ID   A0A1I6RAI3_9BACL        Unreviewed;       411 AA.
AC   A0A1I6RAI3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Aminopeptidase II. Metallo peptidase. MEROPS family M29 {ECO:0000313|EMBL:SFS61739.1};
GN   ORFNames=SAMN05428962_1520 {ECO:0000313|EMBL:SFS61739.1};
OS   Paenibacillus sp. BC26.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1881032 {ECO:0000313|EMBL:SFS61739.1, ECO:0000313|Proteomes:UP000199637};
RN   [1] {ECO:0000313|EMBL:SFS61739.1, ECO:0000313|Proteomes:UP000199637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC26 {ECO:0000313|EMBL:SFS61739.1,
RC   ECO:0000313|Proteomes:UP000199637};
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; FPAD01000001; SFS61739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6RAI3; -.
DR   STRING; 1881032.SAMN05428962_1520; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000199637; 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:SFS61739.1}; 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   411 AA;  45409 MW;  A0D60719B42DC8F5 CRC64;
     MKSFQHRLEQ YAALAVEVGV NVQPGQKLCI ISQIAAAEFV REVAKHAYEI GASYVHVDWM
     DEIITRTRLE KSPEEGLSYY PEWHAKGRVA LAEEGAAFLW VVAENPDLLN GIDASRVGLA
     TKSQQAALQP FRKFTLSNEV AWSIVAVPTP EWAEKVFPAL PAAERVDALW EAIFAATRVD
     AADPVQSWRE HADNLRTKAG RLNERRYKEL RYRGSAGTDV TIGLPEGHLW VSAGTRNGQG
     TTFIPNMPTE EVFTSPLRTS VNGTVVSSKP LSYNGNLIDN FSITFTEGRI TSYQAEVGYD
     ALKGLVETDD GSHYLGEIAL VPYRSPISDT NLTFYNTLFD ENAACHLAIG FAFPFCIEGG
     LSMSKEELAE RGLNHSLTHV DFMIGTEDLD IDGVLQDGTT EPVFRDGNWA F
//