ID A0A0D5NQN8_9BACL Unreviewed; 411 AA.
AC A0A0D5NQN8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:AJY77307.1};
GN ORFNames=VN24_25545 {ECO:0000313|EMBL:AJY77307.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY77307.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY77307.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY77307.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-2015) 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; CP011058; AJY77307.1; -; Genomic_DNA.
DR RefSeq; WP_045672732.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NQN8; -.
DR MEROPS; M29.002; -.
DR KEGG; pbj:VN24_25545; -.
DR PATRIC; fig|1126833.4.peg.5614; -.
DR HOGENOM; CLU_054346_1_0_9; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000032633; 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:UP000032633}.
SQ SEQUENCE 411 AA; 45687 MW; AC8C60C776D3AE65 CRC64;
MGSDFMTQLD RYAELIVKTG VKIQQGQTLV INATLDGAEL VRLLVKKGYE AGAYMVKVNW
SDDTVSRLRY DLAPDESFLE EPKWYAGEML ELVEKGAAVV SIVSSNPDLL KDVPQERIVN
HQKTYGKALH KYRQYAQSDK FSWCVVAAPS RAWAAKVFPG STEEEQMSSL WKAIFKSVRV
DQDDPIAAWD EHIRTLNEKS DYLNARKYKK LHYTAPGTDL TIELPEGHLW VAADSINEKG
IPFVANLPTE EVFTAPKADG VNGYVSSTKP LSYGGNLIDG FTITFENGRI TDVKAEKGEE
TLRNLVEMDE GSHYLGEVAL VPHQSPISQS NILFYNTLFD ENASNHLAIG SAYAFNLEGG
KSMSQEELKE RGLNTSITHV DFMIGSADMD IDGITADGEA EPLFRKGNWA I
//
