ID   A0A433RYA1_9BACL        Unreviewed;       410 AA.
AC   A0A433RYA1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 11.
DE   SubName: Full=Peptidase M29 {ECO:0000313|EMBL:RUS58265.1};
GN   ORFNames=QI30_01400 {ECO:0000313|EMBL:RUS58265.1};
OS   Kurthia sp. 3B1D.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1562256 {ECO:0000313|EMBL:RUS58265.1, ECO:0000313|Proteomes:UP000288623};
RN   [1] {ECO:0000313|EMBL:RUS58265.1, ECO:0000313|Proteomes:UP000288623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B1D {ECO:0000313|EMBL:RUS58265.1,
RC   ECO:0000313|Proteomes:UP000288623};
RA   Lawson J.N., Gonzalez J.E., Rinauldi L., Xuan Z., Firman A., Shaddox L.,
RA   Trudeau A., Shah S., Reiman D.;
RT   "Genome sequence and analysis of novel Kurthia sp.";
RL   Submitted (NOV-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:RUS58265.1}.
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DR   EMBL; JTFC01000006; RUS58265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433RYA1; -.
DR   OrthoDB; 9803993at2; -.
DR   Proteomes; UP000288623; 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:UP000288623}.
SQ   SEQUENCE   410 AA;  45650 MW;  FD9EF029B04EDAC2 CRC64;
     MNDFRQKLEN YAELGIKIGA NLQKNQYLFL NISVENVPLA RALTKKAYEV GAKNVFVNYY
     DDALTRMRYD YAPEDSFDFF PEWQAAEKEW LADHGAAFIT VKSQSPDLLK GVNPDYVARA
     NKAMGQALSK YREYSQANKI SWTVMAAPTD AWAAKVFPDL PEDEQVNALW DAMFKATRAD
     LQDPVAAWKQ HDATLSEKVA FLNDKHYKAL HYTAPGTDLT IELPKTHVWS GGGAVNEKGF
     DFMANIPTEE VFTAPQWDGV NGYVTSKKPL NYSGNLIDNF TVTFENGRIV DVKAEEGEDI
     LKNLVATDEG SHYLGEVALV PHDSPISNSG ILFYNTLFDE NASNHIAIGS AYAFCIEGGT
     TMSQEELKAN GLNRSLVHVD FMIGCADMDI DGVLEDGTTE PVFRKGNWAF
//