ID A0A1B1MYS2_9BACL Unreviewed; 410 AA.
AC A0A1B1MYS2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:ANS74306.1};
GN ORFNames=AWM70_06680 {ECO:0000313|EMBL:ANS74306.1};
OS Paenibacillus yonginensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1462996 {ECO:0000313|EMBL:ANS74306.1, ECO:0000313|Proteomes:UP000092573};
RN [1] {ECO:0000313|EMBL:ANS74306.1, ECO:0000313|Proteomes:UP000092573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY84 {ECO:0000313|EMBL:ANS74306.1,
RC ECO:0000313|Proteomes:UP000092573};
RA Kim Y.J., Yang D.C., Sukweenadhi J.;
RT "Complete Genome Sequence of Paenibacillus yonginensis DCY84, a novel Plant
RT Growth-Promoting Bacteria with Elicitation of Induced Systemic
RT Resistance.";
RL Submitted (JAN-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; CP014167; ANS74306.1; -; Genomic_DNA.
DR RefSeq; WP_068694897.1; NZ_CP014167.1.
DR AlphaFoldDB; A0A1B1MYS2; -.
DR STRING; 1462996.AWM70_06680; -.
DR KEGG; pyg:AWM70_06680; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000092573; Chromosome.
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:UP000092573}.
SQ SEQUENCE 410 AA; 45777 MW; 8ABE92A28CBB17A9 CRC64;
MSDFLQKLEK YAELAVKVGV NVQPGQTLVV NAAIDSAELV RLIVKKAYER GARLVKVNWN
DDTVTRLRYD MAADESFLDE PKWYAGEMLE LVENGAAVLH VISSDPDLLK GVSHERITNL
QKVTGKAMSK YRQYQQADKF SWSIVAVPSK AWAAKVFPDV PESEQIDKLW DAIFHTTRID
REDTFEAWDN HIRTLNEKSD YLNEKKFKKL HYIAPGTDLT IELPEGHLWV AADSINQNGH
TFLANLPTEE VFTAPLKTGV NGKVSSTKPL SYSGNIIDEF TITFENGRIT DVSAKQGEEV
LKQLVSLDEG AHYLGEVALV PHNSPISESN ILFYNTLFDE NASNHLAIGS AYAFNLKGGK
EMTQEQLEQS GLNTSITHVD FMVGSGEMDI FGVTEDGTEI QIFKQGSWAI
//
