Full name: rRNA adenine N-1-methyltransferase
Synonym: aminoglycoside-resistance 16S rRNA methyltransferase
GI: 85813531
Orf: kamB
COG: COG4106
UniProt: P25920
Structures: | 3MQ2 |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: s:1408(1408) - m1A

Comments:

KamB catalyzes the formation of m1A at position 1408 in helix 44 of 16 rRNA and provides panaminoglycoside-resistant nature through interference with the binding of aminoglycosides to the A site of 16S rRNA. Plasmid–mediated NpmA present in certain pathogenic E. coli has the same function. Methylation site was determined for E. coli rRNA.

Protein sequence:

MEKISAKAAAKPAKGGLPNLLYLWATAERLPPLSGVGELHVLMPWGSLLRGVLGSSPEMLRGMAAVCRPG ASFLVALNLHAWRPSVPEVGEHPEPTPDSADEWLAPRYAEAGWKLADCRYLEPEEVAGLETSWTRRLHSS RDRFDVLALTGTISP

Enzymatic activities:

Reaction Substrate Type Position
A:m1A rRNA (r) SSU/16S/prokaryotic cytosol 1408

Publications:

Title Authors Journal Details PubMed Id DOI
Structural insights into the function of aminoglycoside-resistance A1408 16S rRNA methyltransferases from antibiotic-producing and human pathogenic bacteria. Macmaster R, Zelinskaya N, Savic M, Rankin CR, Conn GL Nucleic Acids Res [details] 20639535 -
Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics. Savic M, Lovric J, Tomic TI, Vasiljevic B, Conn GL... Nucleic Acids Res [details] 19589804 -

Links:

_Wikipedia - antibiotic resistance_
_PubMed_
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