QUIP_PSE14
ID QUIP_PSE14 Reviewed; 824 AA.
AC Q48LS4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=PSPPH_1391;
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 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; CP000058; AAZ33717.1; -; Genomic_DNA.
DR RefSeq; WP_004664093.1; NC_005773.3.
DR AlphaFoldDB; Q48LS4; -.
DR SMR; Q48LS4; -.
DR STRING; 264730.PSPPH_1391; -.
DR MEROPS; S45.003; -.
DR EnsemblBacteria; AAZ33717; AAZ33717; PSPPH_1391.
DR KEGG; psp:PSPPH_1391; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_6; -.
DR OMA; EMDVRRH; -.
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; 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_0000253397"
FT CHAIN 27..?
FT /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT /id="PRO_0000253398"
FT PROPEP ?..263
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253399"
FT CHAIN 264..824
FT /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT /id="PRO_0000253400"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 824 AA; 89926 MW; 875140600CB3A924 CRC64;
MASPALRHFL PRFGAAAAAA SFLSLAGCQL GGGDPETVLP ASGTFPLKGL AQNVSVRRNN
MGMPLIESST YHDALFTLGY IHAGDRIGQM LGMRLLAQGR LSEMAGADAL EVDRLMRSVN
LKQNASDLYN AASPRLKRFF DVYARGVNAY LFRYRDKLPA DVASSGYKPE YWKPEDSALI
FSLLNFSLSV NLQEELSALV LAQKVGADKL AWLLPTYPDE ELPFAEADKL KGLNLNNQVN
DLSDLNKIAL QLSDLNMLGV AASSNWAIAP QRSRSGKSLL ASDMQLPAGL NSAWSFVQIR
APKYQVSGVS IAGLPLVLSG FNGKLAWSMS NVKGDNQDLF LEKIKREGNR ISYMADGKWV
PAASHQETFL VKGGSPIRET VYETRHGALL NASATPPGNG LSLALQVPNF KDDKSLDAFF
DLSRAPNVEK AFDTSREIRA ITLNMIFADA SNIGWQVTGR FPNRREGQGL LPSPGWDGKY
DWDGFADSML HPYDQDPRQG WLAAANQRTI PKGYGMQLSN SWGYPERAER IAELANSGKQ
DLRSTVAMQY DQTTTFAAKL KTMFQAPGMS KPLKQAIDAL PEADRNKARE AFTRLMAFDG
KLSATSADAA LYELFLQESA KQIFLDELGP ETSPAWQALV ANASSSYSPQ ADHLLGRDDS
PYWDDVKTPQ KEDKPAILAR SLAAAVTSGD SLLGSDHKAW QWGKLHRDNW TSTSPLAKQL
GGGEFNRGAS PAGGDHSTLN VSGFEWGKGF DTHVAPGLRM IVDFSLVEPM TGLISTGQSG
NPASPYYANS IEPWQKGQYM SIPLQQQNYE KGYGKQRLTL TPGK
