ID   A0A1M3R216_9SPHI        Unreviewed;       815 AA.
AC   A0A1M3R216;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:OJY98271.1};
GN   ORFNames=BGP13_11570 {ECO:0000313|EMBL:OJY98271.1};
OS   Sphingobacteriales bacterium 40-81.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895835 {ECO:0000313|EMBL:OJY98271.1, ECO:0000313|Proteomes:UP000184064};
RN   [1] {ECO:0000313|EMBL:OJY98271.1, ECO:0000313|Proteomes:UP000184064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=40-81 {ECO:0000313|EMBL:OJY98271.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJY98271.1}.
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DR   EMBL; MKWF01000010; OJY98271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3R216; -.
DR   STRING; 1895835.BGP13_11570; -.
DR   Proteomes; UP000184064; 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   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         356
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   815 AA;  91662 MW;  E04C5434CE84DEA0 CRC64;
     MRIVFFCISL LVTALLLFAL GTTTWTPLAL GNFLSPQHGI WQNAEPAKQS FDATLHFPEL
     KGNTTVYLDE RLVPHIVADN DEDAYFIQGY LHAKFRLWQM EFQTYAAAGR ISEIVGDVAK
     DYDRGKRRLG MVYAAENLLK EIEADPVSKA EVDNYTAGVN AYIATLTESR LPVEYKLLGY
     APEKWNNLKT ALFVKQMTET LAGFENDLPM TKALAYFGDA KLRLLFPQIA DALDPVIPKG
     TVYPEATVHP IPPASKDSLY IQPDTTTVQG KLKEINKPNP ANGSNNWAVS GNKTQSGAPI
     LCNDPHLTLS LPSIWYEIQM ITPTMNAYGV SFPGAPGVII GFNDSVAFGF TNSGRDVKDY
     YSIQFKDETK TQYRFGNDWK SADLRIEEIK IKGKPPIYDT VAYTVFGPVT YDNSFPASEM
     PGKALAARWK AHDPSNELLL WHYLDRAKNY EDYENALQYF TCPAQNVAFA SKSGDIAIWQ
     QGTFPARWNR QGVYAMPGED SSYMWQTFIP RSENPHVLNP ERGFISSANQ RPADSAYHYF
     IPGEYDLYRG IEINRRLAAM SNITPQDMMK LQNDNYNAFA ETALPLLLNY ITQSSLEGMA
     NQYLDTIKNW SLNNDINLTA PTLFTLWFKN LERQVWDDEF EKAGVDKMRP SQPTLIEALL
     KDSAFAFADN INTPQTETIS DAVNVAFAKT VATADSLASV NKLTWGMYKN TSIYHLLKTK
     VMPFARTGLM VGGGKHVINA TQHDHGPSWR MIVHLTRDTE AYVVYPGGQS GNPGSPYYDN
     FIDKWAAGEY YKAWIMKKGE EGSDRLVWKM IFKKG
//