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Database: UniProt
Entry: A0A1I4I1I2_9BACL
LinkDB: A0A1I4I1I2_9BACL
Original site: A0A1I4I1I2_9BACL 
ID   A0A1I4I1I2_9BACL        Unreviewed;       371 AA.
AC   A0A1I4I1I2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Leucyl aminopeptidase (Aminopeptidase T) {ECO:0000313|EMBL:SFL48298.1};
GN   ORFNames=SAMN03159341_106286 {ECO:0000313|EMBL:SFL48298.1};
OS   Paenibacillus sp. 1_12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFL48298.1, ECO:0000313|Proteomes:UP000198699};
RN   [1] {ECO:0000313|EMBL:SFL48298.1, ECO:0000313|Proteomes:UP000198699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_12 {ECO:0000313|EMBL:SFL48298.1,
RC   ECO:0000313|Proteomes:UP000198699};
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; FOTE01000006; SFL48298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4I1I2; -.
DR   STRING; 1566278.SAMN03159341_106286; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000198699; 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:SF1; BLL6088 PROTEIN; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:SFL48298.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
SQ   SEQUENCE   371 AA;  42304 MW;  D6A1AB00386FA428 CRC64;
     MRDPRLELLA RNLITYSLDV QPGEKVLIEM IGSEREIVSC LVEEVYARGG LPYVEMIDPV
     VQSAMLRSIT REQIEHWAEM DLKRMQDMSC YVAIRAGSNV SEMSDVPEEQ MKLYDLYYRK
     PIHLEQRVKK TRWVVLRYPN ASMAQLAGMS TAKFENFYFD VCNLDYAQMS KAMDPLQALM
     NRTDRVRIVA PGTDIQFSIK GIGSVKCCGR RNIPDGEVYT APIRDSVNGT ITYNTPSVKS
     GITFEQIAFR FENGKIVEAT SNQTDRLNQI LDTDEGARYI GEFSLGFNPH ILTPMKDTLF
     DEKIDGSLHF TPGQAYEQAD NGNRSSVHWD LVLIQRPEYG GGEIYFDDVL IRKNGRFVIQ
     ELEGLNPEHL K
//
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