rRNA adenine N-6-methyltransferase
Details
- Name
- rRNA adenine N-6-methyltransferase
- Synonyms
- 2.1.1.184
- Erythromycin resistance protein
- Macrolide-lincosamide-streptogramin B resistance protein
- Gene Name
- ermC'
- Organism
- Bacillus subtilis
- Amino acid sequence
>lcl|BSEQ0019300|rRNA adenine N-6-methyltransferase MNEKNIKHSQNFITSKHNIDKIMTNIRLNEHDNIFEIGSGKGHFTLELVQRCNFVTAIEI DHKLCKTTENKLVDHDNFQVLNKDILQFKFPKNQSYKIFGNIPYNISTDIIRKIVFDSIA DEIYLIVEYGFAKRLLNTKRSLALFLMAEVDISILSMVPREYFHPKPKVNSSLIRLNRKK SRISHKDKQKYNYFVMKWVNKEYKKIFTKNQFNNSLKHAGIDDLNNISFEQFLSLFNSYK LFNK
- Number of residues
- 244
- Molecular Weight
- 28907.235
- Theoretical pI
- 10.2
- GO Classification
- Functions23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity / RNA binding / rRNA (adenine-N6,N6-)-dimethyltransferase activityProcessesresponse to antibiotic
- General Function
- Rrna (adenine-n6,n6-)-dimethyltransferase activity
- Specific Function
- This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.
- Pfam Domain Function
- RrnaAD (PF00398)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0019301|rRNA adenine N-6-methyltransferase (ermC') ATGAACGAGAAAAATATAAAACACAGTCAAAACTTTATTACTTCAAAACATAATATAGAT AAAATAATGACAAATATAAGATTAAATGAACATGATAATATCTTTGAAATCGGCTCAGGA AAAGGGCATTTTACCCTTGAATTAGTACAGAGGTGTAATTTCGTAACTGCCATTGAAATA GACCATAAATTATGCAAAACTACAGAAAATAAACTTGTTGATCACGATAATTTCCAAGTT TTAAACAAGGATATATTGCAGTTTAAATTTCCTAAAAACCAATCCTATAAAATATTTGGT AATATACCTTATAACATAAGTACGGATATAATACGCAAAATTGTTTTTGATAGTATAGCT GATGAGATTTATTTAATCGTGGAATACGGGTTTGCTAAAAGATTATTAAATACAAAACGC TCATTGGCATTATTTTTAATGGCAGAAGTTGATATTTCTATATTAAGTATGGTTCCAAGA GAATATTTTCATCCTAAACCTAAAGTGAATAGCTCACTTATCAGATTAAATAGAAAAAAA TCAAGAATATCACACAAAGATAAACAGAAGTATAATTATTTCGTTATGAAATGGGTTAAC AAAGAATACAAGAAAATATTTACAAAAAATCAATTTAACAATTCCTTAAAACATGCAGGA ATTGACGATTTAAACAATATTAGCTTTGAACAATTCTTATCTCTTTTCAATAGCTATAAA TTATTTAATAAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13956 UniProtKB Entry Name ERM_BACIU GenBank Gene ID M13761 - General References
- Monod M, Denoya C, Dubnau D: Sequence and properties of pIM13, a macrolide-lincosamide-streptogramin B resistance plasmid from Bacillus subtilis. J Bacteriol. 1986 Jul;167(1):138-47. [Article]
- Zhong P, Pratt SD, Edalji RP, Walter KA, Holzman TF, Shivakumar AG, Katz L: Substrate requirements for ErmC' methyltransferase activity. J Bacteriol. 1995 Aug;177(15):4327-32. [Article]
- Maravic G, Feder M, Pongor S, Flogel M, Bujnicki JM: Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC'. J Mol Biol. 2003 Sep 5;332(1):99-109. [Article]
- Maravic G, Bujnicki JM, Feder M, Pongor S, Flogel M: Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions. Nucleic Acids Res. 2003 Aug 15;31(16):4941-9. [Article]
- Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C: Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria. Biochemistry. 1998 May 19;37(20):7103-12. [Article]
- Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C: The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism. J Mol Biol. 1999 Jun 4;289(2):277-91. [Article]