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Database: UniProt
Entry: A0A1Y3P4F0_9PSED
LinkDB: A0A1Y3P4F0_9PSED
Original site: A0A1Y3P4F0_9PSED 
ID   A0A1Y3P4F0_9PSED        Unreviewed;       790 AA.
AC   A0A1Y3P4F0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:OUM72433.1};
GN   ORFNames=AUC60_17820 {ECO:0000313|EMBL:OUM72433.1};
OS   Pseudomonas caspiana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1451454 {ECO:0000313|EMBL:OUM72433.1, ECO:0000313|Proteomes:UP000195440};
RN   [1] {ECO:0000313|EMBL:OUM72433.1, ECO:0000313|Proteomes:UP000195440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBF102 {ECO:0000313|EMBL:OUM72433.1,
RC   ECO:0000313|Proteomes:UP000195440};
RX   PubMed=28552245; DOI=10.1016/j.syapm.2017.04.002;
RA   Busquets A., Gomila M., Beiki F., Mulet M., Rahimian H., Garcia-Valdes E.,
RA   Lalucat J.;
RT   "Pseudomonas caspiana sp. nov., a citrus pathogen in the Pseudomonas
RT   syringae phylogenetic group.";
RL   Syst. Appl. Microbiol. 40:266-273(2017).
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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OUM72433.1}.
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DR   EMBL; LOHF01000016; OUM72433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3P4F0; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000195440; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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:SF5; PENICILLIN G ACYLASE; 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   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        244
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         316
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         452
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   790 AA;  87484 MW;  788F001F544C7F75 CRC64;
     MKNALRALTI LSLLIVLSAS LYVYSKQPTR EGTVGLSHLQ RSVAVNYDDR GVPHINAENE
     TDLYRTLGYV HAQDRLFQME IMRRLARGEL AEVLGPKLLD TDKLFRSLRI RERASRYVEQ
     MDHNSASWKA MEAYLDGVNQ YQDSHAKPME FDVLGIQKRP FTAEDTFSIA GYVAYSFAIA
     FRTEPLLTYV RDELGSEYLK VFDLDWQPKG ALNLAASDWK DLGAIAQLSE QAMAGNGLPQ
     FEGSNAWAIS GNRTKSGKPL LAGDPHISFS VPSVWYEAQL TAPGFELYGY HNALVPVAFL
     GHNKDFGWSL TMFQNDDLDL IAEKVNPDNP NQVWYHDKWV DMTSSEQQIA VKGQDPVALT
     LRTSPHGPII NDVLGESAGK TPIAMWWAFL DTENPIFDGF YQLNRADTLD KVRAAAAKVQ
     APGLNIVWAN ANGDIGWWAA AQLPVRPTGV NPSFILDGST VQADKLGFYP FSTNPQEENP
     ARGYVVSANA QPASPTGMPI PGYYNLADRG QQLNAQLSDN SVRWDLESSK ALQLGTTNAY
     GPRLLAPLLP VLREVVKDPA ELRLVEQLAT WRGGYPVDST SATLFNQFLF NLTYNVFHPK
     LGDAMFESLL NTKAVDAALP RLTASPDSPW WNGHRTETVK VAWDHSLLHL KATFGDDPSQ
     WQWGKAHTLT HGHPLGSQKP LDKIVNVGPF AAPGTHEVTN NLSAQIDSAP WPVTYGPSTR
     RLIDFADAAK ALTINPVGQS GVPFDKHYSD QAETYIKGGY EKAYLNEEDV ISNRKSTLIF
     LPANAETPQK
//
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