RSMG_ECOLI
ID RSMG_ECOLI Reviewed; 207 AA.
AC P0A6U5; P17113; Q2M858;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE EC=2.1.1.170 {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=b3740, JW3718;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 192-207.
RC STRAIN=K12;
RX PubMed=6318052; DOI=10.1007/bf00327415;
RA Nielsen J., Joergensen B.B., von Meyenburg K., Hansen F.G.;
RT "The promoters of the atp operon of Escherichia coli K12.";
RL Mol. Gen. Genet. 193:64-71(1984).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
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 [7]
RP INDUCTION, AND MUTAGENESIS OF HIS-53; ASP-56; ASP-71; GLY-73; GLY-75;
RP GLY-77; PRO-79; ASP-96; 100-LYS-ARG-101; ARG-123; ARG-139; LYS-165 AND
RP ARG-197.
RX PubMed=22337945; DOI=10.1261/rna.029868.111;
RA Benitez-Paez A., Villarroya M., Armengod M.E.;
RT "Regulation of expression and catalytic activity of Escherichia coli RsmG
RT methyltransferase.";
RL RNA 18:795-806(2012).
RN [8]
RP MUTAGENESIS OF ASN-39.
RX DOI=10.7705/biomedica.v34i0.1702;
RA Benitez-Paez A., Cardenas-Brito S., Corredor M., Villarroya M.,
RA Armengod M.E.;
RT "Impairing methylations at ribosome RNA, a point mutation-dependent
RT strategy for aminoglycoside resistance: the rsmG case.";
RL Biomedica 34:41-49(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=12001236; DOI=10.1002/prot.10121.abs;
RA Romanowski M.J., Bonanno J.B., Burley S.K.;
RT "Crystal structure of the Escherichia coli glucose-inhibited division
RT protein B (GidB) reveals a methyltransferase fold.";
RL Proteins 47:563-567(2002).
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 527 of 16S rRNA. Requires the intact 30S subunit for
CC methylation. {ECO:0000255|HAMAP-Rule:MF_00074,
CC ECO:0000269|PubMed:17238915}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.170; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00074, ECO:0000269|PubMed:17238915};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- INDUCTION: Induced under stress conditions known to stimulate ppGpp
CC accumulation and down-regulate rRNA synthesis.
CC {ECO:0000269|PubMed:22337945}.
CC -!- DISRUPTION PHENOTYPE: Low-level streptomycin resistance.
CC {ECO:0000269|PubMed:17238915}.
CC -!- MISCELLANEOUS: Mechanisms acting on transcription regulation,
CC translation or protein stability could be responsible for adjusting
CC RsmG expression to rRNA synthesis. {ECO:0000305|PubMed:22337945}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
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DR EMBL; X01631; CAA25774.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62092.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76763.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77548.1; -; Genomic_DNA.
DR EMBL; X01383; CAA25639.1; -; Genomic_DNA.
DR PIR; C30389; BVECQB.
DR RefSeq; NP_418196.1; NC_000913.3.
DR RefSeq; WP_000932839.1; NZ_STEB01000015.1.
DR PDB; 1JSX; X-ray; 2.40 A; A=1-207.
DR PDBsum; 1JSX; -.
DR AlphaFoldDB; P0A6U5; -.
DR SMR; P0A6U5; -.
DR BioGRID; 4263261; 260.
DR BioGRID; 852552; 1.
DR DIP; DIP-47992N; -.
DR IntAct; P0A6U5; 10.
DR STRING; 511145.b3740; -.
DR jPOST; P0A6U5; -.
DR PaxDb; P0A6U5; -.
DR PRIDE; P0A6U5; -.
DR EnsemblBacteria; AAC76763; AAC76763; b3740.
DR EnsemblBacteria; BAE77548; BAE77548; BAE77548.
DR GeneID; 66672356; -.
DR GeneID; 948250; -.
DR KEGG; ecj:JW3718; -.
DR KEGG; eco:b3740; -.
DR PATRIC; fig|1411691.4.peg.2960; -.
DR EchoBASE; EB0371; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_2_2_6; -.
DR InParanoid; P0A6U5; -.
DR OMA; ICFPHLH; -.
DR PhylomeDB; P0A6U5; -.
DR BioCyc; EcoCyc:EG10376-MON; -.
DR BioCyc; MetaCyc:EG10376-MON; -.
DR BRENDA; 2.1.1.170; 2026.
DR EvolutionaryTrace; P0A6U5; -.
DR PRO; PR:P0A6U5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0070475; P:rRNA base methylation; IMP:EcoCyc.
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..207
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000184249"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 124..125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT MUTAGEN 39
FT /note="N->A: Lack of activity. Low-level streptomycin
FT resistance. Slight decrease in AdoMet affinity."
FT /evidence="ECO:0000269|Ref.8"
FT MUTAGEN 53
FT /note="H->A: Decrease in activity. Very low-level
FT streptomycin resistance. Slight decrease in AdoMet
FT affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 56
FT /note="D->A: Strong decrease in activity. Low-level
FT streptomycin resistance. Slight decrease in AdoMet
FT affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 71
FT /note="D->A: Lack of activity. Low-level streptomycin
FT resistance. 10-fold increase in AdoMet affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 73
FT /note="G->A: Slight decrease in activity. Streptomycin-
FT sensitive. Slight decrease in AdoMet affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 75
FT /note="G->A: Lack of activity. Low-level streptomycin
FT resistance. 24-fold decrease in AdoMet affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 77
FT /note="G->A: Lack of activity. Low-level streptomycin
FT resistance. 10-fold decrease in AdoMet affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 79
FT /note="P->A: Lack of activity. Low-level streptomycin
FT resistance. 11-fold decrease in AdoMet affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 96
FT /note="D->A: Lack of activity. Low-level streptomycin
FT resistance."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 100..101
FT /note="KR->AA: Lack of activity. Low-level streptomycin
FT resistance."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 123
FT /note="R->A: Slight decrease in activity. Streptomycin-
FT sensitive."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 139
FT /note="R->A: Lack of activity. Low-level streptomycin
FT resistance. No change in AdoMet affinity."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 139
FT /note="R->K: Decrease in activity. Very low-level
FT streptomycin resistance."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 165
FT /note="K->A: Slight decrease in activity. Streptomycin-
FT sensitive."
FT /evidence="ECO:0000269|PubMed:22337945"
FT MUTAGEN 197
FT /note="R->A: Strong decrease in activity. Low-level
FT streptomycin resistance."
FT /evidence="ECO:0000269|PubMed:22337945"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:1JSX"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1JSX"
FT TURN 75..79
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1JSX"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 154..167
FT /evidence="ECO:0007829|PDB:1JSX"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:1JSX"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:1JSX"
SQ SEQUENCE 207 AA; 23431 MW; 40CF9BA134E9A234 CRC64;
MLNKLSLLLK DAGISLTDHQ KNQLIAYVNM LHKWNKAYNL TSVRDPNEML VRHILDSIVV
APYLQGERFI DVGTGPGLPG IPLSIVRPEA HFTLLDSLGK RVRFLRQVQH ELKLENIEPV
QSRVEEFPSE PPFDGVISRA FASLNDMVSW CHHLPGEQGR FYALKGQMPE DEIALLPEEY
QVESVVKLQV PALDGERHLV VIKANKI
