QUIP_PSESM
ID QUIP_PSESM Reviewed; 824 AA.
AC Q87XP3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=PSPTO_4133;
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 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; AE016853; AAO57589.1; -; Genomic_DNA.
DR RefSeq; NP_793894.1; NC_004578.1.
DR RefSeq; WP_011104884.1; NC_004578.1.
DR AlphaFoldDB; Q87XP3; -.
DR SMR; Q87XP3; -.
DR STRING; 223283.PSPTO_4133; -.
DR MEROPS; S45.003; -.
DR EnsemblBacteria; AAO57589; AAO57589; PSPTO_4133.
DR GeneID; 1185813; -.
DR KEGG; pst:PSPTO_4133; -.
DR PATRIC; fig|223283.9.peg.4243; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_6; -.
DR OMA; EMDVRRH; -.
DR OrthoDB; 186419at2; -.
DR PhylomeDB; Q87XP3; -.
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; 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; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..824
FT /note="Acyl-homoserine lactone acylase QuiP"
FT /id="PRO_0000253405"
FT CHAIN 27..?
FT /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT /id="PRO_0000253406"
FT PROPEP ?..263
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253407"
FT CHAIN 264..824
FT /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT /id="PRO_0000253408"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 824 AA; 89953 MW; 27C0024F1ACFF382 CRC64;
MASPALRHFL PRFGAAAAAA SFLSLAGCQL GGGDPETVLP ASGTFPLKGL AQNVSVRRNN
MGMPLIESST YHDALFTLGY VHAGDRIGQM LGMRLLAQGR LSEVAGADAL EVDRLMRSVN
LKRNASDLYN AASPRLKRFF DVYARGVNAY LFRYRDKLPA DVARAGYTPE YWKPEDSALI
FSLLNFSLSV NLQEELSALV LAQKVGADKL AWLLPTYPDE ELPFAEADKL KGLNLSNQVT
GLSDLNRIAL QLSDLNMLGV AASSNWAIAP QRSRSGKSLL ASDMQLPAGL NSAWSFVQIR
APKYQVSGAS IAGLPLVLSG FNGKLAWSMS NVKGDNQDLF LEKIKREGNR VSYMADGKWV
PAASHQETFL VKGGSPIRET VYETRHGALL NASATPPGNG LSLALQVPDF KDDKSLDAFF
DLSRAPNVEK AFDTSREIRA ITLNMVFADA SNIGWQVTGR FPNRREGQGL LPSPGWDGKY
DWDGFADSML HPYDQDPRQG WLAAANQRTI PKGYGMQLSN SWGYPERAER IAELANSGKQ
DLRSTVAMQY DQTTTFAAKL KTIFQAPGMS KPLKQAIDAL PEADRNNARE AFTRLMAFDG
KLSATSADAA LYELFLQESA KQIFLDELGP ETSPAWQALV ANASSSYSPQ ADHLLGRDDS
PYWDDVKTPQ KEDKPAILAR SLAAAVTRGD SLLGSDHKAW QWGKLHRDNW TSANPLARQL
GGGEFNRSAS AAGGDHTTLN VSGFEWGKGF DARVAPSLRM IVDFSLVEPM TGMINTGQSG
NPASPYYANS IEPWQKGQYM SIPLQQQNYE KGYGKQRLTL TPGK
