ID   A0A257I1G5_9BACT        Unreviewed;       728 AA.
AC   A0A257I1G5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Acylase {ECO:0000313|EMBL:OYU56095.1};
GN   ORFNames=CFE25_02310 {ECO:0000313|EMBL:OYU56095.1};
OS   Chitinophagaceae bacterium BSSC1.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX   NCBI_TaxID=2015574 {ECO:0000313|EMBL:OYU56095.1, ECO:0000313|Proteomes:UP000217121};
RN   [1] {ECO:0000313|EMBL:OYU56095.1, ECO:0000313|Proteomes:UP000217121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSSC1 {ECO:0000313|EMBL:OYU56095.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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}.
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:OYU56095.1}.
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DR   EMBL; NKJC01000001; OYU56095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257I1G5; -.
DR   Proteomes; UP000217121; 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   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; 2.
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:UP000217121};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..728
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013327815"
FT   ACT_SITE        199
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         269
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         272
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   728 AA;  82075 MW;  8B96692C0D557ACC CRC64;
     MFKYLFCLLM PLSLLAQPSQ KEITRWENTA AQVSIVRDHF GVPHIYGKTD AQTVFGLLYA
     QCEDDFKRVE MNYIEKLGRL SEVKGSAELY NDLLIRLIID STDAKKDFEN SPAWLKQLLQ
     AYADGINFYL YKHPQVKPAL LTRFEPWFQL LWTDGSIGAI DVGDVTVGEL RALYSGETNS
     TAYLPTQTKI FEEPLPSGSN GFAFGPSKTK SGNAILYINP HVTFYFRPEV AMESQEGLHA
     YGAVTWGQFF IYQGFNENCG WMHTSGYADV ADLYQEQVMP KNGGYVYSYD KQEKKVGEKT
     INIQYLENGK ILSKSFKTYF THHGPVMAKR NGQWISVRSN NRSLSAIIQS WKRTKAKGFE
     EYKQIMELRS NTSNNTVFAD SKGNIAYWHG NFIPRRDVTL NWSKPVDGST SATEWQGLHS
     LDEMIHVYNP TDGWLQNCNS TPFTVAGTKS PLREKYPRYM ATDGENFRGI NAVKIWGTTE
     KYNIDDVIKN AYNSHLAAFD LFIPALISAN EKYGSAPRFA SLQAAISLLG AWNRNSSDTS
     VATTLAIEWA QKLWPAVMRQ VVEGDESNQV AKTQFFLSTS NPENLLQTLA VVISELESKF
     GTWRKPWGSI NRYQRLTGNL SESFDDNKPS LPDGFAASTW GCLPSFVSRP FPGTKLRYGY
     NGNSFICAVE FGKRVVAKSL LAGGNASDPA SSHFGDQAEM YTKGRFKDVL FYKEDVLKQA
     ERTYKPGE
//