.004; -.
DR PaxDb; 160488-PP_2901; -.
DR KEGG; ppu:PP_2901; -.
DR PATRIC; fig|160488.4.peg.3075; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_6; -.
DR OrthoDB; 9760084at2; -.
DR PhylomeDB; Q88IU8; -.
DR BioCyc; PPUT160488:G1G01-3080-MONOMER; -.
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 CDD; cd01936; Ntn_CA; 1.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Quorum sensing; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..772
FT /note="Acyl-homoserine lactone acylase PvdQ"
FT /id="PRO_0000253365"
FT CHAIN 29..?198
FT /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT /id="PRO_0000253366"
FT PROPEP ?199..220
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253367"
FT CHAIN 221..772
FT /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT /id="PRO_0000253368"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 772 AA; 83333 MW; 88756F5343B43A6D CRC64;
MPVFPFCRPM TCAGLAAALV AFSVGVQAQP APADASAQIR YTRYGVPHIV AKDERGLGYG
VGYAYAQDNL CLLANEVLTV SGERSRYFGA KGQTLEQRDN LASDLFFTWL NSPAAVDAFL
QAQPASVQAL LAGYASGYNR ALVERRRQGL PAECGDGEWV RPISSQDLVK LTRRLLAEGG
VGQFVEALAG AQPPTLARAQ SSAGFASALA RQERFAAERG SNAVAVGAQR SANGRGLLLA
NPHFPWMGGM RFYQMQLTIP GQLDVMGAAL PGLPVVNIGF NQHLAWTHTV DTSKHFTLYR
LQLDPKDPTR YVLDGKSLPM ARQTIRVAVK GTDGSLSQIE RQVYSSQFGP VVQWPGRLDW
DAQAAYSVRD ANLENSRVLQ QWYQINRADS LAALKGSVEQ LQGIPWVNTL AVDQGGRALY
LNQSVVPYVD QQLLDTCSNP QAQGRLVVLD GSRSACQWKV DAQAAQPGIF PARLLPSLER
EDFVQNSNDP AWMANPAQPL TGYSPLVSRN DQPLGMRGRF ALQRLQGKAR LGVDELQRMV
TDEEVYLASL VLPDLLQWCK GASADVQAVC SSLAAWNGKA DLDSGMGLVH FQNLFNALAE
HPESWRVAFN PADPQHTPRG LAVEQAAVSR LVHQAALASL KQVSESGVAG AARWGQVQQA
LDGTPVPGGP QALGVYNAIY SVPHGQGKRL VVSGTSYLQL VSFTDKGPEA RGLLAFSQSS
EKASAHASDQ TKAFAAKQLA LIPFTEAQIK ADPEYREVVI SERDKGAVVS QP
//
