ID   Y146_MYCTO              Reviewed;         310 AA.
AC   P9WFJ2; L0T5V3; P96823; Q7DAE0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT0154;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT0154;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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=AAK44378.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44378.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70617; E70617.
DR   RefSeq; WP_003900814.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFJ2; -.
DR   SMR; P9WFJ2; -.
DR   EnsemblBacteria; AAK44378; AAK44378; MT0154.
DR   GeneID; 45424112; -.
DR   KEGG; mtc:MT0154; -.
DR   PATRIC; fig|83331.31.peg.166; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   Proteomes; UP000001020; 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 MT0154"
FT                   /id="PRO_0000428529"
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