ID U2ZR78_PSEA4 Unreviewed; 841 AA.
AC U2ZR78;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Acyl-homoserine lactone acylase QuiP {ECO:0000256|ARBA:ARBA00039697};
DE EC=3.5.1.97 {ECO:0000256|ARBA:ARBA00039041};
GN ORFNames=PA6_027_00280 {ECO:0000313|EMBL:GAD63587.1};
OS Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC
OS 14159 / NCIMB 9945 / NCTC 10367 / 1577).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1215092 {ECO:0000313|EMBL:GAD63587.1, ECO:0000313|Proteomes:UP000016560};
RN [1] {ECO:0000313|EMBL:GAD63587.1, ECO:0000313|Proteomes:UP000016560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 /
RC NCTC 10367 / 1577 {ECO:0000313|Proteomes:UP000016560};
RA Yoshida I., Hosoyama A., Tsuchikane K., Noguchi M., Hirakata S., Ando Y.,
RA Ohji S., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Pseudomonas alcaligenes NBRC 14159.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00036743};
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 -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC from the same precursor. {ECO:0000256|ARBA:ARBA00038735}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD63587.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BATI01000027; GAD63587.1; -; Genomic_DNA.
DR RefSeq; WP_021701672.1; NZ_BATI01000027.1.
DR AlphaFoldDB; U2ZR78; -.
DR STRING; 43263.A0T30_09045; -.
DR MEROPS; S45.003; -.
DR eggNOG; COG2366; Bacteria.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000016560; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0009372; P:quorum sensing; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Quorum sensing {ECO:0000256|ARBA:ARBA00022654};
KW Reference proteome {ECO:0000313|Proteomes:UP000016560};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 260
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 841 AA; 92554 MW; AD5E39DFFDDC8FC3 CRC64;
MGSRFLRLTI LATLGSTLLL GGCQSFLNSR YANSVHPDQG IVRVQGLAQS VVVRRNPLGM
PLIETTTFHD ALFTLGYVHA ADRLSQMVGM RLLAEGRLAE MNGPGMLEID RFMRTVNLKA
EAEVLYKNAS PRIKKFFEVY ARGVNAYLFR YQDRLPMDLA ESGYRPAYWK PEDSVLLFCL
LNFGLSVNLQ EEIAALKLAD KVGADKLAWL LPSYPDEPLP FEEAEKLRGL SLGGQIPGLA
AVNDAAGQVA ALNMLGVAAS NNWAIAPQNS RSGRSLLAND THLPLSMPSV WNFVHIRSPK
FQAAGVSIAG VPAVVAGFNG KLAWGMTMVM GDNQDLFLEK VKREGGRLYY MADGKWQPAR
ERQETFFIKG QRPIRETIWE TRHGPLLNSA LGERKSPLQP LPLRSGYGLA LRNIQAEADR
SIDAFFDLSR AQSVEQAFEA TREVRAMALN IVLADAQHIG WQVTGRYPNR KQGTGLVPSP
GWNGAYDWDG YADPMLHPYD QDPLQGWLGT ANHRTVPRGY GMQLSNSWFY PERAERIAQL
AGSGKHDQKS MIAMQYDQTT PFAGKLQAML DAPSMAAPLK QAIAALPAPE RTKAEEAYKR
LMAFDGRMAA TSADAALYSA FLQESAKATF LDELGPQTSP AWQALVDTAN NSYSAQADHL
LGRDDSPFWD DVKTAQKEDK AAILARSLAN AVTFLEGGLG ANRSAWQWGK LHQYRWTSNA
SKMAPYLSAS QRSSIESISS YLDRGPYPAG GDHGTLNVAA YAWGNDFDVW LIPAMRIVVD
FGLPEPMIGL NSSGQSGNPA SRHYADGIEA WLKGGYMSFP FQSGNIDRVY GNKRLMLMPG
R
//
