PVDQ_PSE14
ID PVDQ_PSE14 Reviewed; 779 AA.
AC Q48KB0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-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=PSPPH_1937;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(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; CP000058; AAZ35979.1; -; Genomic_DNA.
DR RefSeq; WP_011168299.1; NC_005773.3.
DR AlphaFoldDB; Q48KB0; -.
DR SMR; Q48KB0; -.
DR STRING; 264730.PSPPH_1937; -.
DR MEROPS; S45.004; -.
DR EnsemblBacteria; AAZ35979; AAZ35979; PSPPH_1937.
DR KEGG; psp:PSPPH_1937; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_6; -.
DR OMA; QGIPWVN; -.
DR OrthoDB; 186419at2; -.
DR Proteomes; UP000000551; 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_0000253369"
FT CHAIN 26..?201
FT /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT /id="PRO_0000253370"
FT PROPEP ?202..223
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253371"
FT CHAIN 224..779
FT /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT /id="PRO_0000253372"
FT REGION 731..752
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; 84927 MW; A9E0655350C4229C CRC64;
MIISRPLCGF VFAGLSFAVI LPAQALVAAD NQAARAEIRR TGFGVPHIVA ANERGLGYGI
GYAYAQDNLC LLANEVVTVN GERSRYFGPD KATLEQRSNM ASDLLFKWLN TPEALADFWK
AQPPEIRQLM QGYVAGYNRS LDEQKTKGLP RPCAADWVRP ISTDDLLRLT RRLLVEGGVG
QFTEAFAGAK PPSAQKPLQV DSQQVQALQL AAVRNQRFAL ERGSNAVAVG HELSANGRGM
LLANPHFPWG GGMRFYQMHL TIPGKLDVMG AALPGLPLIN IGFNRHLAWS HTVDTSKHFT
LHRLQLDPKD STRYLLDGKS IAMGQQQVSV EVKQPDGSLK DVPRIIYSSK FGPVVQWPGK
LDWDDKFAFS LRDANLENDR VLQQWYSMDK ADSLKAFQDS LHKIQGIPWV NTLAVDAKGQ
ALYMNLSVVP NVDAAKLAKC SDPRIGTELI VLDGSRSECN WDISAEAAQA GIYPSSRQPQ
LLRSDFVQHS NDSAWMVNPA APLKGFSPLI SQDGQPLGQR ARFALDRLGS LQQAGKVSAE
NLQAMVMDNE VYQAGQVLPD LLKFCASELG DDVARLTPLC AALKAWDGRA DLNSGIGFVY
FQRIMTSMQG VASRWRVVFD PQNPIHTPSG LAIENPQVAS ALRAAMLAAV DEVAKAGLSP
ESKWGDIQVS SLSGKPIPIH GGPAGLGVYN AMQTIAGKDG KREVVSGTSY LQVVTFDEQG
PRAQGLLAFS ESSNPQSAHS SDQTEAFSKK QWSELPFTEQ QIKADPAYQV QVISEEGSR
