ID   Y756_MYCTO              Reviewed;         318 AA.
AC   P9WFI4; L0T4P9; Q7ARS3; Q7D9D6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT0756;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT0756;
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}.
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DR   EMBL; AE000516; AAK44989.1; -; Genomic_DNA.
DR   RefSeq; WP_003403717.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFI4; -.
DR   SMR; P9WFI4; -.
DR   EnsemblBacteria; AAK44989; AAK44989; MT0756.
DR   KEGG; mtc:MT0756; -.
DR   PATRIC; fig|83331.31.peg.809; -.
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..318
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT0756"
FT                   /id="PRO_0000428533"
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   318 AA;  34950 MW;  F25150B40E9D1BE5 CRC64;
     MTQTGSARFE GDSWDLASSV GLTATMVAAA RAVAGRAPGA LVNDQFAEPL VRAVGVDFFV
     RMASGELDPD ELAEDEANGL RRFADAMAIR THYFDNFFLD ATRAGIRQAV ILASGLDSRA
     YRLRWPAGTI VFEVDQPQVI DFKTTTLAGL GAAPTTDRRT VAVDLRDDWP TALQKAGFDN
     AQRTAWIAEG LLGYLSAEAQ DRLLDQITAQ SVPGSQFATE VLRDINRLNE EELRGRMRRL
     AERFRRHGLD LDMSGLVYFG DRTDARTYLA DHGWRTASAS TTDLLAEHGL PPIDGDDAPF
     GEVIYVSAEL KQKHQDTR