ID   Y151_MYCBO              Reviewed;         310 AA.
AC   Q7U2R2; A0A1R3XV23; X2BE60;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb0151;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=BQ2027_MB0151;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIT98589.1; -; Genomic_DNA.
DR   RefSeq; NP_853817.1; NC_002945.3.
DR   RefSeq; WP_003900814.1; NC_002945.4.
DR   AlphaFoldDB; Q7U2R2; -.
DR   SMR; Q7U2R2; -.
DR   GeneID; 45424112; -.
DR   PATRIC; fig|233413.5.peg.172; -.
DR   OMA; PMDITEL; -.
DR   Proteomes; UP000001419; 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 Mb0151"
FT                   /id="PRO_0000361131"
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