ID A0A089LTE2_9BACL Unreviewed; 409 AA.
AC A0A089LTE2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:AIQ64192.1};
GN ORFNames=PSTEL_14995 {ECO:0000313|EMBL:AIQ64192.1};
OS Paenibacillus stellifer.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=169760 {ECO:0000313|EMBL:AIQ64192.1, ECO:0000313|Proteomes:UP000029507};
RN [1] {ECO:0000313|EMBL:AIQ64192.1, ECO:0000313|Proteomes:UP000029507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14472 {ECO:0000313|EMBL:AIQ64192.1,
RC ECO:0000313|Proteomes:UP000029507};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-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}.
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DR EMBL; CP009286; AIQ64192.1; -; Genomic_DNA.
DR RefSeq; WP_038696274.1; NZ_CP009286.1.
DR AlphaFoldDB; A0A089LTE2; -.
DR STRING; 169760.PSTEL_14995; -.
DR MEROPS; M29.002; -.
DR KEGG; pste:PSTEL_14995; -.
DR HOGENOM; CLU_054346_1_0_9; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000029507; 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:UP000029507}.
SQ SEQUENCE 409 AA; 44997 MW; DD774C120E47EB1F CRC64;
MEFKQKLENY ALLAVKIGVN IQPGQKLVIN ADIAAAELVR LVVRNAYESG ATLVKVNWND
EVVTRTRYDL APEESFLEPP TRHAEEMEEL ALNNACFLTI ISADPDLLKG VDPARVANNQ
RVTAKAMAGY RKQLMGNHAS WSGIAFPSAS WAAKVFPDAP ENEQVSLLWD AIFRAVRADQ
EDPLEAWQLH LDGLKRRCDR LNARKYRKLH YTAPGTDLTL ELPEGHIWCQ AGAVNGRGVP
FLANIPTEEV FTVAHRDGTN GTVSSTKPLS YAGNVIDRFT LTFKDGKVTD YTAEIGQDQL
EKLFAMDEGA RSLGEVALVP HRSPISESGI LFFTTLFDEN ASCHLALGAS YPFTLEGGTA
MTKEELVERG MNQSLIHVDF MMGSPEMNID GITEDGSVEP IFVGGGWAD
//
