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}.
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; 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
//