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Database: UniProt
Entry: J0LND9_9BACT
LinkDB: J0LND9_9BACT
Original site: J0LND9_9BACT 
ID   J0LND9_9BACT            Unreviewed;       735 AA.
AC   J0LND9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Penicillin amidase family protein {ECO:0000313|EMBL:EJF10958.1};
GN   ORFNames=O71_06162 {ECO:0000313|EMBL:EJF10958.1};
OS   Pontibacter sp. BAB1700.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1144253 {ECO:0000313|EMBL:EJF10958.1, ECO:0000313|Proteomes:UP000003746};
RN   [1] {ECO:0000313|EMBL:EJF10958.1, ECO:0000313|Proteomes:UP000003746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB1700 {ECO:0000313|EMBL:EJF10958.1,
RC   ECO:0000313|Proteomes:UP000003746};
RX   PubMed=23105068; DOI=10.1128/JB.01550-12;
RA   Joshi M.N., Sharma A.C., Pandya R.V., Patel R.P., Saiyed Z.M., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of Pontibacter sp. nov. BAB1700, a Halotolerant,
RT   Industrially Important Bacterium.";
RL   J. Bacteriol. 194:6329-6330(2012).
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:EJF10958.1}.
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DR   EMBL; AKIS01000038; EJF10958.1; -; Genomic_DNA.
DR   RefSeq; WP_007654067.1; NZ_AKIS01000038.1.
DR   AlphaFoldDB; J0LND9; -.
DR   MEROPS; S45.002; -.
DR   PATRIC; fig|1144253.3.peg.1217; -.
DR   Proteomes; UP000003746; 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; cd01936; Ntn_CA; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..735
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003735893"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         283
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   735 AA;  83092 MW;  C6BA8BDE1F24B4E8 CRC64;
     MNYLFRPQVF LLLLFLFVSS CATNPKTDPA SEVAKWEEQA ARVTIMRDDF GVPHIYGKTD
     ADAVFGLLYA QCEDDFNRVE RNYMWAIGRL SEVEGEEQLY SDLRARLYMT EEEAKAEYER
     SPAWLKELCQ AFADGINYYL HTHPEVKPKL LTRFEPWMPM YFSEGSIGGD IESVSTKGIK
     AFYEEDRSLG LNSQGHGLVQ PALLEEPKGS NGFAISGKHT ASGDAMLLIN PHTSFFFRGE
     VHAVSEEGLN AYGAVTWGQF FIYQGFNEKT GWMHTSAYAD VIDEFEETIV RQDGKLFYRY
     GEELRPVETK EVTLAYKDGG ELKEKTFTTY RTHHGPITHM NGDKWVATAL MWKPVDALIQ
     SYTRTKKSNL KEFNEMMQMR TNSSNATVYA DADGNIAYYH GNFFPKRDTS FDYSKPVDGS
     NPKTDWNGLH TLDETIRIMN PPNGWIQNCN STPYTAAAEY SPKKEDYPVY MAPSPENFRG
     VHAIRLLKKA ENLTLDKLID LAYDPYLPGF EVLIPGLVKA YDAQKPNDPK LKAAIDVMRN
     WDYAVSKESV AMSLAHFYAT NLLRDGSAPK GHIMERFDYY ANTAPAAERL DIFSKTITEL
     EQDFGQWNTP WGEINRFQRL TGDIKQPFND AAPSIPVGMA SGNWGALASY GANRYDTKRL
     YGTSGNSFVA VVEFGDKVKA KTILAGGQSG DPSSPHFNDQ AARYANVEFK DVAYYREDVE
     KRAKATYKPG QKQSK
//
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