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
Functions
23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity / RNA binding / rRNA (adenine-N6,N6-)-dimethyltransferase activity
Processes
response 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
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
ResourceLink
UniProtKB IDP13956
UniProtKB Entry NameERM_BACIU
GenBank Gene IDM13761
General References
  1. 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. [PubMed:3087948]
  2. 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. [PubMed:7543473]
  3. 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. [PubMed:12946350]
  4. 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. [PubMed:12907737]
  5. 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. [PubMed:9585521]
  6. 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. [PubMed:10366505]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01752S-adenosyl-L-homocysteineexperimentalunknownDetails
DB01910SinefunginexperimentalunknownDetails