ID   Y883_MYCBP              Reviewed;         301 AA.
AC   A1KGW3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_0883;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_0883;
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; CAL70869.1; -; Genomic_DNA.
DR   RefSeq; WP_003404349.1; NC_008769.1.
DR   AlphaFoldDB; A1KGW3; -.
DR   SMR; A1KGW3; -.
DR   GeneID; 45424793; -.
DR   KEGG; mbb:BCG_0883; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TRFYDQF; -.
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..301
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_0883"
FT                   /id="PRO_0000361152"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33416 MW;  5F6C68208D1E6199 CRC64;
     MVRADRDRWD LATSVGATAT MVAAQRALAA DPRYALIDDP YAAPLVRAVG MDVYTRLVDW
     QIPVEGDSEF DPQRMATGMA CRTRFFDQFF LDATHSGIGQ FVILASGLDA RAYRLAWPVG
     SIVYEVDMPE VIEFKTATLS DLGAEPATER RTVAVDLRDD WATALQTAGF DPKVPAAWSA
     EGLLVYLPVE AQDALFDNIT ALSAPGSRLA FEFVPDTAIF ADERWRNYHN RMSELGFDID
     LNELVYHGQR GHVLDYLTRD GWQTSALTVT QLYEANGFAY PDDELATAFA DLTYSSATLM
     R