ID   A0A268SBT4_9BACL        Unreviewed;       371 AA.
AC   A0A268SBT4;
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:PAF30063.1};
GN   ORFNames=CHI14_18620 {ECO:0000313|EMBL:PAF30063.1};
OS   Paenibacillus sp. 7516.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2022549 {ECO:0000313|EMBL:PAF30063.1, ECO:0000313|Proteomes:UP000216732};
RN   [1] {ECO:0000313|EMBL:PAF30063.1, ECO:0000313|Proteomes:UP000216732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7516 {ECO:0000313|EMBL:PAF30063.1,
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:PAF30063.1}.
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DR   EMBL; NPBI01000021; PAF30063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268SBT4; -.
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: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:PAF30063.1}; 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;  41691 MW;  76F8BEFD52DE57CC CRC64;
     MKDPRIQKLA ANLVGYSVDV QPGENVLVEM IGSERDLINA IIEEVGKKGG NVFVQLTDKT
     VQRAMLKNAT EEMMKTWAEI DLNRMKQMDC YIGIRAGENV NDLSDVPEEK MKMYNSLYSH
     PVHSEQRVKH TKWVVLRYPN ASMAQLANTS TEAFEDFYFD VCNLDYAKMD KAQDSLANLM
     NRTDKVRITG PGTDLSFSIK DIGAVKCSGQ KNIPDGEVYS APVRDSVNGT ISYNAATLYN
     GVTFENIKFT FKDGKIIEAT SNDTERLNEI LNSDDGARHI GEFAIGFNPH ILHPMKDILF
     DEKIAGSLHF TPGQAYEETD NGNRSSIHWD LVLIQRPDYG GGEIYFDDVL IRKDGIFVIP
     ELECLNPDQL K
//