ID   F2R7N0_STRVP            Unreviewed;       912 AA.
AC   F2R7N0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:CCA56315.1};
DE            EC=3.5.1.11 {ECO:0000313|EMBL:CCA56315.1};
GN   OrderedLocusNames=SVEN_3029 {ECO:0000313|EMBL:CCA56315.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA56315.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA56315.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA56315.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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   ---------------------------------------------------------------------------
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; FR845719; CCA56315.1; -; Genomic_DNA.
DR   RefSeq; WP_015034231.1; NZ_JABVZO010000155.1.
DR   AlphaFoldDB; F2R7N0; -.
DR   STRING; 953739.SVEN_3029; -.
DR   MEROPS; S45.003; -.
DR   GeneID; 69865152; -.
DR   KEGG; sve:SVEN_3029; -.
DR   PATRIC; fig|953739.5.peg.5221; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_011790_0_1_11; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:CCA56315.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   REGION          246..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        309
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         387
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         390
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   912 AA;  100317 MW;  489AFA4EC0F4D527 CRC64;
     MPSNTTAPPA KKKGRRARLI LLVLVLALVA GVGYGGYWGV STVRASFPQT TGEIRLDRLS
     GEVEVKRDAN GVPQIYADNE TDLFRAQGYV QAQDRFYEMD VRRHVTAGRL SEMFGDGQVE
     TDAFLRTLGW RRVAQQEYDK VLSAETKKYL QAYAEGVNAY LKDRDPADVS VEYAALAFSN
     DYTIEPWTPV DSVAWLKAMA WDLRGNMQDE IDRSLMTSRL SAAQIKQLYP EYPYALHQPI
     VGQGAVDEST GKFDPKAKAT EGDGATTGDT PGNGPGGSSQ GMNSQLGALS EVLDGIPALL
     GPNGNGIGSN SWVVSGRYTT SGKPLLANDP HLAPQLPSLW YQMGLHCRSV SATCRYDVAG
     YTFSGMPGVI IGHNDKIAWG LTNLGADVTD LYLEKIGPDG YLVDGRTKPF IVRDEIIKVA
     GGEDRTITIR STDRGPLVSD RSSELEKVGQ QAPVGNAAPD RGTGYGVSLQ WTALQPGKSM
     DAIFALDRAK DFKQFRAAAK NFEVPSQNLV YADTEGHIGY QSPGKIPQRT KGDGTLPAPG
     WDSSYRWKGY IPFEQLPYEY DPERGYVVTA NQAVIDAKGY PDLLTKDWGY GSRSQRINDL
     IESKIKDGGK ISPDDMRTMQ TDNRSEIATL LNPLLLKIDI SDPYVREAQK LLEGWDYTQE
     PDSAAAAYFN AVWRNVLKLS FGNKLPKELR AEGDCINVRP ADATGPVDEQ NKLVRECGQR
     DPDSAQPDGG DRWYEVVRPL LKQEKSEWWV TPGNRTDQAT ETRDQLLARA MKDARWELTA
     KLGKDVSTWS WGRLHQLTLK NQTLGTAGPG VVQQLLNRGP WNLGGGEAAV DATGWNAAGG
     YEVIWVPSMR MVVNVGDWDK SRWINLTGAS GHAFNSHYTD QTDAWARGDL YDWAYGRAAV
     DASTKDTLKL KP
//