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Database: UniProt
Entry: A0A1I0X8P7_9BACI
LinkDB: A0A1I0X8P7_9BACI
Original site: A0A1I0X8P7_9BACI 
ID   A0A1I0X8P7_9BACI        Unreviewed;       416 AA.
AC   A0A1I0X8P7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Aminopeptidase II. Metallo peptidase. MEROPS family M29 {ECO:0000313|EMBL:SFA97291.1};
GN   ORFNames=SAMN04488072_104243 {ECO:0000313|EMBL:SFA97291.1};
OS   Lentibacillus halodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX   NCBI_TaxID=237679 {ECO:0000313|EMBL:SFA97291.1, ECO:0000313|Proteomes:UP000198642};
RN   [1] {ECO:0000313|EMBL:SFA97291.1, ECO:0000313|Proteomes:UP000198642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFA97291.1,
RC   ECO:0000313|Proteomes:UP000198642};
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; FOJW01000004; SFA97291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0X8P7; -.
DR   STRING; 237679.SAMN04488072_104243; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000198642; 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:SFA97291.1}; 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:UP000198642}.
SQ   SEQUENCE   416 AA;  46271 MW;  9C987B7A57809969 CRC64;
     MADQKTKEKY AELALRTGVN LQNNQALMIN APIEGADFTR IVARKAYEMG AKDVHINWTD
     DELTLLKYEN APDDVIGTYP EWKVKLHDMY AEDGAAVLSI RSTNPDLLKD IDSSRVAMAN
     KAAAQAMKNF RQYTMNDRIT WSIISIPTGD WAQKIFPDKS REDAVERLWD AIVNIVRVDQ
     EAPMAAWEEH NKTLETAREI LNRKKYKKLV FKAPGTDLEI ELPDGHIWKG GSAVSEQGTT
     FNPNIPTEEV FSLPHKYGVN GTVSSTKPLN YGGSLIDQFS LIFKDGNVVD YQAEQGEETL
     KHLLNTDEGA RHLGEVALVP HESPVSQSGL IFYNTLYDEN ASCHIALGKA YPTNLEGGAN
     MDDETLDQHG VNDSLTHVDF MIGSEKLDID GVLEDGTTEP VFRKGTWALN VKGNDG
//
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