ID   A0A2A4Z1L1_9PROT        Unreviewed;       821 AA.
AC   A0A2A4Z1L1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acyl-homoserine-lactone acylase {ECO:0000313|EMBL:PCJ00781.1};
GN   ORFNames=COB13_09230 {ECO:0000313|EMBL:PCJ00781.1};
OS   OCS116 cluster bacterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; OCS116 cluster.
OX   NCBI_TaxID=2030921 {ECO:0000313|EMBL:PCJ00781.1, ECO:0000313|Proteomes:UP000218076};
RN   [1] {ECO:0000313|Proteomes:UP000218076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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:PCJ00781.1}.
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DR   EMBL; NVUS01000010; PCJ00781.1; -; Genomic_DNA.
DR   Proteomes; UP000218076; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         194
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"
FT   BINDING         343
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   821 AA;  92489 MW;  24533EF19ABCC063 CRC64;
     MYIVKRAFKY LGYLVGFLCV ILIVAAISIY AYFTNGLPSY NGQVQLAGLK DKVTITRDQH
     ALPHIIAQTS DDAYFAIGYA HAQDRLFQMQ LHRHIAMGRL SELIGQQGLE TDKFLRTLGM
     YQAAEASYHL LSQQTKTQLE AYSAGINAYL AEDHILPVEF AILQLDKPQP WQPLHSAAWM
     KIMAWDLNNT WRKELDRLVM SANFTPQQIA EYHHAYPGDK AFIPPKPIDI YGFELNAPSP
     LQTSALSRQI KISAIIDRQT IEGIGSNNWV LAGSLSQTGK PLLANDPHLG LTAPALWYHA
     HLKTTDGSLN AIGATMPGVP YIALGRNDRI AWGFTNTAPD AQDLYVEKIT REGFYKTPDG
     ELPFITRQEV IKIKGQDDYI LTTRATRHGP VLSDRLANVA KLLGDQHVLA LRWTALDNDS
     LSLEASANIA TAQNWQQFLA NAKNLKAPQQ SIVYADVDGN IGLIAPGAVP IRHPDNELYG
     QYPSPGWLAK YDWQGYIPFD ELPQKFNPAK NYIATANHKI IDDDYKHYIA SKWTLPYRYN
     RIVKLLEAKP KHNLDSLKTI QLDQYSNFLE IMRPILDKAL SQQPLADPDA IKAYELVKQW
     DGRATAESRE MLILTLWIRN LQSVILTPEF DKLRSRNHQF LIDVLNDKDG MSRWCGXLAK
     QDGNAETCAI LVSQTFYITT QQITKQLGVN MQNWQWGKVH QAVGEHRIFD KVPLLNRLFN
     LSTPIGGGKM TINVATFGLS DSDDLEKIFK NNVGPSLRHL FDLSDLEKSR YIHSSGQSGN
     VFSPYYADYM PLWAKGDFIP MTMLKANYLP NAIGSLELIP Q
//