ID   A0A9E8L1Y0_9PSED        Unreviewed;       847 AA.
AC   A0A9E8L1Y0;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   13-SEP-2023, entry version 3.
DE   SubName: Full=Acyl-homoserine-lactone acylase QuiP {ECO:0000313|EMBL:UZX34387.1};
DE            EC=3.5.1.97 {ECO:0000313|EMBL:UZX34387.1};
GN   Name=quiP {ECO:0000313|EMBL:UZX34387.1};
GN   ORFNames=M6E97_17880 {ECO:0000313|EMBL:UZX34387.1};
OS   Pseudomonas sp. B111.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2944252 {ECO:0000313|EMBL:UZX34387.1};
RN   [1] {ECO:0000313|EMBL:UZX34387.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B111 {ECO:0000313|EMBL:UZX34387.1};
RA   Flores Clavo R., Fantinatti Garboggini F.;
RT   "Enviromental Metabolomic of bacterial saloons of nort west Peru.";
RL   Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001227-2};
CC       Note=Binds 1 Ca(2+) ion per dimer. {ECO:0000256|PIRSR:PIRSR001227-2};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; CP097857; UZX34387.1; -; Genomic_DNA.
DR   RefSeq; WP_034005179.1; NZ_CP097857.1.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd03747; Ntn_PGA_like; 1.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 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:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR   PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   PIRSF; PIRSF001227; Pen_acylase; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:UZX34387.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..847
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038760910"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         337
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         340
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   847 AA;  94028 MW;  EA6074CB4D64F6F7 CRC64;
     MASPAFMRFL PRCGAAAAFG TLLGLAGCQS WLDDRYADSL PPTSGVQPIK GLAQNVSIRR
     NALGMPLIET GTFHDALFAL GYVHASDRLS QMVSLRLLAQ GRLAEMAGPG ALEIDRFMRT
     VNLRQAAEIQ YRNASPRLQR FFEVYARGVN AYLYRYRDKL PMDLAQSGYR PEYWKPEDSA
     LVFALLNFGL AVNLQEEIAS LTLAQKVGSD KLAWLTPTYP DENLPFDEAE KLKGLRLDGQ
     VPGLAGVEGA ARQVAALSML GVAASNNWAI APQRSRSGKS LMANDTHLPL SMPSVWNYVQ
     IRSPKYQAAG VSIAGLPGVV AGFNGKLAWG MTMVLGDNQD LYLEQLRRQG NRLYYLADGK
     WQPTRERQET FFIKGQRPIR EVIHETRHGP LLNSALGERK NILQPLPLKS GYGLAYRSIQ
     QEADKTLDGF FDLSRAKTIE QAFDATREIR AMPLNIVFAD EKHIGWQVTG RYPNRKEGRG
     LLPSPGWDGR YDWDGYADPI LHPSDQDPQQ GWLGTANHRT VQPGYGAQLS NSWYYPERAE
     RIAQLAGASK SHDTQSMIRM QYDQTSLFVA KLQAMFDNPG MAAPLRQAID ALPEAQRSRA
     REAYDRLMAF DGKLTASSSD AALYGAFLHE SARQIFLDEL GPEDGPAWKA FVETANLSYS
     AQADHLLGRD DSPFWDDTRT PQKEDKPAIL ARSLAAAVEF CEQRLGSERK AWQWGKLHTY
     EWRSDSSKMA PYLGAGERAG LGAIKGYLDR GPYPAGGDHT TLDVSAYGWG QDFDTWLIPA
     MRLIVDFGQS EPMIGVNSSG QSGNPASPHY ADGIDAWLKG RYVSFPFQPQ NLDRVYGNKR
     LTLTPAR
//