ID   A0A0F4JSF9_9ACTN        Unreviewed;       992 AA.
AC   A0A0F4JSF9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KJY36693.1};
GN   ORFNames=VR44_07455 {ECO:0000313|EMBL:KJY36693.1};
OS   Streptomyces katrae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY36693.1, ECO:0000313|Proteomes:UP000033551};
RN   [1] {ECO:0000313|EMBL:KJY36693.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY36693.1};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJY36693.1}.
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; JZWV01000145; KJY36693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4JSF9; -.
DR   STRING; 68223.GCA_002028425_02981; -.
DR   MEROPS; S45.003; -.
DR   PATRIC; fig|68223.7.peg.3966; -.
DR   Proteomes; UP000033551; 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          255..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        345
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         423
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         426
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   992 AA;  106446 MW;  E7670614F91C517D CRC64;
     MPAKESGPSV KKKGRRARLL VLVLVLALLA GLGYGAYWSV DTVRASFPQT TGSLKVPGLT
     GTVDVKRDEH GIPQLYADND EDLFRAQGFV HAQDRFWEMD VRRHMTSGRL SEMFGSGQVE
     TDAFLRTLGW RQVAQEEYDK KLAPETKKYL QAYADGVNAW LKGKSGKDLS VEHAALKISS
     DYKPEQWTPV DSVAWLKAMA WDLRGNMQDE IDRSLMSNKL TQAQIDELYP AYPFDRNKPI
     VEGGTVAGGK YAPQGTAGAG SSSTGTGATG TAAGAGTGTG STTGTGAGTG SQATPNGGTN
     PATGLADNAS AQGAAVGLRT QLTALSKTLD DIPAILGPNG SGIGSNSWVV SGKYTTTGKP
     LLANDPHLSP QLPSVWYQMG LHCRAVSAKC QYDVAGFTFS GMPGVVIGHN ADIAWGMTNL
     GADVTDLYLE QVRPEGYVYD NKVVPFTIRE EEIKVAGGKS KKITVRTTNN GPLISDRSEQ
     LETVGSRAPV PSSAPDRGTG YAVALRWTAL DPGKSMDAVF KLDRAKDFAS FRAAAADFEV
     PSQNLIYADN KGPSGNIGYQ APGRIPVRGQ GDGRMPAPGW DPKYAWKGGR DGNAGYIPQN
     ELPWELNPQR GYIVTANQAV TESAPATAAG AGSATGTGAA TGAGTGTAAG ASGPAGAGKY
     PYVLTTDWGY GARSQRINDL IEAKIKDSGK ISTDDMRTMQ MDNSSEIAAL LTPMLAKIPV
     SDPDVRSAQK LLEGWNYTQE NDSAAAAYFN AVWRNILKLA FGDKMPKELR VTDSCMNVIE
     EGTGPNDDLA KTVRECGTRG PDSAQPDGGD RWFEVVRRLV KDEKSPWWTA TPKTVHDKPI
     KTRDELFARA MEDARWELTA KLGKDQSTWS WGRLHQLTLK NQTIGKEGPG FMQWILNRGP
     WNLGGGEATV NATGWNASSG YDVTWVPSMR MVVNLNDLDK SRWINLTGAS GHAYDGTYTD
     QTTLWAKGEL LDWPFGKDAV DKSTVDTLTL KP
//