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Database: UniProt
Entry: A0A0B4R869_9BACL
LinkDB: A0A0B4R869_9BACL
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ID   A0A0B4R869_9BACL        Unreviewed;       788 AA.
AC   A0A0B4R869;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Penicillin acylase {ECO:0000313|EMBL:AIY04349.1};
GN   ORFNames=Plano_0384 {ECO:0000313|EMBL:AIY04349.1};
OS   Planococcus sp. PAMC 21323.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY04349.1, ECO:0000313|Proteomes:UP000031496};
RN   [1] {ECO:0000313|EMBL:AIY04349.1, ECO:0000313|Proteomes:UP000031496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY04349.1,
RC   ECO:0000313|Proteomes:UP000031496};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT   "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT   Antarctica.";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009129; AIY04349.1; -; Genomic_DNA.
DR   RefSeq; WP_038702507.1; NZ_CP009129.1.
DR   AlphaFoldDB; A0A0B4R869; -.
DR   STRING; 1526927.Plano_0384; -.
DR   MEROPS; S45.003; -.
DR   KEGG; pln:Plano_0384; -.
DR   eggNOG; COG2366; Bacteria.
DR   HOGENOM; CLU_011790_0_1_9; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000031496; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031496};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        255
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         327
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         330
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   788 AA;  88079 MW;  FBFD7A85D873CC49 CRC64;
     MKGKVKNKRW LKWLLGVLGV MVILIVALLI FINVFLNKSK PFIEGEVSVE ILDNDATIIR
     DDIGVPHIKA ETDADLYRAQ GYVQAQDRMF QMDLSRRQAS GQLAEVIGAD AVDTDKFFRT
     FSLRDAAEKS WGGYDEQAQQ VLEWYAEGVN AYMKSAKADN TLSFEFSILG YEPTEWTPID
     SLTIGKFMAY DLGGHWNTLA VRHWALNEFP EDKAAELFIN YPENAPAILA ANKQQQVQVA
     GEFDASVIPP EFNGSNNWVV SGDKTASGKP LLADDPHLGL STPSIWYQMH LESPEQNVSG
     VIFAGVPGII LGHNEEIAWG VTNVGPDVQD LYIETPNPED PTQFEYEGEW EQAEVRKEPI
     KIKGEKTEDF EVLVTRHGPV VSNILYEDEK PEAVFSMQWT ALEPTLELQA VLNFNKAANW
     EEFELALEDF QAPAQNFVFA STDGTIAYKA NGRIPIRKTG DGQLPVPGNS ADYGWEGYVP
     FDELPTSVNP ESGFIATANN EVIDDSYPYH ITNFWAQPYR YERIAEVLEA SDKLTAEDMM
     ELQMDQKNLY AAEFLEDMIA TVRSNTEEHN EVLTLLEKWD QVDSKDQGAP LVFHKWIKQL
     PETLLADEFP EDVYKMLDGK NHITDEMMRD AFAGNEGVWV SEYGGAEKWL VDSLETAIAE
     IEEEQGSDVA DWSWGDHHQL TFPHPLAGAS PVFAEFLNPD SVPIGGSNIT VQAAASTPDG
     DVDHGASWRF VADLADLSSA YHIVGPGLSG HMKSDYFHNQ VDDWAQGDFH ETEIEERVEG
     STLILNAE
//
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