ID   Y152_MYCTA              Reviewed;         311 AA.
AC   A5TYM0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0152;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MRA_0152;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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=ABQ71870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000611; ABQ71870.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A5TYM0; -.
DR   SMR; A5TYM0; -.
DR   STRING; 419947.MRA_0152; -.
DR   EnsemblBacteria; ABQ71870; ABQ71870; MRA_0152.
DR   KEGG; mra:MRA_0152; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   Proteomes; UP000001988; 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 MRA_0152"
FT                   /id="PRO_0000361222"
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