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Database: UniProt
Entry: A0A1G8DBE9_9BACI
LinkDB: A0A1G8DBE9_9BACI
Original site: A0A1G8DBE9_9BACI 
ID   A0A1G8DBE9_9BACI        Unreviewed;       410 AA.
AC   A0A1G8DBE9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Aminopeptidase II. Metallo peptidase. MEROPS family M29 {ECO:0000313|EMBL:SDH55012.1};
GN   ORFNames=SAMN05192534_10733 {ECO:0000313|EMBL:SDH55012.1};
OS   Alteribacillus persepolensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX   NCBI_TaxID=568899 {ECO:0000313|EMBL:SDH55012.1, ECO:0000313|Proteomes:UP000199163};
RN   [1] {ECO:0000313|EMBL:SDH55012.1, ECO:0000313|Proteomes:UP000199163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21632 {ECO:0000313|EMBL:SDH55012.1,
RC   ECO:0000313|Proteomes:UP000199163};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNDK01000007; SDH55012.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8DBE9; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000199163; 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:SDH55012.1}; 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:UP000199163}.
FT   REGION          390..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  45558 MW;  98E27EE6E21479A2 CRC64;
     MNTFEQHLDN YAELAVKQGV NLQNNQTLFI SAPITSASFV HLLAEKAYDN GAKNVHVDWV
     DEALTRMKYE KAPDEAFHEF PSWVAQGREQ LAQEGAAFIT VKSTDPDLLK GIDQNRIAAA
     NKAAGEAMEM FREYIQSDTV SWLVIAAPSP GWAQKVFPDA SEKEAEQKLW EAIFQAVRAD
     QKDPVQNWEE HKQKLQEKAD LLNNKQFTQL HYTAPGTDLT IELAEGHIWT GGGSKNQDGV
     SFIPNMPTEE VFTAPHKTGV NGYVTNTKPL NYSGNIIDDF TLHFKNGKIV DYQVKQGKET
     LKHLIETDDG SHYLGEVALV PHSSPISQTG TLFYNTLFDE NASNHLAIGS AYAFCVQNGT
     DMSKEEKEAH GINTSITHVD FMVGSADMNI DGQHKDGSTE PIMRNGEWAI
//
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