Protein Summary

NpmA from Escherichia coli

Full name: rRNA adenine N-1-methyltransferase
Synonym: aminoglycoside-resistance 16S rRNA methyltransferase
GI: 157734594
Orf: npmA
COG: COG0220
UniProt: A8C927
Structures: | 3P2E | 3P2I | 3P2K | 3PB3 | 3MTE | 4OX9 |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: s:1408(1408) - m1A

Comments:

Only in pathogens (KamB family).

Protein sequence:

MLILKGTKTVDLSKDELTEIIGQFDRVHIDLGTGDGRNIYKLAINDQNTF
YIGIDPVKENLFDISKKIIKKPSKGGLSNVVFVIAAAESLPFELKNIADS
ISILFPWGTLLEYVIKPNRDILSNVADLAKKEAHFEFVTTYSDSYEEAEI
KKRGLPLLSKAYFLSEQYKAELSNSGFRIDDVKELDNEYVKQFNSLWAKR
LAFGRKRSFFRVSGHVSKH

Enzymatic activities

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

Publications

Title Authors Journal Details PubMed Id DOI
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides. Wachino J, Shibayama K, Kurokawa H, Kimura K, Yamane K, Suzuki S, Shibata N, Ike Y, Arakawa Y Antimicrob Agents Chemother [details] 17875999 -
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 -
Structural basis for the methylation of A1408 in 16S rRNA by a panaminoglycoside resistance methyltransferase NpmA from a clinical isolate and analysis of the NpmA interactions with the 30S ribosomal subunit. Husain N, Obranic S, Koscinski L, Seetharaman J, Babic F, Bujnicki JM, Maravic-Vlahovicek G, Sivaraman J Nucleic Acids Res [details] 21062819 -
Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA. Dunkle JA, Vinal K, Desai PM, Zelinskaya N, Savic M, West DM, Conn GL, Dunham CM... Proc Natl Acad Sci U S A [details] 24717845 -

Last modification of this entry: 2014-04-23 11:41:16.135967
Edited by a user: magda
Edited content: Changed papers.