Y2258_MYCTU
ID Y2258_MYCTU Reviewed; 353 AA.
AC O53532; F2GJC0; I6X3Q8; Q7D7D1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=S-adenosylmethionine-dependent methyltransferase Rv2258c {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
GN OrderedLocusNames=Rv2258c {ECO:0000312|EMBL:CCP45039.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=32634279; DOI=10.1111/mmi.14571;
RA Zaveri A., Wang R., Botella L., Sharma R., Zhu L., Wallach J.B., Song N.,
RA Jansen R.S., Rhee K.Y., Ehrt S., Schnappinger D.;
RT "Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the
RT DNA-damage response and leads to cell death.";
RL Mol. Microbiol. 114:641-652(2020).
RN [4] {ECO:0007744|PDB:5F8C, ECO:0007744|PDB:5F8E, ECO:0007744|PDB:5F8F}
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 6-353 OF APOENZYME AND IN
RP COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE AND SINEFUNGIN, FUNCTION, SUBUNIT,
RP AND DOMAIN.
RC STRAIN=H37Rv;
RX PubMed=26772148; DOI=10.1016/j.jsb.2016.01.002;
RA Im H.N., Kim H.S., An D.R., Jang J.Y., Kim J., Yoon H.J., Yang J.K.,
RA Suh S.W.;
RT "Crystal structure of Rv2258c from Mycobacterium tuberculosis H37Rv, an S-
RT adenosyl-l-methionine-dependent methyltransferase.";
RL J. Struct. Biol. 193:172-180(2016).
CC -!- FUNCTION: Probable methyltransferase that may target bulky nonpolar
CC molecules with aromatic rings. {ECO:0000305|PubMed:26772148}.
CC -!- SUBUNIT: Homodimer (PubMed:26772148). Co-immunoprecipitates with DarG
CC in the presence and absence of darT (PubMed:32634279).
CC {ECO:0000269|PubMed:26772148, ECO:0000269|PubMed:32634279}.
CC -!- DOMAIN: Consists of two domains which are linked by a long alpha-helix.
CC The N-terminal domain is essential for dimerization and the C-terminal
CC domain has the class I MTase fold. {ECO:0000269|PubMed:26772148}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305|PubMed:26772148}.
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DR EMBL; AL123456; CCP45039.1; -; Genomic_DNA.
DR RefSeq; NP_216774.1; NC_000962.3.
DR RefSeq; WP_003411622.1; NZ_NVQJ01000008.1.
DR PDB; 5F8C; X-ray; 1.83 A; A/B/C=6-353.
DR PDB; 5F8E; X-ray; 2.90 A; A/B/C=6-353.
DR PDB; 5F8F; X-ray; 1.90 A; A/B/C=6-353.
DR PDBsum; 5F8C; -.
DR PDBsum; 5F8E; -.
DR PDBsum; 5F8F; -.
DR AlphaFoldDB; O53532; -.
DR SMR; O53532; -.
DR STRING; 83332.Rv2258c; -.
DR PaxDb; O53532; -.
DR PRIDE; O53532; -.
DR DNASU; 888755; -.
DR GeneID; 888755; -.
DR KEGG; mtu:Rv2258c; -.
DR PATRIC; fig|83332.111.peg.2512; -.
DR TubercuList; Rv2258c; -.
DR eggNOG; COG2230; Bacteria.
DR OMA; IHDQAHP; -.
DR PhylomeDB; O53532; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:MTBBASE.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..353
FT /note="S-adenosylmethionine-dependent methyltransferase
FT Rv2258c"
FT /id="PRO_0000450837"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26772148"
FT BINDING 179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26772148"
FT BINDING 202..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26772148"
FT BINDING 229..230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26772148"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26772148"
FT HELIX 8..33
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:5F8C"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5F8C"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 136..153
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 205..217
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5F8F"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 265..276
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:5F8C"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5F8C"
FT STRAND 344..352
FT /evidence="ECO:0007829|PDB:5F8C"
SQ SEQUENCE 353 AA; 37514 MW; 2D6AC793EE7FC40F CRC64;
MSGALETTEE FGNRFVAAID SAGLAILVSV GHQTGLLDTM AGLPPATSME IAEAAGLEER
YVREWLGGMT TGQIVEYDAG SSTYSLPAHR AGMLTRAAGP DNLAVIAQFV SLLGEVEQKV
IRCFREGGGV PYSEYPRFHK LMAEMSGMVF DAALIDVVLP LVDGLPDRLR SGADVADFGC
GSGRAVKLMA QAFGASRFTG IDFSDEAVAA GTEEAARLGL ANATFERHDL AELDKVGAYD
VITVFDAIHD QAQPARVLQN IYRALRPGGV LLMVDIKASS QLEDNVGVPL STYLYTTSLM
HCMTVSLALD GAGLGTVWGR QLATSMLADA GFTDVTVAEI ESDVLNNYYI ARK
