ID   A0A0M8Z615_9ACTN        Unreviewed;       721 AA.
AC   A0A0M8Z615;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Penicillin amidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ADL09_06305 {ECO:0000313|EMBL:KOX50802.1};
OS   Streptomyces sp. NRRL F-7442.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX50802.1, ECO:0000313|Proteomes:UP000037772};
RN   [1] {ECO:0000313|EMBL:KOX50802.1, ECO:0000313|Proteomes:UP000037772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX50802.1,
RC   ECO:0000313|Proteomes:UP000037772};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOX50802.1}.
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DR   EMBL; LGEH01000050; KOX50802.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8Z615; -.
DR   PATRIC; fig|1519498.3.peg.1309; -.
DR   Proteomes; UP000037772; 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   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   REGION          463..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   721 AA;  76566 MW;  639569FA7879CDBC CRC64;
     MRADSAAGLA RAQGRVTARD RAWQLEVERH RAQGTSASFL GPEALSWDRL ARRARLADTA
     RRCFTALERQ DPETAAWVRA YVDGVNEGLT TGEPAPEFAR TGLAPGRWEP WTPLGVWLAT
     HILFAGFPAK LWREHIAAHL GPEAVALFAA DGPGTAGSNG WLVSGGRTTT GHALIAGDPH
     RFIEEPGVYQ QIHLSCPEFD VVGLAVPGVP GIAHFGHTGT VAWAITNAMA DYQDLYRERL
     RRTGAGVEAL GPDGTWHRAA RHSERIDVAG EETVEVEVIE TGRGPVIAGG PEGLDDGTPA
     ALSLRYPPRV TADLGFGALL PLLRARTVAD VDRALDAWTE PVNVVQAADT GGGLLHRVAG
     RVPVRPEANG LRPVPAWEPG HEWTGWHTPP RAGLTHGVAV MANQRGPATH LGVEFAPPHR
     ADRITALLAG RERWSASDMP TIHTDTHLAS ATPLLAHIKR LTTATTQTTG TTPTTGTTPT
     TGTTPTTQTT GTAPLTQTTG AAPGTTPLTP EAAALGARLL AWDRRMDADS TDAAAYAAVR
     AAVVRRLAAH PALAPAAVAP AYPDVLQPWL ALVPRVAYAL EHLLRADDLY GVDRAATVRA
     ALEEVAADPP AGTWGDTHRL APWRALPDAT APAREPGLSG DHDCVLCTSP VPGLTDRAAR
     GPAARYVWDL ADRQNSRWVV PHGASGAPGS AHRRDQQALW LTGELVPVVT DFTRLTKESD
     D
//