ID   Y182_MYCBP              Reviewed;         310 AA.
AC   A1KEW6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_0182;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_0182;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; AM408590; CAL70166.1; -; Genomic_DNA.
DR   RefSeq; WP_003900814.1; NC_008769.1.
DR   AlphaFoldDB; A1KEW6; -.
DR   SMR; A1KEW6; -.
DR   GeneID; 45424112; -.
DR   KEGG; mbb:BCG_0182; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; PMDITEL; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..310
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_0182"
FT                   /id="PRO_0000361143"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34016 MW;  1B27617869F6059E CRC64;
     MRTHDDTWDI KTSVGATAVM VAAARAVETD RPDPLIRDPY ARLLVTNAGA GAIWEAMLDP
     TLVAKAAAID AETAAIVAYL RSYQAVRTNF FDTYFASAVA AGIRQVVILA SGLDSRAYRL
     DWPAGTIVYE IDQPKVLSYK STTLAENGVT PSAGRREVPA DLRQDWPAAL RDAGFDPTAR
     TAWLAEGLLM YLPAEAQDRL FTQVGAVSVA GSRIAAETAP VHGEERRAEM RARFKKVADV
     LGIEQTIDVQ ELVYHDQDRA SVADWLTDHG WRARSQRAPD EMRRVGRWVE GVPMADDPTA
     FAEFVTAERL