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Database: UniProt
Entry: A0A1M5BKY0_9BACT
LinkDB: A0A1M5BKY0_9BACT
Original site: A0A1M5BKY0_9BACT 
ID   A0A1M5BKY0_9BACT        Unreviewed;       817 AA.
AC   A0A1M5BKY0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SHF43096.1};
GN   ORFNames=SAMN02745131_02629 {ECO:0000313|EMBL:SHF43096.1};
OS   Flavisolibacter ginsengisoli DSM 18119.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1121884 {ECO:0000313|EMBL:SHF43096.1, ECO:0000313|Proteomes:UP000184048};
RN   [1] {ECO:0000313|EMBL:SHF43096.1, ECO:0000313|Proteomes:UP000184048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18119 {ECO:0000313|EMBL:SHF43096.1,
RC   ECO:0000313|Proteomes:UP000184048};
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   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; FQUU01000010; SHF43096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5BKY0; -.
DR   STRING; 1121884.SAMN02745131_02629; -.
DR   Proteomes; UP000184048; 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   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:UP000184048};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         359
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   817 AA;  92908 MW;  6FCEC91BFC3A1451 CRC64;
     MLMRIIPFVI SLVVTLGLVF ALNTKIGTIP PLGKFLSPQQ GFWQNAEPCD ARLDEDLRFP
     DLKGKVKVYM DERMVPHVFA ENDEDVYFVQ GYLHAKYRLF QMEFQTHAAA GRLSEILGNN
     PQIINYDRLQ RRMGMVYGAE NELKAVAKDA LTQKVYDAYT AGVNSYINSL SAGNLPVEYK
     LLDFRPEPWT NLKIALFFKV MCSDLAGQEY AKDISFSNEK SLFSKEEMDM LYPQVSDSSV
     SIIPKGTIFE SPSVHPEIPA NADSFYLQKD SIAEPVKVPK PFEVKGSNNW VVSGAKTKSG
     APILCNDPHL RLTLPSIWYE MQLHTPTMNV YGVGFPSVPG IVIGYNDSIA IGLTNAGRDV
     MDYYQVKFKD ASRNEYWYKN QWQAAEHRIE KIKVKGGATI IDTVAYTVFG PVTYDRSFTT
     ADSNTNKALA MRWTAHDPSN EVLTLIKLNR AKNYSEYSQA IKEFACPGQN IIFGSTNGDI
     AIWQQGKFPA RWKNQGLYVM PGEDDTYSWQ GFIPQGENPH VLNPPDNFLQ SANQRAVDSS
     YPYFIPGDYY VPRGRSIYRQ LSQMQDITPQ DMMRLQGNAY STLAGDAMPL FSKYLKTNEL
     SDNELKYWEE VSKWNFEYTG QERAPTIFQT WMDSLESVIW SDEFTQASKP VTIPSEQILL
     ENLLRDSAFR FVDNINTPEK ENLYQDVTLS FKKAVGELVK NEDGVIWWKH RNTFIQHLLR
     DALPAFGRTG LMCNGWSTTI NALTKTHGPS WRMVIHLTKP IEAYGVYPGG QSGNPGSKFY
     ENFIDTWATG KYFTLWMMHE NESSDKRIIG QINFTNS
//
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