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Database: UniProt
Entry: A0A1E8YR62_9LACT
LinkDB: A0A1E8YR62_9LACT
Original site: A0A1E8YR62_9LACT 
ID   A0A1E8YR62_9LACT        Unreviewed;       413 AA.
AC   A0A1E8YR62;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   SubName: Full=Peptidase M29 {ECO:0000313|EMBL:OFK58211.1};
GN   ORFNames=HMPREF2811_05850 {ECO:0000313|EMBL:OFK58211.1};
OS   Globicatella sp. HMSC072A10.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Globicatella.
OX   NCBI_TaxID=1739315 {ECO:0000313|EMBL:OFK58211.1, ECO:0000313|Proteomes:UP000176615};
RN   [1] {ECO:0000313|EMBL:OFK58211.1, ECO:0000313|Proteomes:UP000176615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC072A10 {ECO:0000313|EMBL:OFK58211.1,
RC   ECO:0000313|Proteomes:UP000176615};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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; KV805727; OFK58211.1; -; Genomic_DNA.
DR   RefSeq; WP_071408515.1; NZ_KV805727.1.
DR   AlphaFoldDB; A0A1E8YR62; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000176615; 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:UP000176615}.
SQ   SEQUENCE   413 AA;  45666 MW;  95C544F73DB628D3 CRC64;
     MVLENFDVLL DKYANLLMTK GLNVSTDDYV LINAEIEQAP LVRLMTQHAY QLGAKHVKVN
     WTDTAISILG YQHQSVETLT DIPEYRVAES KYDIETRAKR IALRSANPNA LKDIAPEKLA
     AASKAASLAF SEQRIASQAN VMSWLVCAAA GQEWAALVFP ELESSEAQVD ALWDQIFKTT
     RVYEQDPVAT WEKHEATLNE KADFLNEKQF DSLHYTAPGV DFTVGLPLNH VWESAGSTNQ
     QGEIFIANMP TEEVFTAPDF RRADGIIKSS KPLSYNGVVI RDMTFKFKDG EIIEVSAAEG
     EATLKTLIEN NEGARSLGEV ALVPHSSPIS QSNITFFNTL FDENASNHLA IGQAYATSVQ
     NGTKMSQEEL KASGLNRSTV HVDFMVGNAE MNIDGITKDG ETFAIFRNGE WAF
//
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