ID A0A448V1L4_9FIRM Unreviewed; 419 AA.
AC A0A448V1L4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Aminopeptidase 2 {ECO:0000313|EMBL:VEJ35620.1};
DE EC=3.4.11.- {ECO:0000313|EMBL:VEJ35620.1};
GN ORFNames=NCTC13079_00789 {ECO:0000313|EMBL:VEJ35620.1};
OS Peptoniphilus ivorii.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=54006 {ECO:0000313|EMBL:VEJ35620.1, ECO:0000313|Proteomes:UP000269544};
RN [1] {ECO:0000313|EMBL:VEJ35620.1, ECO:0000313|Proteomes:UP000269544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13079 {ECO:0000313|EMBL:VEJ35620.1,
RC ECO:0000313|Proteomes:UP000269544};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LR134523; VEJ35620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448V1L4; -.
DR KEGG; piv:NCTC13079_00789; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000269544; Chromosome 1.
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:VEJ35620.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:VEJ35620.1};
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:UP000269544}.
SQ SEQUENCE 419 AA; 46538 MW; 67578E9DB9B5D9A3 CRC64;
MNFTEKLNDY ARLLVRVGVG LEKGQLLVIR SPIEGRDLAV ACAKCAYELG APSVHVIWSD
DDLVLLRYTH APDEVLNTVP EYERDMFRYY LDKGAAFLSF TGSDPELLKQ IDGKRLQEAT
KHRMQAMAFY SEAMMADRNP WTVAGVPTRA WAKKVFPDAE NAAAVSQLWE AIFETARVNG
DAIENWKTHM ETVNQKARAL TALELKTLRY RSSNGTDFEI GLPEGHLWAG GGSKTPAGKP
FVANIPTEEV FTLPHKDTAN GVVYASMPLQ YNGNTIDKFW LRFEDGKVVD FDAEIGKDVL
KHLLETDEGA ARLGEVALVP YDSPISNRNH LFFNTLYDEN ASCHLALGRA YPTCLKGGEE
LSKEALAERG ANDSLVHVDF MVGAEDMDID GIDRAGTVLP IFKKGNWAAE FEEIANKTI
//
