ID   A0A1G9W1T1_9ACTN        Unreviewed;       928 AA.
AC   A0A1G9W1T1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SDM78502.1};
GN   ORFNames=SAMN04487981_102563 {ECO:0000313|EMBL:SDM78502.1};
OS   Streptomyces sp. cf386.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDM78502.1, ECO:0000313|Proteomes:UP000198720};
RN   [1] {ECO:0000313|Proteomes:UP000198720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FNHV01000002; SDM78502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9W1T1; -.
DR   STRING; 1761904.SAMN04487981_102563; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000198720; 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   Reference proteome {ECO:0000313|Proteomes:UP000198720};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        319
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         397
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         400
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   928 AA;  101462 MW;  0765A2C5D487C245 CRC64;
     MPPNTTASTG QQPGKSGRKK GRRARLIVLV LALALIAGVT GGAYWSISTV RASFPQTKGS
     ISLDGLSGPV DVKRDDYGIP QIYASSDEDL FMAQGYVQAQ DRFYEMDVRR HMTSGRLSEM
     FGKSQVENDE FLRTLGWDRI AQEEYDKTLS ASTKKYLQAY AKGVNAYLDG KDNKDISLEY
     AALGFANDYK PAKWTPVDSV AWLKAMAWDL RGNMQDEIDR ALMTSRLGPK EIADLYPGYP
     YSRNKTIVQS GQYDEITKTF EQGGSASTAG SSTGGSTSGS TGTASSSAAN GLQSQLAGLQ
     DVLDGLPTAV GVNGNGIGSN SWVVAGKHTI TGKPLLANDP HLSASLPSVW YQMGLHCRAV
     SSKCQYDVSG YTFAGMPGVI IGHNQNISWG MTNSGVDVTD LYLEKLSGDG YLYDAKTVPF
     KTREETIKVA GGESKKIVVR ETNNGPLLSD RSSELVKVGK KASVNTAAPD RGDGYGISLR
     WTALDPGTSM DAVFAMNKAA DWNDFRAAAT LFDVPSQNLV YADTKGHIGY TLPGKIPTRA
     SGYDGSVPAP GWDSKSRWTG YIDDDELPYE YDPSRGYIVT ANQAVVDKTK YPYTLTTDWG
     YGSRSQRITD LIQSKIDDGG KISTDDMRQM QLDNSSEIAK LLVPKLLKID IDDKKVRDAE
     DVREAQELLE GWDYTQDADS AAAAYFNSVW RNILKLAFGN KLPKELRVKG QCLLVDPVNT
     TGPADQTDKV RECGERDADQ AQPDGGDRWF EVVRSLMDDE DSDWWTTPSS GNRPGATNRD
     DLFMRAMVDA RWELTAKLGK DIDTWSWGRL HRLFLKNQTL GTEGPGFLQY ALNRGPWKLS
     GGEATVNATG WNAAGGYGVV WVPSMRMVVN LGDLDKSKWI NLTGASGHAY NAHYTDQTDK
     WADGELLDWS FSDGAVDEST EDTLVLRP
//