ID   A0A099G8K5_9RHOB        Unreviewed;       919 AA.
AC   A0A099G8K5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Penicillin acylase {ECO:0000313|EMBL:KGJ18942.1};
GN   ORFNames=IX56_16480 {ECO:0000313|EMBL:KGJ18942.1};
OS   Paracoccus sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ18942.1, ECO:0000313|Proteomes:UP000029858};
RN   [1] {ECO:0000313|EMBL:KGJ18942.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ18942.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ18942.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ18942.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-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   -!- 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:KGJ18942.1}.
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DR   EMBL; JRKQ01000143; KGJ18942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099G8K5; -.
DR   Proteomes; UP000029858; Unassembled WGS sequence.
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   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
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; 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; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029858};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          580..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..610
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         350
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         353
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   919 AA;  95192 MW;  8FD3290B512AE93F CRC64;
     MLTLFRWLVR LTIGLILGLV AAVALVWYFA VRSLPGYDES FDLAGIEQPV EIVRTTEGVP
     HILAQTDHDA FFALGLAHAQ DRLFQMVVLR RAAQGRLAEL FGTRAYASDD LARRLGLWRT
     AQASLTAQDE ATQAALKAYA DGVNAWVEQV NSGARGRGAP EFFLLPGDIT YWQPADSLAI
     LKLIAAGATT QAVAEIERAQ VSLAVPERAA DLVGAAGEPP LPAYAALFGE GALFQPLAPG
     GAEGARGDAA RASGSQDAAA AWAARLLGYV PLFEGTSANA FAAVAERTAA GAPILANDPH
     VALTAPSLWY LARMDLRAGS VIGGTIPGIP AVLSGRNPTL AWGLTPAAID DQDLVMEEVQ
     PGAPDRYLGP GGWRDFVTTH EIIRVRDAEP RRITLRESLA GPVIPPAHLG LASVTPAGFV
     PALRWTGLAT DDRTMSALVA LMAAPDRAAA RRAVEAVVAP AVEVTLADKA GVAQVLAGAI
     PIRGDHPTGG RMPAPGSDPR TTWQGLVPPG DPRRETQPAQ GLVAATGGEI PGSAVAVGAA
     APGAAPAGGA TAVPIGAIGA PSLGTASGVG AVAAAPATAA GGAAPAPTPL NTDQPAPAQP
     AAPAPAGPAT APATGPLALG FDRDDPLRLA RLRRLLAARE IHSRDSFIDA QLDTVSPAAR
     ALLPLVGADL WFTGEPAPPG TPERQRQDAL GLLAEWDGNM GEHLPEPLIY AAWMAALQDR
     LVHDELGALA PVVAGRLRPA FIDRVFRNTG GAGVWCDVVQ SAPVEDCVTI ARRALDAALV
     DLTARFGPDV TSWRWGDVHA ARHLHPALGR MPGVAWVVNL VQSISGDGSS LARAGTLGEG
     ADPWQAVTGA GFRGVYDLAD PDSSVFVIST GQSGHPLSRH YDDVAERWRR GEYIAMSLDP
     TLARAGASGV TWLRPAKAE
//