RSMG_MYCTU
ID RSMG_MYCTU Reviewed; 224 AA.
AC P9WGW9; E7E4Z6; O53597;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=Glucose-inhibited division protein B;
GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; Synonyms=gidB;
GN OrderedLocusNames=Rv3919c; ORFNames=MTV028.10c;
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 [GENOMIC DNA].
RC STRAIN=MP 31;
RA Verma J.S., Routela R.S., Rawat D.S., Das R., Manzoor N., Nair D.;
RT "Evaluation of alterations responsible for streptomycin resistance in
RT Mycobacterium tuberculosis.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=17238915; DOI=10.1111/j.1365-2958.2006.05585.x;
RA Okamoto S., Tamaru A., Nakajima C., Nishimura K., Tanaka Y., Tokuyama S.,
RA Suzuki Y., Ochi K.;
RT "Loss of a conserved 7-methylguanosine modification in 16S rRNA confers
RT low-level streptomycin resistance in bacteria.";
RL Mol. Microbiol. 63:1096-1106(2007).
RN [4]
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).
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 518 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- DISRUPTION PHENOTYPE: Confers low-level streptomycin resistance. Seems
CC to be an important cause of resistance in resistant M.tuberculosis
CC isolates. {ECO:0000269|PubMed:17238915}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
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DR EMBL; HQ611141; ADU15870.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46748.1; -; Genomic_DNA.
DR PIR; G70851; G70851.
DR RefSeq; NP_218436.2; NC_000962.3.
DR RefSeq; WP_003899763.1; NZ_NVQJ01000005.1.
DR PDB; 7CFE; X-ray; 2.02 A; A=1-224.
DR PDBsum; 7CFE; -.
DR AlphaFoldDB; P9WGW9; -.
DR SMR; P9WGW9; -.
DR STRING; 83332.Rv3919c; -.
DR PaxDb; P9WGW9; -.
DR DNASU; 886243; -.
DR GeneID; 45427919; -.
DR GeneID; 886243; -.
DR KEGG; mtu:Rv3919c; -.
DR PATRIC; fig|83332.111.peg.4365; -.
DR TubercuList; Rv3919c; -.
DR eggNOG; COG0357; Bacteria.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31760; PTHR31760; 1.
DR Pfam; PF02527; GidB; 1.
DR PIRSF; PIRSF003078; GidB; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..224
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184283"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 119..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7CFE"
FT TURN 71..75
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 76..82
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7CFE"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:7CFE"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:7CFE"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:7CFE"
SQ SEQUENCE 224 AA; 24032 MW; B56E90FBF91A1DCA CRC64;
MSPIEPAASA IFGPRLGLAR RYAEALAGPG VERGLVGPRE VGRLWDRHLL NCAVIGELLE
RGDRVVDIGS GAGLPGVPLA IARPDLQVVL LEPLLRRTEF LREMVTDLGV AVEIVRGRAE
ESWVQDQLGG SDAAVSRAVA ALDKLTKWSM PLIRPNGRML AIKGERAHDE VREHRRVMIA
SGAVDVRVVT CGANYLRPPA TVVFARRGKQ IARGSARMAS GGTA
