ID   A0A2C1YN62_9BACI        Unreviewed;       371 AA.
AC   A0A2C1YN62;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:PGV46643.1};
GN   ORFNames=COD92_29745 {ECO:0000313|EMBL:PGV46643.1};
OS   Bacillus sp. AFS037270.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV46643.1, ECO:0000313|Proteomes:UP000225442};
RN   [1] {ECO:0000313|EMBL:PGV46643.1, ECO:0000313|Proteomes:UP000225442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS037270 {ECO:0000313|EMBL:PGV46643.1,
RC   ECO:0000313|Proteomes:UP000225442};
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   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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:PGV46643.1}.
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DR   EMBL; NUNF01000098; PGV46643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1YN62; -.
DR   Proteomes; UP000225442; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:PGV46643.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
SQ   SEQUENCE   371 AA;  41968 MW;  85FE3E95DF5C3A47 CRC64;
     MKDPRIEKLA RNLINYSVQL QKGEKVLIEN FGLQRELVTA LVKEAYAAGG YPFVLLKDHQ
     VDRSLLMGAQ EEQFNMMAEF EANVMRKMDA YIGLRSGDNI SEQSDVPDEK MKIHGNTIGK
     KVHRDIRVPK TKWVVLRYPT SSMAQLAKMS TEAFEDFYFN VCNLDYAKMD QAMDSLVELM
     NRTDKVHITG PGTDLRFSIK DIPAIKCAGR LNIPDGEVYT APVRDSVNGV ITYNTPSPYQ
     GFTFENVELT FKNGKIVEAV SNDSDRINKI FDTDEGARYV GEFAIGVNPF ILTPMQDILF
     DEKIAGSFHF TPGQCYDDAF NGNHSNIHWD MVNIQRGEYG GGEIYFDDVL IRKDGLFVLP
     ELDVLNPNNL K
//