ID   Y153_MYCTO              Reviewed;         311 AA.
AC   P9WFJ0; L0T2T4; P96822; Q7DAE1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT0153;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT0153;
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=AAK44377.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44377.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70617; D70617.
DR   AlphaFoldDB; P9WFJ0; -.
DR   SMR; P9WFJ0; -.
DR   EnsemblBacteria; AAK44377; AAK44377; MT0153.
DR   KEGG; mtc:MT0153; -.
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..311
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT0153"
FT                   /id="PRO_0000428530"
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