ID   A0A1V9GD01_9BACT        Unreviewed;       819 AA.
AC   A0A1V9GD01;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Acyl-homoserine-lactone acylase {ECO:0000313|EMBL:OQP68470.1};
GN   ORFNames=A4R26_01295 {ECO:0000313|EMBL:OQP68470.1};
OS   Niastella populi.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=550983 {ECO:0000313|EMBL:OQP68470.1, ECO:0000313|Proteomes:UP000192276};
RN   [1] {ECO:0000313|Proteomes:UP000192276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=208 {ECO:0000313|Proteomes:UP000192276};
RA   Chen L., Zhuang W., Wang G.;
RL   Submitted (APR-2016) 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   -!- 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:OQP68470.1}.
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; LWBP01000001; OQP68470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9GD01; -.
DR   STRING; 550983.A4R26_01295; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000192276; Unassembled WGS sequence.
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   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};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192276};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   819 AA;  93343 MW;  8ADEAE419CE06A7D CRC64;
     MRIIPLIVTV VVTIGLIITL SMPIGSIPPL GSFLSPQTGF WQNAEPVDAH ADLNLYLPQL
     KEKVQVYVDD RMVPHVFAQN DEDLYLVQGY LHAKYRLWQM EFQTHAAAGR LSEVLGAGPN
     NAYLNYDRNM RRVGMKLGAS RSLDSMENDP NTKSMLDAYT AGVNAYIDHL PANELPLEYR
     LLNYVPEHWN NFKTALFLKY MSYDLTGSEN DFEYTNVRNV LSQEDFELLY PVMQDSLDPI
     VPRGTTFNAP AARPLMPVTT DSLYFKWNTF ADIAPTPVDK PDKDNGSNNW AVDGTKTKSG
     RPILCNDPHL GLNLPSLWFE MQLHTPQYNV YGVTFPGSPA VIIGFNDSCS WGVTNAGRDV
     KDYFVVHFKD QTREQYEFNG AWKQSELHVD TFKIKGRAPF YDTVAYTIFG PVQYDNSFTG
     SNRASAYTNY AVRWKAHDGS NELKTFYLLN RMKSKSDYED AIKYFYCPGQ NFVFASKSGD
     IAIWQQGKFP AKWRRQGDFI MPGTDTAYLW QGYIDQKDNP HNDNEIDSAR GFVSSANQAA
     TDTTYPFYLG GSYPIYRGII INRYLRQLNG ITIDDMKKMQ TDNFNVFAET ALPIMMANID
     ENTLSTEENK YLDILRGWNL RYDAMEKAPA IFQLWIENLE KEVWNDELDV ANKPVIMPEK
     ATLVKCLSFA NFKFADNINT QTVESVKDVV TAAFKKVVPV VSKADAEGEL NWGKYKDAGI
     RHLLRLAPLS RYHMETGGGE NVINATKQFH GPSWRMIVEM TDKTDAWGIY PGGQSGNPGS
     RYYDNFVYDW AAGRYNQLWV MDEKDVKDKR ILFTINFNN
//