ID   A0A0A0B5E1_9CELL        Unreviewed;       837 AA.
AC   A0A0A0B5E1;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KGM00471.1};
GN   ORFNames=Q760_08480 {ECO:0000313|EMBL:KGM00471.1};
OS   Cellulomonas cellasea DSM 20118.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM00471.1, ECO:0000313|Proteomes:UP000029833};
RN   [1] {ECO:0000313|EMBL:KGM00471.1, ECO:0000313|Proteomes:UP000029833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM00471.1,
RC   ECO:0000313|Proteomes:UP000029833};
RA   Wang G., Zhuang W.;
RL   Submitted (OCT-2013) 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:KGM00471.1}.
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DR   EMBL; AXNT01000201; KGM00471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0B5E1; -.
DR   MEROPS; S45.003; -.
DR   Proteomes; UP000029833; 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; 1.10.1400.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
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; IPR043147; Penicillin_amidase_A-knob.
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:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029833};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        266
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         344
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         347
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   837 AA;  89869 MW;  79436BE5C3FF984B CRC64;
     MLALAATAVG TVLVVREPLP QVAGRVEVPG LGAGVTVSRD ERGVPFIEAD TSGDLFRAQG
     YVHAQDRFFE MDYRRHVTAG RLSELVGENP DALEADAVIR TLGWRRVAEQ EWELLQPETR
     ENLQAYADGV NAYLDQRDRS ALAVEYSILD VRLDLADPEP WTPVDSLAWL KAMAWDLKAN
     YADELARGMA FETIGDVARV DELFPAYPQE VNLPILQASS VQPTAAAQQA TTVDLSSSHL
     QEALASAERA LSSVPNLLGE GDGIGSNSWV VSGTHTVSGL PVLANDPHLG ISAPGIWTQI
     GLHCRERSVE CPYDVSGFSF AGLPGVVIGH NGALAWGLTN LGADVTDFFL ERVSDGTALL
     DGERVPLSTR REVIKVNGGD DVEITVRSTK HGPIVSDVLD IDALGDVPVP EGSPYGRYEV
     ALGWAALTPG RTADAVFALA QASDADDVAA AAAMFEVPSQ NIVYATTDGH IGYQAPGRIP
     VRADVVDSVL PSDGSWPRPG WDSAYDWQGW VPAEQMPAVQ DPAEGFVVAA NQAVTPAGAG
     PYLTSDWDYG FRAQRIRSVL EEQIRSGEQI DVATTRSLQA DVDNPYARVL LPALLAVDVP
     DSFDDDGQDL LRTWDMRSDA DSAAAAYFAS VWSNLLELTF WDDLPEGYEP TGGARWLEVV
     RRLLETPDGS WWDDRSTVGV VEGRDEILTR ALVAARRELT ADLGKDPSDW RWGKVHTAAP
     EHDVLGSPAL PAPVRRLVNP TPREVGGGAA LVNATAWDAG SGSFGVTAAP AMRMVVDLAD
     LDSSAWVTMT GASGHPGSVH YADQLTPWAE GRLFPWPFSA DAIDEAASDV LELEPGR
//