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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//