ID   A0A1G7TI06_9LACT        Unreviewed;       413 AA.
AC   A0A1G7TI06;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:SDG34987.1};
GN   ORFNames=SAMN05421791_10628 {ECO:0000313|EMBL:SDG34987.1};
OS   Facklamia miroungae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=120956 {ECO:0000313|EMBL:SDG34987.1, ECO:0000313|Proteomes:UP000199708};
RN   [1] {ECO:0000313|EMBL:SDG34987.1, ECO:0000313|Proteomes:UP000199708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-466 {ECO:0000313|EMBL:SDG34987.1,
RC   ECO:0000313|Proteomes:UP000199708};
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; FNCK01000006; SDG34987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7TI06; -.
DR   STRING; 120956.SAMN05421791_10628; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000199708; 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:SDG34987.1}; 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:UP000199708}.
SQ   SEQUENCE   413 AA;  45899 MW;  2A22F0E8D2BEF1B8 CRC64;
     MTLKNFDQLL KKYANLIVNK GIGVNKDDYI LIFADLDQAP LVRLVTEAAY QAGAKFVKVN
     WADDALTRLH FTHQTEETLT DIPQYKIDEG NYYVEKRAKR ISLRSSDPNV LKGIDPAKIN
     AANRASSHAM KDVRIATQSN LVSWLVVAGA GKEWAALVFP DLETSQEQVD ALWDQIFKTT
     RIYEDDPIKA WDEHEDRLSE KARFLNEQQF DQLHYTGPGT DFTVGLPKNH VWESAGSLNE
     KGEVFIANMP TEEVFTAPDA RRAEGYISSS KPLAYGGTVI DGMKFTFKDG KVTEVNAKEG
     EETLRQLVKE NDGSDALGEV ALVAHKSPIS QSGIIFYNTL FDENASNHIA LGQAYATSVK
     NGAKMSQEEL EEVGLNRSNV HVDFMVGNAE MNIDGIAADG TVTPIFRKGE WAF
//