ID   Y181_MYCBP              Reviewed;         311 AA.
AC   A1KEW5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase BCG_0181;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BCG_0181;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL70165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM408590; CAL70165.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A1KEW5; -.
DR   SMR; A1KEW5; -.
DR   KEGG; mbb:BCG_0181; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
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..311
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase BCG_0181"
FT                   /id="PRO_0000361142"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  33709 MW;  BD0ACB7D30CF10CD CRC64;
     MSSLPSSRRT AGDTWAITES VGATALGVAA ARAVETAATN PLIRDEFAKV LVSSAGTAWA
     RLADADLAWL DGDQLGRRVH RVACDYQAVR THFFDEYFGA AVDAGVRQVV ILAAGLDARA
     YRLNWPAGTV VYEIDQPSVL EYKAGILQSH GAVPTARRHA VAVDLRDDWP AALIAAGFDG
     TQPTAWLAEG LLPYLPGDAA DRLFDMVTAL SAPGSQVAVE AFTMNTKGNT QRWNRMRERL
     GLDIDVQALT YHEPDRSDAA QWLATHGWQV HSVSNREEMA RLGRAIPQDL VDETVRTTLL
     RGRLVTPAQP A