ID   A0A229UL31_9BACL        Unreviewed;       410 AA.
AC   A0A229UL31;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:OXM84014.1};
GN   ORFNames=CF651_22455 {ECO:0000313|EMBL:OXM84014.1};
OS   Paenibacillus rigui.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=554312 {ECO:0000313|EMBL:OXM84014.1, ECO:0000313|Proteomes:UP000215509};
RN   [1] {ECO:0000313|EMBL:OXM84014.1, ECO:0000313|Proteomes:UP000215509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16352 {ECO:0000313|EMBL:OXM84014.1,
RC   ECO:0000313|Proteomes:UP000215509};
RA   Mayilraj S.;
RT   "Genome sequencing and assembly of Paenibacillus rigui.";
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:OXM84014.1}.
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DR   EMBL; NMQW01000035; OXM84014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A229UL31; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000215509; 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:OXM84014.1}; 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:UP000215509}.
SQ   SEQUENCE   410 AA;  45375 MW;  B3A020A4779E0328 CRC64;
     MSQFQELLSK YAEIVVNVGV NIQQGQTLVI NAAIDSAELV RLLVKKAYET GAYHVKVNWT
     DDTVSRLRYD LAPDESFLEE PKWYAGEMTE LAEKGFAVIS IVSADPDLLK GVAQERIVNH
     QKTYGKAMAK YRQYMQSDKF SWCVIAAPSR AWAAKVFPDV PEEQQVGKLW EAILKTVRVD
     QPDPTSAWEE HIRTLNAKSD YLNAKKYKKL HYLAPGTDLT IELPEGHIWV AADSINEQGN
     AFVANMPTEE VFTAPLASGV NGKVSSTKPL SYGGNIIDGF TLTFENGRIV DVKAEKGEDT
     LKGLIEMDEG SHYLGEVALV PHRSPISESN ILYYNTLFDE NASNHLAIGS AYAFCLEGGK
     GLSQDELKAR GLNTSIAHVD FMIGSAEMDI FGVTAEGKEE PIFHKGNWAF
//