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Database: UniProt
Entry: A0A3S2W0A8_9BACI
LinkDB: A0A3S2W0A8_9BACI
Original site: A0A3S2W0A8_9BACI 
ID   A0A3S2W0A8_9BACI        Unreviewed;       305 AA.
AC   A0A3S2W0A8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:RVT56110.1};
GN   ORFNames=EM808_28310 {ECO:0000313|EMBL:RVT56110.1};
OS   Niallia taxi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT56110.1, ECO:0000313|Proteomes:UP000288024};
RN   [1] {ECO:0000313|EMBL:RVT56110.1, ECO:0000313|Proteomes:UP000288024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT56110.1,
RC   ECO:0000313|Proteomes:UP000288024};
RA   Tuo L.;
RT   "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL   Submitted (JAN-2019) 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:RVT56110.1}.
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DR   EMBL; RZTZ01000048; RVT56110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S2W0A8; -.
DR   Proteomes; UP000288024; 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:SF3; AMINOPEPTIDASE AMPS; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:RVT56110.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288024}.
SQ   SEQUENCE   305 AA;  34378 MW;  5F4A8B9CDBE6E040 CRC64;
     MTSFSDEDSN LVERAWKINR AKSIAMRPCR TFGMENHNKW VVVNAPTKEW ALQVFPGQHE
     DKANELLWKY ILHATKSNEA NPVSAWEKQN CILKNKAKKL NDYQFSALHF VSEKTDLTVA
     LVKNHVWLGG SETTKEGKGF MSNIPVEEVW TMPNKYHVDG YVTTTKPIIL AGATIQNLKL
     FFKNGKVIRI EPKQQLLLDL LQTDEGARML GEVALVSANS SIAKMGITFK STLLDENAAC
     HIALGQAYID NLLNRSLIDE EELTELGMNK SAVHEDIMIG DSSLNVYGIL EKERILIMEN
     GEWSI
//
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