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Database: UniProt
Entry: A0A1A5YQU2_9BACL
LinkDB: A0A1A5YQU2_9BACL
Original site: A0A1A5YQU2_9BACL 
ID   A0A1A5YQU2_9BACL        Unreviewed;       414 AA.
AC   A0A1A5YQU2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Peptidase M29 {ECO:0000313|EMBL:OBR67943.1};
GN   ORFNames=A7K91_18590 {ECO:0000313|EMBL:OBR67943.1};
OS   Paenibacillus oryzae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1844972 {ECO:0000313|EMBL:OBR67943.1, ECO:0000313|Proteomes:UP000092024};
RN   [1] {ECO:0000313|EMBL:OBR67943.1, ECO:0000313|Proteomes:UP000092024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1DrF-4 {ECO:0000313|EMBL:OBR67943.1,
RC   ECO:0000313|Proteomes:UP000092024};
RA   Zhang J., Zhang X.;
RT   "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL   Submitted (MAY-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   -!- 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:OBR67943.1}.
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DR   EMBL; LYPA01000030; OBR67943.1; -; Genomic_DNA.
DR   RefSeq; WP_068679858.1; NZ_LYPA01000030.1.
DR   AlphaFoldDB; A0A1A5YQU2; -.
DR   STRING; 1844972.A7K91_18590; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000092024; 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   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:UP000092024}.
SQ   SEQUENCE   414 AA;  45446 MW;  01349EB3BAED8D60 CRC64;
     MTATVKAKQH FEKYAELIVR TGVNVQKGQE VFLAGASIEI ADLVRVIVAK AYEAGASNVH
     VDWMDETVSR LKYEHADEST LSRFPAWETL KRNTFVENGA AFISITSSSP DLLKGIPSGK
     ISAYQKAAGA GLKEFRQAVQ ADKVSWTVVA AAGSEWAKKV FPNLPAEEAV ERLWSAIFDS
     VRLHTADPVQ EWVKHNETLH SKAEILNKLR FKSLHYTAPG TDLTVELHEK HIWVGAGSTN
     QDGLDFMANM PTEEVFSVPL KTGTNGYVSS TKPLSYGGNI IDRFKLTFKD GRIIKAEAEE
     GEEILQKLVE IDEGSHYLGE VALVPHYSPI SESGILFYNT LFDENASNHF AIGSGYAFNV
     EGGKTMSAEE LEAHGVNASI THNDFMIGSA DMDIDGIQHD GTVVPVFRKG NWAI
//
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