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Database: UniProt
Entry: A0A0M8SKP2_9ACTN
LinkDB: A0A0M8SKP2_9ACTN
Original site: A0A0M8SKP2_9ACTN 
ID   A0A0M8SKP2_9ACTN        Unreviewed;       952 AA.
AC   A0A0M8SKP2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KOU34593.1};
GN   ORFNames=ADK51_06725 {ECO:0000313|EMBL:KOU34593.1};
OS   Streptomyces sp. WM6368.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415554 {ECO:0000313|EMBL:KOU34593.1, ECO:0000313|Proteomes:UP000037718};
RN   [1] {ECO:0000313|EMBL:KOU34593.1, ECO:0000313|Proteomes:UP000037718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6368 {ECO:0000313|EMBL:KOU34593.1,
RC   ECO:0000313|Proteomes:UP000037718};
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:KOU34593.1}.
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DR   EMBL; LGDA01000036; KOU34593.1; -; Genomic_DNA.
DR   RefSeq; WP_053701846.1; NZ_LGDA01000036.1.
DR   AlphaFoldDB; A0A0M8SKP2; -.
DR   PATRIC; fig|1415554.3.peg.1410; -.
DR   Proteomes; UP000037718; 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; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2}.
FT   REGION          246..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         410
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         413
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   952 AA;  102836 MW;  F3AE0BDFA6F97CB5 CRC64;
     MPANETAPPV KKKGRRARLI VLVLVLALVA GLGYGAYWSV DGVRASFPQT TGQLKVPGLT
     GTVEVKRDAR GIPQLYADSD DDLFRAQGFV HAQDRFWEMD VRRHMTSGRL SEMFGSGQVE
     TDAFLRTLGW RQVAQAEFDT KLSPETKKYL QAYADGVNAY LKGKSGKDLS VEHAALKLSD
     DYRPEQWSPV DSVAWLKAMA WDLRGNMQDE IDRALMATKL SQAQIDELYP PYPFDRNKPI
     VEGGKVDGGK YTPQGGAAGG GNGTGTGTGS GSGNAVGTQT VTPTGTGAGT GLADNATAQG
     ATVGLRTQLT ALSDTLDKIP AILGPNGSGI GSNSWVISGK YTTTGKPLLA NDPHLSPQLP
     SVWYQMGLHC RTASAQCQYD VAGYTFSGMP GVVIGHNADI AWGMTNLGAD VTDLYLEQVK
     PEGYVYDNRV LPFTTREEVI KVAGGASKKI TVRTTNNGPL VSDRSEELGT VGTRAPVASA
     APDRGDGYAV ALRWTALDPG RTMDAVFKLN RAKDFPSFRA AAAEFDVPSQ NLIYADNKGA
     SGNIGYQAPG RIPVRGQGDG RMPTPGWDSK YAWKGGKDGN TGYIPQNEMP WDSNPSRGYI
     VTANQAVVET GTGAGKYPYL LTTDWGYGAR SQRINDLIEA KIKDGGRIST DDMRTMQMDN
     SSEIAALLTP MLSKIEISDP GVRAAQKLLD GWNYTQESDS AAAAYFNAVW RNILKLSFGD
     KMPKELRLEG SCMNVLGNGT GPADDLAKTV RECGTRDADS AQPDGGDRWF EVVRRLVKDE
     KSPWWSAPAK GLNKPATTTR DQLFARAMAD ARWELTAKLG KDQSTWSWGR LHQLTLKNQT
     IGTEGPGFMQ WLLNRGPWNL GGGEATVNAT GWNASSGYGV TWVPSMRMVV NLNELDKSRW
     INLTGASGHA YNAHYTDQTT MWAKGELLEW PFGKDAVEKA TVDTLTLTPE GS
//
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