ID   A0A1Q3WJB1_9BACT        Unreviewed;       790 AA.
AC   A0A1Q3WJB1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:OJW75176.1};
GN   ORFNames=BGO59_17930 {ECO:0000313|EMBL:OJW75176.1};
OS   Spirosoma sp. 48-14.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW75176.1, ECO:0000313|Proteomes:UP000186057};
RN   [1] {ECO:0000313|EMBL:OJW75176.1, ECO:0000313|Proteomes:UP000186057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=48-14 {ECO:0000313|EMBL:OJW75176.1};
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:OJW75176.1}.
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DR   EMBL; MKUD01000037; OJW75176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3WJB1; -.
DR   STRING; 1895854.BGO59_17930; -.
DR   Proteomes; UP000186057; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 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   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   790 AA;  89156 MW;  59D3088159F3C976 CRC64;
     MLLRFTLFLL FVSIGCVRQS DKVRQLPGLQ EPVDIVRDKW GVNHIYAKNE HDLFFAQGYS
     AAQDRLFQLE MWRRQATGTT AELLGPQELK RDIGARLFRF RGNLDDELRQ YHPHGPQIVR
     AFVDGINAYI NTILKTPDQL PFEFQVLRTK PGLWTPEVVV SRHQGIMANV RDELNYGRLV
     HLLGPDKVRA LQWFHPTSKP NEPDLTLHVN GDELFQPILE LYEAFRLPLK YKGVLSKADE
     DEALQFDSGR WFDTEKQYTG SNNWVISGAK SASGFPMLAN DPHRSQATPS LRYWVHLDAP
     GWHVVGAGEP TLPGISIGHN EYGAWGLTIF ETDNEDLYVY ETNPANPNQY RYKGAWVDMK
     TLTETIPVKG GKPVNAILKY TQHGPVVFDD TVHHKVYAVR AGWLEPGCAP YLASLRMNQA
     RNWAEFRQAC LQSRVPGENM IWAERPVDGK AGNIGWQVVA LSPVRPNYTG LVPVPGDGRF
     EWNDYLPIQQ LPNALNPPEG YIVTANNNLL PPDYPYRNAV GWTWASPSRA DRIKEVLNDG
     EPKSLNDFKA LQADYLSIPA RMIVPLLQQS TSANPQTQRA LTYLRRWDYR LDPNSIAATI
     FIAWDDALKA AVYEEKVPAK ARPYLKSLPT SRVTEALLQP GSHRDSLLIR CLDKAVTGLT
     EQLGPNMASW QYGQPKFKHI TITHPLSGLV DKGMQKRINL GPMARGGYGE TVNATSFDLN
     QTHGASFRIL VDTQDWDKTL GINTPGQSGN PDSPHYSDLF PIWAKNDYFP VYFSKDKVNS
     VSEAKVVLKP
//