ID   A0A1M5MJA4_9GAMM        Unreviewed;       799 AA.
AC   A0A1M5MJA4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SHG77295.1};
GN   ORFNames=SAMN02745129_0663 {ECO:0000313|EMBL:SHG77295.1};
OS   Ferrimonas marina.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=299255 {ECO:0000313|EMBL:SHG77295.1, ECO:0000313|Proteomes:UP000184268};
RN   [1] {ECO:0000313|EMBL:SHG77295.1, ECO:0000313|Proteomes:UP000184268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16917 {ECO:0000313|EMBL:SHG77295.1,
RC   ECO:0000313|Proteomes:UP000184268};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC       from the same precursor. {ECO:0000256|ARBA:ARBA00038735}.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; FQXG01000001; SHG77295.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5MJA4; -.
DR   STRING; 299255.SAMN02745129_0663; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000184268; 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   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
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:UP000184268};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   799 AA;  87860 MW;  F51C9D74826E626B CRC64;
     MEASVGRLEA WSVTRWLKRT LISLLILLLL AAAGLYAVIA GSKGKLSGEV SVAGLEQPVS
     IHLDDLGRPH VQAQNLADAL AAQGYLHGSE RLWQMELFRR AGQGRLAALF GSDMVEADIE
     LWRMGVPQLG QQLQQHASDS MKQWVTAYVA GINQAIELQR SRPLELWLLQ GEISPWTESD
     VFAVGALIAF NSANNHKNEL LRLALAQALT PAQFERFLDD GSDTAGFPFI LAGEGESQAL
     LSPSAMLDPM DNPNIPRLRF GSNGWVVAPD KTAEGQALFA FDSHDYLGLP NLFYEVHLHF
     GQQQIRGWSV PGLPGVINGY NDKIAWGFTN IGDTQDLFIE TRHPDKPDHF LLDGQWLPAE
     VSQHSLPVKG SAPVAFTITR THNGPLIREE PLLSFRWTMH QFDQFADSGM GLEGLLMLNL
     ATDWDSFTAA IDRHAAPTLN ATYADSDGNI GFRTAGLIPE RGLGEGLYPL DGSRSEHQWQ
     GMVPVTEMPR RYNPPEGFLA AANARVNPRG VGPMVSADNA APYRIARLQQ VLAEDNAITF
     EQMQRWQMDW HDGQAQALLP ALLRQAQAGG VDQDARFAEG ISLLKAWQTQ PLADTDSAAA
     LIFQQWYLQI ADAVFAQPLG EFLYGQLLKR NYVLNFALDG LILEAEDPQW WVEGRDDMVA
     NALAHTLASL HGELGGEPRT WRLDQKQSVA LPHEIGKAVP ALGRWLNGEQ QPWGGTPAAV
     GRASYRYDRP FKVSHGATVR VVAQMGEQVK AASVIPGGQS GHPLSPHYRD QYDLWREGQL
     IPVEDAPASA PQLTLLPLE
//