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Database: UniProt
Entry: A0A1S2K2T6_9ACTN
LinkDB: A0A1S2K2T6_9ACTN
Original site: A0A1S2K2T6_9ACTN 
ID   A0A1S2K2T6_9ACTN        Unreviewed;       743 AA.
AC   A0A1S2K2T6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:OII62352.1};
GN   ORFNames=BJP40_28690 {ECO:0000313|EMBL:OII62352.1};
OS   Streptomyces sp. CC53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII62352.1, ECO:0000313|Proteomes:UP000179639};
RN   [1] {ECO:0000313|EMBL:OII62352.1, ECO:0000313|Proteomes:UP000179639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC53 {ECO:0000313|EMBL:OII62352.1,
RC   ECO:0000313|Proteomes:UP000179639};
RA   Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT   "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT   transport.";
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}.
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:OII62352.1}.
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DR   EMBL; MKXB01000157; OII62352.1; -; Genomic_DNA.
DR   RefSeq; WP_071281244.1; NZ_MKXB01000157.1.
DR   AlphaFoldDB; A0A1S2K2T6; -.
DR   STRING; 1906740.BJP40_28690; -.
DR   Proteomes; UP000179639; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179639}.
FT   REGION          316..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         243
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   743 AA;  78639 MW;  F6C58F4B7168F452 CRC64;
     MSIEVYRDPW GIPHLRADDP RELARAQGRT TAHDRAWQLE VERHRTQGTT AAFLGPDAVE
     WDVFARRARL ADTARRCFDR LDDDTRAWVG AYVDGVNAGL AEGARRSPEF ARTGLEPGGW
     EPWVPLAVWL STHILFAGFP TKLWREEVAR CLGDDSAALF ATDGPGTSGS NGWLVTAART
     ATGSAVVAGD PHRFIEAPGV YQQIRLACPQ YDVVGLAVPG VPGLAHFGHT GTVAWAITNA
     MADYQDLYRE QLRRTVDGGV EALGPDGWRP ARTHTETVEV KGAAPVTVEV VETDRGPVII
     PDPGVRAPAE TTGTALLAPA TGPCTGPGSG SGTAAGPPAE AFPDREGDAE PGGAGGGGAP
     PAGGAISLRY PPRVTGDLGF AALPALLAAA TVDDVDRAVD RWVEPVNVVQ AADTLGGTLH
     RVAGHVPVRD RANMLRVVPA WEPRHAWSGL REPLPRAAVD GVAVMANERG LAAPLGVEFA
     PPHRARRIAE LLGASRDWDA AGMRAVLTDT QLASARPLLA LAAGLDAAAL TPPAAALRDR
     LLRWDRRMDA DSVDAAHYAA VRAAVVRRVA AHPVFAGLAA PPAYPALFQP WLSLTARVAY
     ALETLLTGGP VPPADREGAV RDALEEVAAA PPEGPWGASH RLAPWAAVPD PEDEPRWPGL
     DGDQDCVLST SSVPGLTDRS ARGPAARYVW DLARRDDSLW VVPFGASGVP GAPHHRDQLP
     LWLRGGLVPV TTDWNRLSKE QPA
//
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