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Database: UniProt
Entry: A0A0E9N1N0_9BACT
LinkDB: A0A0E9N1N0_9BACT
Original site: A0A0E9N1N0_9BACT 
ID   A0A0E9N1N0_9BACT        Unreviewed;       737 AA.
AC   A0A0E9N1N0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Putative hydrolase {ECO:0000313|EMBL:GAO43536.1};
GN   ORFNames=FPE01S_02_06410 {ECO:0000313|EMBL:GAO43536.1};
OS   Flavihumibacter petaseus NBRC 106054.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavihumibacter.
OX   NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO43536.1, ECO:0000313|Proteomes:UP000033121};
RN   [1] {ECO:0000313|EMBL:GAO43536.1, ECO:0000313|Proteomes:UP000033121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO43536.1,
RC   ECO:0000313|Proteomes:UP000033121};
RA   Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., Ohji S.,
RA   Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT   "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC 106054.";
RL   Submitted (APR-2015) 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:GAO43536.1}.
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DR   EMBL; BBWV01000002; GAO43536.1; -; Genomic_DNA.
DR   RefSeq; WP_052955759.1; NZ_BBWV01000002.1.
DR   AlphaFoldDB; A0A0E9N1N0; -.
DR   STRING; 1220578.FPE01S_02_06410; -.
DR   MEROPS; S45.002; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000033121; 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, ECO:0000313|EMBL:GAO43536.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033121};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        209
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         279
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   737 AA;  81691 MW;  62B9B01C47795444 CRC64;
     MIRWTGIILV FLGCSGGSGN HGTGTGSGAG DSLVTRADGG QSRAEIYRDK WGIQHVYGET
     DAAAVYGLIW SQCQDDFASL EEHYIERLGR QSEVYGKEWL YADLLIRLQY DSTDAQRDYQ
     QAPPEMKQLL DAFAAAVNDY LGSQDTVQAQ LLSHFEPWYP LLFPDGSYTG APSGGLTVND
     IRSLYPLPEV AGSAQLSPLR WTDNIPTGSN GFAVNGKKTI DGAAMLFINP HTSFYYRTEA
     QVASGEGLNA YGAVTWGQFF VYQGFNRHCG WMHTSSQADA ADLYAEAVTP SGSEFVYRYD
     RQTRPVAEKK IVLRYREKKD IKETVVRTFR THHGPVVGAR NGKWLSLRMP EQGLKALAQS
     WLRMKADGLK SFTTVLNLRT NTSTNTVYAD DSGNIAYWHG NGIARRDPEF DWSSPIDGSI
     AATEWKGQHE LNELIHFLNP PGGWLQNCNS SGFTAAGRPG LSSSAFPGYM STEGENFRSL
     HLQQLLQAVT TGGPETFQHI GFDRRLSAFD SLLPPLFQAW DARNKSGAGG RQPDSSAGNK
     TFDLSVAEAI DSLRRWNREA DTNSVATTIA IEWAGILFNL LPQPANAFYD QEALYRLLEQ
     TIPPETQLKK LEEVISFLQR HFGTWKIQWG SINRFQRQPR GEPFLDDQPS VAVPFAPGLF
     GCLPAFETTW QGTKKGYGIA GNSFVALVHF SKPLRAWSSF TGGHAEDPRS AHFTDQVELL
     QKGKLKDVIF LPGGRKE
//
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