Full name: Ribosomal RNA small subunit methyltransferase G
Synonym: gidB
GI: 121190
Orf:
COG: COG0357
UniProt: P25813
Structures: | 1XDZ |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: s:533(527) - m7G

Comments:

RsmG is responsible for the synthesis of m7G535 (position 527 in E. coli) in the universally conserved loop of hairpin 18 in domain I. This modified nucleotide plays an essential role in binding antibiotics like streptomycin and kasugamycin. However the dependence on RsmG for antibiotic binding depends on the activity of RsmA (KsgA) catalyzing the formation of m6,6A1518,1519 at the 3'-end of 16S rRNA by RsmA (KsgA). In B. subtilis, mutations in both RsmA and RsmG allow better cell viability in the presence of antibiotics. AdoMet is the methyl group donor.

Protein sequence:

MNIEEFTSGLAEKGISLSPRQLEQFELYYDMLVEWNEKINLTSITEKKEVYLKHFYDSITAAFYVDFNQV NTICDVGAGAGFPSLPIKICFPHLHVTIVDSLNKRITFLEKLSEALQLENTTFCHDRAETFGQRKDVRES YDIVTARAVARLSVLSELCLPLVKKNGLFVALKAASAEEELNAGKKAITTLGGELENIHSFKLPIEESDR NIMVIRKIKNTPKKYPRKPGTPNKSPIEG

Enzymatic activities:

Reaction Substrate Type Position
G:m7G rRNA (r) SSU/16S/prokaryotic cytosol 535

Publications:

Title Authors Journal Details PubMed Id DOI
Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants. Nishimura K, Johansen SK, Inaoka T, Hosaka T, Tokuyama S, Tahara Y, Okamoto S, Kawamura F, Douthwaite S, Ochi K J Bacteriol [details] 17573471 -
Inactivation of KsgA, a 16S rRNA methyltransferase, causes vigorous emergence of mutants with high-level kasugamycin resistance. Ochi K, Kim JY, Tanaka Y, Wang G, Masuda K, Nanamiya H, Okamoto S, Tokuyama S, Adachi Y, Kawamura F Antimicrob Agents Chemother [details] 19001112 -
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