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Database: UniProt
Entry: A0A1M5YZ34_9FIRM
LinkDB: A0A1M5YZ34_9FIRM
Original site: A0A1M5YZ34_9FIRM 
ID   A0A1M5YZ34_9FIRM        Unreviewed;       411 AA.
AC   A0A1M5YZ34;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:SHI17134.1};
GN   ORFNames=SAMN02745180_02565 {ECO:0000313|EMBL:SHI17134.1};
OS   Sporanaerobacter acetigenes DSM 13106.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Sporanaerobacteraceae;
OC   Sporanaerobacter.
OX   NCBI_TaxID=1123281 {ECO:0000313|EMBL:SHI17134.1, ECO:0000313|Proteomes:UP000184389};
RN   [1] {ECO:0000313|EMBL:SHI17134.1, ECO:0000313|Proteomes:UP000184389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13106 {ECO:0000313|EMBL:SHI17134.1,
RC   ECO:0000313|Proteomes:UP000184389};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQXR01000017; SHI17134.1; -; Genomic_DNA.
DR   RefSeq; WP_072745188.1; NZ_FQXR01000017.1.
DR   AlphaFoldDB; A0A1M5YZ34; -.
DR   STRING; 1123281.SAMN02745180_02565; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000184389; 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:SHI17134.1}; 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:UP000184389}.
SQ   SEQUENCE   411 AA;  46086 MW;  DE318606C3BDB9C6 CRC64;
     MNNFNTMLEN YARLAVKVGI NIQKGQKLVV NSPIECADFV RLVAKCAYEE GASDVYVEWH
     DEELLLMKYI NAPMEVFEKF PKWKADGFAQ MAEEGAGFLS IAASNPELLK DVDPEKIAAS
     NKSSSTAMKK FREYTMGNKN SWCVISIPTK DWATKVFPDV SEDDAIEKLW EAIFKTVRID
     KEDPVKAWEE HLENVNEKVK FLNEKKFKTL HYTSSNGTDL TIELPKGHIW AGGGENTTGG
     VYFVANMPTE EVFTMPKKTG INGLVVSTKP LNYGGNLIDN FKLTFKDGKV VDFEAEKGYE
     TLKHLLDTDE GSRYLGEVAL VPYDSPISNS NILFYNTLFD ENASCHLAFG MAYPTCIEGG
     NDMNEKEKEA HGVNTSLVHV DFMVGAKDLD IVGETESKEK FQVFKNGNWA F
//
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