ID A0A081NZY0_9BACL Unreviewed; 412 AA.
AC A0A081NZY0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:KEQ24003.1};
GN ORFNames=ET33_09800 {ECO:0000313|EMBL:KEQ24003.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ24003.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ24003.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ24003.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) 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:KEQ24003.1}.
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DR EMBL; JNVM01000017; KEQ24003.1; -; Genomic_DNA.
DR RefSeq; WP_036686081.1; NZ_JNVM01000017.1.
DR AlphaFoldDB; A0A081NZY0; -.
DR MEROPS; M29.002; -.
DR eggNOG; COG2309; Bacteria.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000028123; 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:UP000028123}.
SQ SEQUENCE 412 AA; 45739 MW; 086FB389023D938C CRC64;
MSTFAHKLEK YATLAVRVGA NVQQGQTVVV MAPVVAAELV RLVAVKAYEA GAKNVMVEWN
DEELTRIKYK MAPMEAFHEY PMWKAQGLQE LAENDAAFIQ FYGPNPDLLK DVDPERVSTA
NKTASTALKG YRSQLMAHRA SWTLMAYATP EWALKIFPDL SPEAALDALW ERIFEATRVN
ADDPVEAWKE HNARLARTVS YLNEKRYKQL VYEASGTNLT VDLPEKHVWL GGAKENAKGI
FFNPNLPTEE VFTMPHHDGV NGVVRSTKPL NHGGQLIDGF SLTFKDGKVV DFSADKGYEM
LKRLLDTDEG ARKLGEVALV PHESPISNTN LIFYNTLFDE NASSHLALGQ AYPVNLDGGT
EMKEEELSQH GANSSLVHVD FMIGSADMNI DGITQDGVRE PVFRAGNWAL PV
//
