ID   A0A1W6D122_9RHOB        Unreviewed;       865 AA.
AC   A0A1W6D122;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:ARJ70832.1};
GN   ORFNames=B0A89_08820 {ECO:0000313|EMBL:ARJ70832.1};
OS   Paracoccus contaminans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ70832.1, ECO:0000313|Proteomes:UP000193017};
RN   [1] {ECO:0000313|EMBL:ARJ70832.1, ECO:0000313|Proteomes:UP000193017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC   {ECO:0000313|Proteomes:UP000193017};
RA   Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT   "Genome sequence of Paracoccus contaminans isolated from a water
RT   microcosm.";
RL   Submitted (MAR-2017) 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; CP020612; ARJ70832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6D122; -.
DR   STRING; 1945662.B0A89_08820; -.
DR   KEGG; pcon:B0A89_08820; -.
DR   Proteomes; UP000193017; Chromosome.
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:UP000193017};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   REGION          245..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        327
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         399
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         402
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   865 AA;  93112 MW;  898DEC869A3001D1 CRC64;
     MLTPGLFGLG LILAGWPACA ELPSSVRREQ ASVAGLEQPA EIIVDQWGVP HIYAGTDRDA
     LFLQGFNAAR DRLWQIDLWR KRGLGRLSES FGQSFVAQDR AARMFLYRGD IEKEWAAYGP
     NGKTYAEAFV AGINAYVQQV LDARQPLPVE FELTGSRPEL WSPEDVVRIR SHGLTRNASS
     EVARARMTCA KGLEADRLRQ KLEPEWTPSI PEGLDPCTIP EDVLKDYELA TQNVKFEAAK
     AEGDAAKADA PAPDAAAKPA GGSAPAAAPA QAAGAAAPAA DAAPAAAAPA GPAPTHENNQ
     SSGDKRSDAD PASFLRVTSA NVQEIGSNNW TIAGSRTETG RPMLANDPHR AHGVPSLRYV
     VHLNGPGMSV IGAGEPALPG ISIGHNGKIG FGLTIFAVDQ EDLYVYELNP ENPNQYRYKD
     GWADMEVIED TVAVRDGQPE KVTMKFTRHG PVLKVDEANH RAYAFRSVWF EPGTSAYFGS
     VDYMGARNWE EFSTAMERFS APSENQVYAD TEGNIGWIVG AMSPLRQNWD GLLPVPGDGR
     YEWEFLDRKK LPSVYNPPEG FFATANQMNL PEGYPYKENK VGFEWSDPAR FDRITEVLSK
     DDKVSLADSM ALQNDDHSMV QRRMVALFKG LTLPDDAAQA DRDALALIQG WDGVTAADSA
     AAAVAEVLLS KHLVKTAGPR LVGDDMAKLL GRGAITSIVD LLDAPDGRLG ADPAKARDEI
     LAKALAGAVA EVTEALGPDQ KAWRWGDLHK GKFTSSVASL ARPGLASQLN VGPLSMGGSA
     FSPRAASYND KFEVTSGASF RMVLDVGNWD ASRFINTPGQ SGDPMSAHYR DLAPLWAAGD
     YAPLVYSRQA VEAAAEKVIS LTPGN
//