ID   A0A1H8K225_9FIRM        Unreviewed;       408 AA.
AC   A0A1H8K225;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:SEN87023.1};
GN   ORFNames=SAMN05216454_1216 {ECO:0000313|EMBL:SEN87023.1};
OS   Peptostreptococcus russellii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptostreptococcus.
OX   NCBI_TaxID=215200 {ECO:0000313|EMBL:SEN87023.1, ECO:0000313|Proteomes:UP000199512};
RN   [1] {ECO:0000313|EMBL:SEN87023.1, ECO:0000313|Proteomes:UP000199512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Calf135 {ECO:0000313|EMBL:SEN87023.1,
RC   ECO:0000313|Proteomes:UP000199512};
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; FODF01000021; SEN87023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8K225; -.
DR   STRING; 215200.SAMN05216454_1216; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000199512; 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:SEN87023.1}; 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:UP000199512}.
SQ   SEQUENCE   408 AA;  46227 MW;  D780D35649C81454 CRC64;
     MELNKRIDKF AKLAIKTGIN IQKGETLLIR ADVEASDFAR RCVKEAYKAG AKHVYVEYSD
     EVIFRETYLS APDEAFDEYP EWQSYKYTEI AKESGSFLNI VSANPDLLKG VDTDRISRFQ
     KIAGKYLKEW RSYTLTDKVK WSIVAVPSEA WASRLHPDLE LNDAIEKLWN EILDCSRVSE
     NPVEDWKSHV SNIRNKMNTL NKLDLDRLIY KSSKTNLEIG LPQGHIWQGG SAFDPNNIEF
     CPNIPTEEVY GMPHKNRVNG IVHSTKPLIF AGNTIDNFWI EFKDGQIIDY KAEKGHESLK
     LLIETDEGSL RLGEMALVPF DSPISNSNIV FYSTLFDENA SCHLAIGAAY SSNIENGDSL
     NENEMDKVGM NSSITHVDFM IGDSDLNIMG IDKSGKSHEI FKNGNWAF
//