PVDQ_PSESM
ID PVDQ_PSESM Reviewed; 773 AA.
AC Q884D2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=PSPTO_2161;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO55678.1; -; Genomic_DNA.
DR RefSeq; NP_791983.1; NC_004578.1.
DR RefSeq; WP_011103880.1; NC_004578.1.
DR AlphaFoldDB; Q884D2; -.
DR SMR; Q884D2; -.
DR STRING; 223283.PSPTO_2161; -.
DR MEROPS; S45.004; -.
DR PRIDE; Q884D2; -.
DR EnsemblBacteria; AAO55678; AAO55678; PSPTO_2161.
DR GeneID; 1183808; -.
DR KEGG; pst:PSPTO_2161; -.
DR PATRIC; fig|223283.9.peg.2192; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_6; -.
DR OMA; QGIPWVN; -.
DR OrthoDB; 186419at2; -.
DR PhylomeDB; Q884D2; -.
DR Proteomes; UP000002515; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..773
FT /note="Acyl-homoserine lactone acylase PvdQ"
FT /id="PRO_0000253377"
FT CHAIN 24..?199
FT /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT /id="PRO_0000253378"
FT PROPEP ?200..221
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253379"
FT CHAIN 222..773
FT /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT /id="PRO_0000253380"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 773 AA; 84377 MW; 3402BA5500258FE6 CRC64;
MSRALPGFLF AGLSVAVVLP AQALVAHEQK AAGAEIRRTG FGVPHIVADD ERGLGYGIGY
AYAQDNLCLL ANEVVTVNGE RSRYFGPDKA TLEQRNNMAS DLLFKWLNTP QALADFWKAQ
PAEIRHLMQG YVAGYNRSLA EQTTQGLPQP CAAEWVRPIS TDDLVRLTRR LLVEGGVGQF
TEAFAGAKPP STQKPLQVDS QQVQALQLAA ARNERFALER GSNAVAVGRD LSANGRGMLL
ANPHFPWGGG MRFYQMHLTI PGKLDVMGAA LPGLPLINIG FNQHLAWSHT VDTSKHFTLH
RLQLDPKDST RYLLDGKSVA MGKQQVSVEV KQADGTLKAV PRIIYSSKFG PVVQWPGKLD
WDDKFAFSLR DANLKNDRVL QQWYAMDQAD SLKAFQDSVH RIQGIPWVNT LAVDAKGQAL
YMNISVVPNV DAVKLARCSD PRIGTELIVL DGSRSECNWD VSPEAAQAGI YPSSRQPQLL
RTDFVQHSND SAWMVNPAAP LKDFSPLISQ DGQPLGQRAR FALDRLSSLE KTGKVSVENL
QAMVMDNEVY HAGQVLPDLL KFCASELGDD AARLAPLCTA LKAWDGRADL NSGIGFVYFQ
RIVTSMQAVA SRWRVVFDPQ NPVHTPSGLA IEYPEVATAL RAAMLAAVDE VAKAGLSADT
RWGDIQVSSI SGKPIPIHGG PAGLGIYNAM QTVAGRDGKR EVVSGTSYLQ VVTFDEHGPK
AQGLLAFSES SNPQSAHSRD QTEAFSKKHW SVLPFTEQQI KADPAYQVQV VKE
