PVDQ_PSEAE
ID PVDQ_PSEAE Reviewed; 762 AA.
AC Q9I194;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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; Synonyms=qsc112; OrderedLocusNames=PA2385;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 24-28 AND 217-221, FUNCTION, SUBSTRATE SPECIFICITY,
RP MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16495538; DOI=10.1128/iai.74.3.1673-1682.2006;
RA Sio C.F., Otten L.G., Cool R.H., Diggle S.P., Braun P.G., Bos R.,
RA Daykin M., Camara M., Williams P., Quax W.J.;
RT "Quorum quenching by an N-acyl-homoserine lactone acylase from Pseudomonas
RT aeruginosa PAO1.";
RL Infect. Immun. 74:1673-1682(2006).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12207696; DOI=10.1046/j.1365-2958.2002.03084.x;
RA Ochsner U.A., Wilderman P.J., Vasil A.I., Vasil M.L.;
RT "GeneChip expression analysis of the iron starvation response in
RT Pseudomonas aeruginosa: identification of novel pyoverdine biosynthesis
RT genes.";
RL Mol. Microbiol. 45:1277-1287(2002).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=14532048; DOI=10.1128/aem.69.10.5941-5949.2003;
RA Huang J.J., Han J.-I., Zhang L.-H., Leadbetter J.R.;
RT "Utilization of acyl-homoserine lactone quorum signals for growth by a soil
RT pseudomonad and Pseudomonas aeruginosa PAO1.";
RL Appl. Environ. Microbiol. 69:5941-5949(2003).
RN [5]
RP GENE NAME, AND ROLE IN PYOVERDIN BIOSYNTHESIS.
RX PubMed=12686626; DOI=10.1099/mic.0.26085-0;
RA Lamont I.L., Martin L.W.;
RT "Identification and characterization of novel pyoverdine synthesis genes in
RT Pseudomonas aeruginosa.";
RL Microbiology 149:833-842(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). Degrades 3-oxo-
CC C12-HSL, one of the two main AHL signal molecules of P.aeruginosa, and
CC thereby functions as a quorum quencher, inhibiting the las quorum-
CC sensing system. Therefore, may enable P.aeruginosa to modulate its own
CC quorum-sensing-dependent pathogenic potential. Also appears to be
CC required for pyoverdin biosynthesis. {ECO:0000269|PubMed:12686626,
CC ECO:0000269|PubMed:14532048, ECO:0000269|PubMed:16495538}.
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:0000269|PubMed:16495538}.
CC -!- INTERACTION:
CC Q9I194; Q9I194: pvdQ; NbExp=3; IntAct=EBI-15828240, EBI-15828240;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated under iron starvation conditions.
CC {ECO:0000269|PubMed:12207696}.
CC -!- MASS SPECTROMETRY: [Acyl-homoserine lactone acylase PvdQ subunit
CC alpha]: Mass=18574; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16495538};
CC -!- MASS SPECTROMETRY: [Acyl-homoserine lactone acylase PvdQ subunit beta]:
CC Mass=60426; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16495538};
CC -!- MISCELLANEOUS: A variable cleavage site between the alpha-subunit and
CC the spacer peptide was observed: Ala-194 may be a part of the alpha-
CC subunit or the spacer peptide. This step of the maturation process may
CC not be very specific.
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; AE004091; AAG05773.1; -; Genomic_DNA.
DR PIR; H83348; H83348.
DR RefSeq; NP_251075.1; NC_002516.2.
DR RefSeq; WP_003115642.1; NZ_QZGE01000021.1.
DR PDB; 2WYB; X-ray; 2.10 A; A=24-193, B=217-762.
DR PDB; 2WYC; X-ray; 1.90 A; A=24-193, B=217-762.
DR PDB; 2WYD; X-ray; 1.90 A; A=24-193, B=217-762.
DR PDB; 2WYE; X-ray; 1.80 A; A=24-193, B=217-762.
DR PDB; 3L91; X-ray; 1.66 A; A=24-193, B=217-762.
DR PDB; 3L94; X-ray; 1.95 A; A=24-193, B=217-762.
DR PDB; 3SRA; X-ray; 2.30 A; A=29-191, B=217-762.
DR PDB; 3SRB; X-ray; 1.80 A; A=29-191, B=217-762.
DR PDB; 3SRC; X-ray; 2.00 A; A=29-192, B=217-762.
DR PDB; 4BTH; X-ray; 1.90 A; A=24-193, B=217-762.
DR PDB; 4K2F; X-ray; 1.99 A; A=24-193, B=217-762.
DR PDB; 4K2G; X-ray; 2.30 A; A=24-193, B=217-762.
DR PDB; 4M1J; X-ray; 1.80 A; A=28-192, C=217-762.
DR PDB; 4WKS; X-ray; 1.63 A; A=28-192, C=217-762.
DR PDB; 4WKT; X-ray; 1.78 A; A=28-192, C=217-762.
DR PDB; 4WKU; X-ray; 2.00 A; A=28-192, B=217-762.
DR PDB; 4WKV; X-ray; 2.14 A; A=28-192, C=217-762.
DR PDB; 5UBK; X-ray; 2.55 A; A=217-762.
DR PDB; 5UBL; X-ray; 1.80 A; A=217-762.
DR PDBsum; 2WYB; -.
DR PDBsum; 2WYC; -.
DR PDBsum; 2WYD; -.
DR PDBsum; 2WYE; -.
DR PDBsum; 3L91; -.
DR PDBsum; 3L94; -.
