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
//