ID   A0A069K1S5_9ACTN        Unreviewed;       914 AA.
AC   A0A069K1S5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KDQ67812.1};
GN   ORFNames=DT87_11510 {ECO:0000313|EMBL:KDQ67812.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ67812.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ67812.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ67812.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-2014) 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:KDQ67812.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JJOB01000001; KDQ67812.1; -; Genomic_DNA.
DR   RefSeq; WP_037877667.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069K1S5; -.
DR   MEROPS; S45.003; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000027475; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        310
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         388
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         391
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   914 AA;  100601 MW;  1CBF5D7906BFAAA7 CRC64;
     MPANTTAPSG SSDAKKKGRK KGRRARLLVI VLVLALVAGV GYGAYWSVST VRASYPQTTG
     TLELKGLTGD VDVKRDAYGI PQIYADSDAD LFRAQGFVQA QDRFWEMDVR RHMTSGRLSE
     MFGSGQVDTD AFLRTLGWRK VAQEEYDKVL DKDTKKNLQA YAEGVNAYLE GKDGKDISVE
     YAALGLTNDY KPTEWTPVDS VAWLKAMAWD LRGNMQDEID RSLLTSRLTE KQIGDLYPEY
     PYKKNKPIVQ KGAVSPVTGE FDPEAEPSEN IGGDTATDAA EGLNTQLSAL SRTLDEIPAL
     LGPNGNGIGS NSWVVDGKHT TTGKPLLAND PHLAPMLPSL WYQMGLHCRE VSKDCRYDTA
     GYTFSGMPGV IIGHNQDIAW GFTNLGADVT DLFLEKVSAD GYQYEGKTKA FDTRDETIKV
     AGGKSRKITV RETNNGPLVS DRSSEMAKVG KKAPVANAAP DRGDGYAIAL KWTALEPGKS
     MDAVFELNRA KDFKSFRAAA SHFEVPSQNL IYADTEGNIG YQAPGKIPVR LKGDGTMPSP
     GWSSEYGWEK DPIPFDELPY EYNPKRGYIV TANQAVIDDS YQHMLTKDWG YGTRSQRIND
     LIQKKIDDGG KVSTDDMQSM QMDNQSAIAA KLVPKLLKIN ISDTSIREAQ KLLEGWDYTQ
     ESDSAAAAYF NGVWRNILKL AFGNKLPKEL RAKGDCIYVR PAAGSGPVDE QDKFVRECGQ
     RAPDAAQPDG GDRWYEVVES ILDDTDNEWW KAPAQGREKA IDGRDELFAR AMEDARWELT
     AKLGKDISTW SWGRLHQLTL RNQTLGTEGP DLLQRALNRG PWNLGGGEAA VNATGWNAAG
     GYGVIWVPSM RMVVNVGDWD KSRWINLTGA SGHAFSAHYT DQTDKWVNGE LLDWSYGTGA
     VDSATVDTLT LKKP
//