ID   A0A1A9C2C3_9ACTN        Unreviewed;       929 AA.
AC   A0A1A9C2C3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SBT94607.1};
GN   ORFNames=GA0115233_10968 {ECO:0000313|EMBL:SBT94607.1};
OS   Streptomyces sp. DI166.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT94607.1, ECO:0000313|Proteomes:UP000198690};
RN   [1] {ECO:0000313|Proteomes:UP000198690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-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}.
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DR   EMBL; FLSP01000096; SBT94607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9C2C3; -.
DR   STRING; 1839783.GA0115233_10968; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000198690; 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; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198690};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          257..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        326
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         404
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         407
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   929 AA;  101870 MW;  419852584C33F72C CRC64;
     MPPNTTASTG QQPGKSGRKK GRKARLVVFV LVLAIIGGVA YGAYWSISTV RASFPQTTGS
     ITLEGLSGEV EVKRDGYGIP QIYASTDEDL FMAQGFVQAQ DRFYEMDVRR HMTSGRLSEM
     FGKGQIDNDE FLRTLGWHRI AKKEYDSKLS DETKKYLQAY SKGVNAYLEG KEGKELSLEY
     AALGFANDYK PAEWTPVDSV AWLKAMAWDL RGNMEDEIDR ALLTSRLGPK QIKDLYPQYP
     YDRNKAIVQE GQLDELTGTF GQGGQTAGGS ASTDGTAAGG TTASGTGAAG TSTSGTSGLQ
     SQLSGLYGVL EDLPTAVGVN GNGIGSNSWV VSGDHTISGK PLLANDPHLS ASLPSVWYQM
     GLHCRSVSDK CQYDVTGYTF AGMPGVIIGH NKNISWGMTN SGVDVTDLYL EKLTGTGYLY
     DNKVKPFTTR EETINVAGGD SKTIVVRETN NGPLLSDRSD ELVRVGKKAE VDTSAPDRGD
     GYGISLRWTA LDPGTSMDAV FAMNKAADWD DFRAAAALFE VPSQNLIYAD TEGHIGYTLP
     GKIPTRAEGV DGSIPQPGWN SKYRWTGYIP QNELPFELDP ARGYIVTANQ AVIDKDKYPY
     TLTTDWGYGT RSQRITSLIK SKIDGGGKIS TDDMRQMQLD NSSEIAKLLV PQLLKIDIAD
     PDVREAQKLL EGWDYTQDAD SAAAAYFNSV WRNILKLAFG HKLPKEVRVK GQCLWVDPIN
     TTGPADEAEK VRECGQRDAE QAQPDGGDRW FEVVRTLMDD EDSDWWKTPR SGTRPKAENR
     DQLFKRAMID ARWELTAKLG KDIETWNWGR LHRLFLKNQT LGTEGPGFLQ YVLNRGPWKL
     SGGEATVNAT GWNAAGGYGV VWVPSMRMVV NLGDLDKSKW INLTGASGHA YSAHYTDQTD
     KWADGELLDW SFSKSAVDKS TSDTLVLQP
//