PVDQ_PSEU2
ID PVDQ_PSEU2 Reviewed; 779 AA.
AC Q4ZV08;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Psyr_1971;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000075; AAY37014.1; -; Genomic_DNA.
DR RefSeq; WP_011267358.1; NC_007005.1.
DR RefSeq; YP_235052.1; NC_007005.1.
DR AlphaFoldDB; Q4ZV08; -.
DR SMR; Q4ZV08; -.
DR STRING; 205918.Psyr_1971; -.
DR MEROPS; S45.004; -.
DR EnsemblBacteria; AAY37014; AAY37014; Psyr_1971.
DR KEGG; psb:Psyr_1971; -.
DR PATRIC; fig|205918.7.peg.2013; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_6; -.
DR OMA; QGIPWVN; -.
DR BRENDA; 3.5.1.97; 5193.
DR Proteomes; UP000000426; 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; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..779
FT /note="Acyl-homoserine lactone acylase PvdQ"
FT /id="PRO_0000253373"
FT CHAIN 26..?201
FT /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT /id="PRO_0000253374"
FT PROPEP ?202..223
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253375"
FT CHAIN 224..779
FT /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT /id="PRO_0000253376"
FT REGION 731..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 779 AA; 84673 MW; 7DCDEFC186736830 CRC64;
MIISRPLCSF VFAGLSFAVI LPAQALVEPG NQAARAEIRR TGFGVPHIVA ANERGLGYGI
GYAYAQDNLC LLANEVVTVN GQRSRYFGPD KATLEQRNNM ASDLLFQWLN TPQALADFWN
AQPREIRQLM QGYVAGYNRS LAEQTTQGLP QPCAAEWVRP ISTDDLLRLT RRLLVEGGVG
QFAEALAGAT PPAQQKPLQV DAQQAQALQL AAARNQRFAL ERGSNAVAIG RELSANGRGM
LLANPHFPWG GGMRFYQMHL TIPGKLDVMG AALPGLPLIN IGFNQHLAWS HTVDTSKHFT
LHRLQLDPKD STRYLLDGQS VAMGKQQVSV DVKQADGSLK SVPRIVYSSI FGPVVQWPGK
LDWDSKFAFS LRDANLQNDR VLQQWYAMDK ADSLKAFQDS VRKIQGIPWV NTLAVDAQGQ
ALYMNLSVVP NVDAARLARC SDPRIGTELI VLDGSRSECN WEVSAEAAQA GIYPSSRQPQ
LLRTDFVQHS NDSAWMVNPA APLQGFSPLI SQDGQPLGQR ARFALDRLES LKTAGKISVE
NLQAMVMDNE VYQAGQVLPD LLTFCASELG DDAARLAPLC AALKDWDGRA DLNSGIGFVY
FQKIMTSMQA VASRWRVAFD PQDPVHTPSG LAIENPSVAT ALRAAMLAAV DDVAKAGLPA
GSKWGDIQVS SISGKQIPIH GGPAGLGVYN AMQTVAGKDG KREVVSGTSY LQVVTFDEQG
PKAQGLLAFS ESSNPQSAHS SDQTEAFSKK QWQALPFTEQ QIKADPAYEV QVISEEPDR