QUIP_PSEF5
ID QUIP_PSEF5 Reviewed; 809 AA.
AC Q4KH86;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=PFL_1268;
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(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; CP000076; AAY90553.1; -; Genomic_DNA.
DR RefSeq; WP_011059611.1; NC_004129.6.
DR AlphaFoldDB; Q4KH86; -.
DR SMR; Q4KH86; -.
DR STRING; 220664.PFL_1268; -.
DR MEROPS; S45.003; -.
DR EnsemblBacteria; AAY90553; AAY90553; PFL_1268.
DR KEGG; pfl:PFL_1268; -.
DR PATRIC; fig|220664.5.peg.1299; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_6; -.
DR OMA; EMDVRRH; -.
DR OrthoDB; 186419at2; -.
DR Proteomes; UP000008540; 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..809
FT /note="Acyl-homoserine lactone acylase QuiP"
FT /id="PRO_0000253385"
FT CHAIN 27..?
FT /note="Acyl-homoserine lactone acylase QuiP subunit alpha"
FT /id="PRO_0000253386"
FT PROPEP ?..260
FT /note="Spacer peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000253387"
FT CHAIN 261..809
FT /note="Acyl-homoserine lactone acylase QuiP subunit beta"
FT /id="PRO_0000253388"
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 809 AA; 88603 MW; 90EBF693B18E3819 CRC64;
MASPAFSHFL PRFGVAAAVA SALSLAGCQS WNTQDTLPPT SGVQPLKGLA QNVSVRRNAV
GVPLIESSSF HDALFTLGYV HASDRIGQMV TLHLLAQGRL AEMSGADALE VDRLMRAINL
KKSADELYKA SSPRIKRFFE VYARGVNAYL FRYRDKLPPD LAAQGYTPEY WKAEDSALIF
CLLNFGQSAN LQEEINALVL AQKVGSDKLP WLTPSYPDEP LPLAEADKLK GLNLTVPGLN
EVSRAINRLA QLNSLGTRGG SNLAIAPQRS RTGRSLLAAD SHLQAWYYTQ IRAPKYQAAG
ASIAGLPAIL QGFNGKVAWS MSSVEGDNQD LFLEKLKRQG NALYYQNNGK WQPVTVRNET
YFVKGQRPIR EAVYETRHGP LLNSALGAAL GNGFGLALQT PELKDDKTLD AFFDLSRAQN
VEKASDASRE IRAIALNMVF ADASNIGWQV TGRFPNRREG EGLLPSPGWD GRYDWDGYAD
PMLHPYDQDP PQGWIATANQ RVISQGYGMQ LSNSWHAPER AERMAGLASS GKQDNRSLIA
LQYDQSTLFA AKLKKMFEAP GMAQPLKQAI EALPDTERAK AREAYSRLLA FDGKVSAGSA
DAALYELFLQ ESAKQIFLDK LGPESSDAWQ AFVANGNLSY SAQADHLLGQ EDSPFWDDSR
TAQKEDKPAI LARSLAAAIS SGEQLLGADR KAWQWGKLHS YQWTNANGRQ IRGPLQAGGD
HNTINSAAYR WGQDFAITDT PALRLIVDFS LSEPLMGLNS SGQSGNPVSP NYANGIDGWL
KAQYLSLPMQ PQNFERSYGK TRLTLVPGK
