ID   QUIP_PSEU2              Reviewed;         824 AA.
AC   Q4ZPM1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Acyl-homoserine lactone acylase QuiP;
DE            Short=AHL acylase QuiP;
DE            Short=Acyl-HSL acylase QuiP;
DE            EC=3.5.1.97;
DE   Contains:
DE     RecName: Full=Acyl-homoserine lactone acylase QuiP subunit alpha;
DE              Short=Acyl-HSL acylase QuiP subunit alpha;
DE   Contains:
DE     RecName: Full=Acyl-homoserine lactone acylase QuiP subunit beta;
DE              Short=Acyl-HSL acylase QuiP subunit beta;
DE   Flags: Precursor;
GN   Name=quiP; OrderedLocusNames=Psyr_3871;
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 seven or more carbons in length) (By
CC       similarity). {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:0000305}.
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; CP000075; AAY38901.1; -; Genomic_DNA.
DR   RefSeq; WP_011268708.1; NC_007005.1.
DR   RefSeq; YP_236939.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZPM1; -.
DR   SMR; Q4ZPM1; -.
DR   STRING; 205918.Psyr_3871; -.
DR   MEROPS; S45.003; -.
DR   EnsemblBacteria; AAY38901; AAY38901; Psyr_3871.
DR   KEGG; psb:Psyr_3871; -.
DR   PATRIC; fig|205918.7.peg.3979; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_011790_0_1_6; -.
DR   OMA; EMDVRRH; -.
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; 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   3: Inferred from homology;
KW   Hydrolase; Periplasm; Quorum sensing; Signal; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..824
FT                   /note="Acyl-homoserine lactone acylase QuiP"
FT                   /id="PRO_0000253401"
FT   CHAIN           27..?
FT                   /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT                   /id="PRO_0000253402"
FT   PROPEP          ?..263
FT                   /note="Spacer peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000253403"
FT   CHAIN           264..824
FT                   /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT                   /id="PRO_0000253404"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   824 AA;  90087 MW;  BCDF35CAE080EE32 CRC64;
     MASPALRHFL PRFGAAAAAA SFLSLAGCQL GGNDPETVLP VSGTFPLKGL AQNVSVRRNN
     MGMPLIESSS YHDALFTLGY VHAGDRISQM LGMRLLAQGR LSEMAGADAL DVDRLMRSVN
     LKQNASDLYN AASPRLKRFF DVYARGVNAY LFRYRDKLPA DIASSGYKPE YWKPEDSALI
     FSLLNFSLSV NLQEELSALV LAQKVSADKL AWLLPTYPDE ELPFAEADKL KGLNLNNQVT
     GLSDLNRIAL QLSDLNMLGV AASSNWAIAP QRSRNGKSLL ASDMQLPAGL NSAWSFVQIR
     APKYQVSGVT IAGMPLVLSG FNGKLAWSMS NVKGDNQDLF LEKIKREGNR VSYMVDGKWL
     PAAAHQETFL VKGGSPLRET VYETRHGALL NASATPPGNG LSLALQVPNF KDDKSLDAFF
     DLSRAPNVEK AFDTSREIRA ITLNMIFADA SNIGWQVTGR FPNRREGQGL LPSPGWDGKY
     DWDGFADSML HPYDQDPRQG WLAAANQRTI PKGYGMQLSN SWGYPERAER IAELANGGKQ
     DLRSTIAMQY DQTTTFAAKL KSMFQAPGMS KPLKQAIDAL PEADRNKARE AFTRLMAFDG
     KLSATSADAA LYELFLQESA KQIFLDELGP ETSPAWQALV ANASSSYSPQ ADHLLGRDDS
     PYWDDVKTPQ KEDKPAILAR SLAAAITSGD SLLGSDHKAW QWGKLHRDNW ASTSPLAKQL
     GGGEFNRGAT PTGGDHTTLN VSGFEWGKGF DARMAPGLRM IVDFSLVEPM TGLISTGQSG
     NPASPYYANS IEPWQKGQYQ SIPVQQQNYE KGYGKQRLTL TPGK