ID   A0A137SWS3_9FIRM        Unreviewed;       410 AA.
AC   A0A137SWS3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Putative aminopeptidase II {ECO:0000313|EMBL:KXO16911.1};
GN   ORFNames=HMPREF3189_00363 {ECO:0000313|EMBL:KXO16911.1};
OS   Clostridiales bacterium KA00134.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO16911.1, ECO:0000313|Proteomes:UP000070500};
RN   [1] {ECO:0000313|EMBL:KXO16911.1, ECO:0000313|Proteomes:UP000070500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00134 {ECO:0000313|EMBL:KXO16911.1,
RC   ECO:0000313|Proteomes:UP000070500};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXO16911.1}.
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DR   EMBL; LTAF01000006; KXO16911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137SWS3; -.
DR   STRING; 1588750.HMPREF3189_00363; -.
DR   PATRIC; fig|1588750.3.peg.357; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000070500; 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:KXO16911.1}; 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:UP000070500}.
SQ   SEQUENCE   410 AA;  46625 MW;  FC925AD22E003606 CRC64;
     MNLKDRIRKY ANLIVNTGLG INPKDVLVIR APVENYEFVR VLAEEAYKAG AKDVKTNFRD
     IKLNALRFEN VAEEVLTDIP QYFIDEQNHF VDNNYKLIAL IGEDPNGLKG LDPQKLMAAG
     KAQSQALKHF AAEQMRNKVS WCVVGAPTKA WARMIFEGID DELAVEKLWE LILDVSRVDE
     DPVKNWEAHI KLMGENADFL NENKFTKLKI KSSNGTDLEV GLPESYVFQA CGEDNLRGER
     FVANIPTEEV FSMPHRDRVN GLVYASKPLN YNGNVIEDFW FKFKDGKVVD FDAKKGREIL
     ENMLNMDEGA RHLGEVALVP YDSPISNTNR LFFETLYDEN ASCHLALGKA YPTCIENGDQ
     MSEDELKKRG VNDSIIHVDF MFGYKDTEIV GVRQDGREVL IFENGNWAKK
//