ID   A0A2B2C0N6_9BACI        Unreviewed;       394 AA.
AC   A0A2B2C0N6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:PFP25829.1};
GN   ORFNames=COJ96_18910 {ECO:0000313|EMBL:PFP25829.1};
OS   Bacillus sp. AFS073361.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP25829.1, ECO:0000313|Proteomes:UP000223997};
RN   [1] {ECO:0000313|EMBL:PFP25829.1, ECO:0000313|Proteomes:UP000223997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS073361 {ECO:0000313|EMBL:PFP25829.1,
RC   ECO:0000313|Proteomes:UP000223997};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PFP25829.1}.
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DR   EMBL; NUZU01000037; PFP25829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B2C0N6; -.
DR   OrthoDB; 9776731at2; -.
DR   Proteomes; UP000223997; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd08021; M20_Acy1_YhaA-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF166; AMIDOHYDROLASE YHAA-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:PFP25829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223997}.
FT   DOMAIN          191..283
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   394 AA;  43518 MW;  F77E1242351D2F40 CRC64;
     MSITTTVNLN QLAEETKEQV IAWRRHLHQN PELSFQEEKT SQFIYDTLQS FGNLEISRPT
     KTSVVARLIG AEPGKTLAIR ADMDALPIQE ENTFEFASQT PGVMHACGHD GHTAMLLGTA
     KILSGLKDHI KGEVRFLFQH AEELFPGGAE EMVQAGVMDG VDLVIGTHLW SPIEKGKVGV
     VYGPMMASPD TFWITVNGKG GHAALPHQTI DSIAVAAQVV TNLQHIVSRN TDPLDSLVIS
     VTQFLAGTTH NVIPGSVKLW GTVRSFDSTL RESIPAKMER VVKGITEAHE ASYEFKYEFG
     YRPVINDNEV TAVIEETVRE VFGEEALDMM RPNMGGEDFS AFMEKAPGCY FYVGAGNEEK
     GITYPHHHER FTIDEDALEI GVKTFLHATF KFLA
//