ID A0A172ZEK9_9BACL Unreviewed; 411 AA.
AC A0A172ZEK9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Peptidase M29 {ECO:0000313|EMBL:ANF95933.1};
GN ORFNames=AR543_07885 {ECO:0000313|EMBL:ANF95933.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95933.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF95933.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF95933.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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; CP013023; ANF95933.1; -; Genomic_DNA.
DR RefSeq; WP_060533331.1; NZ_CP013023.1.
DR AlphaFoldDB; A0A172ZEK9; -.
DR KEGG; pbv:AR543_07885; -.
DR OrthoDB; 9803993at2; -.
DR Proteomes; UP000078148; 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:UP000078148}.
SQ SEQUENCE 411 AA; 45732 MW; 66A2C5002F5FBF89 CRC64;
MNSFTTMLQK YAELVIQVGV NIQPGQVLIV NAPLETAELT RLIVAKAYDA GAKYVMVDWD
DEQITRIRYE HAADDTFGYY PQWHADMMEK FAEEGGAILR IKVPNPELFD GIDSWKVSAS
VKATAIANEK YSVYTRNSRI SWSLIKAPTA AWANKVYADL PEAERIPAMW EAIFMMNRVT
ADNDPVAAWR EHIEHLRKGK NLLNGKKYKS LHYRAPGTDL HVQLPEGHIW RSGGGENDAG
TYFVANMPTE EVFSMPHRTG VNGTVKSTMP LNLNGRLVEG IILTFKDGKV VEYDAAAGRE
YLTDLLDTDE GASYLGEIAL VPYDSPISRL NRIFYNTGID ENASCHFALG SAYPTNIEGG
TQLSKEELVQ RGANVSLTHV DFMVGSAELD IDGELPDGTV EPVFRQGNWA F
//