DR PDBsum; 3SRA; -.
DR PDBsum; 3SRB; -.
DR PDBsum; 3SRC; -.
DR PDBsum; 4BTH; -.
DR PDBsum; 4K2F; -.
DR PDBsum; 4K2G; -.
DR PDBsum; 4M1J; -.
DR PDBsum; 4WKS; -.
DR PDBsum; 4WKT; -.
DR PDBsum; 4WKU; -.
DR PDBsum; 4WKV; -.
DR PDBsum; 5UBK; -.
DR PDBsum; 5UBL; -.
DR AlphaFoldDB; Q9I194; -.
DR SMR; Q9I194; -.
DR DIP; DIP-58522N; -.
DR STRING; 287.DR97_6047; -.
DR ChEMBL; CHEMBL1741161; -.
DR DrugBank; DB03017; Lauric acid.
DR MEROPS; S45.004; -.
DR PaxDb; Q9I194; -.
DR PRIDE; Q9I194; -.
DR EnsemblBacteria; AAG05773; AAG05773; PA2385.
DR GeneID; 882260; -.
DR KEGG; pae:PA2385; -.
DR PATRIC; fig|208964.12.peg.2495; -.
DR PseudoCAP; PA2385; -.
DR HOGENOM; CLU_017615_0_0_6; -.
DR InParanoid; Q9I194; -.
DR OMA; QGIPWVN; -.
DR PhylomeDB; Q9I194; -.
DR BioCyc; MetaCyc:MON-20241; -.
DR BioCyc; PAER208964:G1FZ6-2423-MON; -.
DR BRENDA; 3.5.1.97; 5087.
DR EvolutionaryTrace; Q9I194; -.
DR PHI-base; PHI:4058; -.
DR PHI-base; PHI:4713; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:PseudoCAP.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0047379; F:ADP-dependent short-chain-acyl-CoA hydrolase activity; IMP:PseudoCAP.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:PseudoCAP.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:PseudoCAP.
DR GO; GO:0002049; P:pyoverdine biosynthetic process; IDA:PseudoCAP.
DR GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IMP:PseudoCAP.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Periplasm;
KW Quorum sensing; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:16495538"
FT CHAIN 24..762
FT /note="Acyl-homoserine lactone acylase PvdQ"
FT /id="PRO_0000253353"
FT CHAIN 24..193
FT /note="Acyl-homoserine lactone acylase PvdQ subunit alpha"
FT /id="PRO_0000253354"
FT PROPEP 194..216
FT /note="Spacer peptide"
FT /evidence="ECO:0000269|PubMed:16495538"
FT /id="PRO_0000253355"
FT CHAIN 217..762
FT /note="Acyl-homoserine lactone acylase PvdQ subunit beta"
FT /id="PRO_0000253356"
FT ACT_SITE 217
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 50..76
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3SRC"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 121..140
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4WKS"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:3L91"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:4WKS"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:4WKS"
FT TURN 256..258
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:4WKS"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 374..382
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 429..433
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 474..486
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:3L94"
FT TURN 502..504
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 543..556
FT /evidence="ECO:0007829|PDB:4WKS"
FT TURN 557..560
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 585..596
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:4WKS"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 624..643
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 663..666
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 676..685
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 688..695
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 697..702
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 709..714
FT /evidence="ECO:0007829|PDB:4WKS"
FT HELIX 729..735
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:2WYE"
FT HELIX 746..750
FT /evidence="ECO:0007829|PDB:4WKS"
FT STRAND 756..762
FT /evidence="ECO:0007829|PDB:4WKS"
SQ SEQUENCE 762 AA; 84040 MW; 8CAD38D280EDD43B CRC64;
MGMRTVLTGL AGMLLGSMMP VQADMPRPTG LAADIRWTAY GVPHIRAKDE RGLGYGIGYA
YARDNACLLA EEIVTARGER ARYFGSEGKS SAELDNLPSD IFYAWLNQPE ALQAFWQAQT
PAVRQLLEGY AAGFNRFLRE ADGKTTSCLG QPWLRAIATD DLLRLTRRLL VEGGVGQFAD
ALVAAAPPGA EKVALSGEQA FQVAEQRRQR FRLERGSNAI AVGSERSADG KGMLLANPHF
PWNGAMRFYQ MHLTIPGRLD VMGASLPGLP VVNIGFSRHL AWTHTVDTSS HFTLYRLALD
PKDPRRYLVD GRSLPLEEKS VAIEVRGADG KLSRVEHKVY QSIYGPLVVW PGKLDWNRSE
AYALRDANLE NTRVLQQWYS INQASDVADL RRRVEALQGI PWVNTLAADE QGNALYMNQS
VVPYLKPELI PACAIPQLVA EGLPALQGQD SRCAWSRDPA AAQAGITPAA QLPVLLRRDF
VQNSNDSAWL TNPASPLQGF SPLVSQEKPI GPRARYALSR LQGKQPLEAK TLEEMVTANH
VFSADQVLPD LLRLCRDNQG EKSLARACAA LAQWDRGANL DSGSGFVYFQ RFMQRFAELD
GAWKEPFDAQ RPLDTPQGIA LDRPQVATQV RQALADAAAE VEKSGIPDGA RWGDLQVSTR
GQERIAIPGG DGHFGVYNAI QSVRKGDHLE VVGGTSYIQL VTFPEEGPKA RGLLAFSQSS
DPRSPHYRDQ TELFSRQQWQ TLPFSDRQID ADPQLQRLSI RE
