ID   A0A268SLY5_9BACL        Unreviewed;       414 AA.
AC   A0A268SLY5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:PAF32896.1};
GN   ORFNames=CHI14_05985 {ECO:0000313|EMBL:PAF32896.1};
OS   Paenibacillus sp. 7516.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF32896.1, ECO:0000313|Proteomes:UP000216732};
RN   [1] {ECO:0000313|EMBL:PAF32896.1, ECO:0000313|Proteomes:UP000216732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7516 {ECO:0000313|EMBL:PAF32896.1,
RC   ECO:0000313|Proteomes:UP000216732};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) 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:PAF32896.1}.
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DR   EMBL; NPBI01000006; PAF32896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268SLY5; -.
DR   Proteomes; UP000216732; 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:PAF32896.1}; 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   414 AA;  46290 MW;  49FC9A6263740B9C CRC64;
     MSNFEQTFEQ SLEQYAELVV KVGVNIQKGQ DLLVTAPIET LEFTRLIVAK AYAAGAKYVQ
     VDFEDDQITR SRFQQGSDDS FDYYPAWKGD MMERFAEAGG ATLTIKVPDP ELYNGIDSDK
     VSRATKAAAQ ARRGYSKYTR NHEISWCLIK APTKAWANKV FADIPEEDRI NVMWDTIFKM
     NRVDGGDAIQ NWRQHLDTLN TKSDQLNQKN YKSLHYRAPG TDLKIELVDN HIWGGGGSEN
     KAGVYTVANM PTEEVFTMPK RSGVNGYVSS TMPLNLNGQL VDQMRITFKD GQVVAFTAAS
     GEEHLKNLFA TDEGARYLGE VALVPHDSPI SNLNRIFYNT GIDENASCHL AVGSAYPFNM
     KDGTTMSNEE LLKHECNVSL THVDFMIGSA ELDIDGELQD GTIEPVFRKG NWAF
//