Reviewed,
UniProtKB/Swiss-Prot P13978 (ERMC3_STAAU)
Last modified
March 3, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: rRNA adenine N-6-methyltransferase EC=2.1.1.48 Alternative name(s): Macrolide-lincosamide-streptogramin B resistance protein Erythromycin resistance protein | ||
| Gene names |
| ||
| Encoded on | Plasmid pT48 | ||
| Organism | Staphylococcus aureus | ||
| Taxonomic identifier | 1280 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 244 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | This protein produces a dimethylation of the adenine residue at position 2058 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics. |
| Catalytic activity | S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing N(6)-methyladenine. |
| Sequence similarities | Belongs to the rRNA adenine N(6)-methyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance |
| Ligand | RNA-binding S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Plasmid |
| Gene Ontology (GO) | |
| Biological process | rRNA modification Inferred from electronic annotation. Source: InterPro response to antibioticInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW rRNA (adenine-N6,N6-)-dimethyltransferase activityInferred from electronic annotation. Source: InterPro rRNA (adenine-N6-)-methyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 244 | 244 | rRNA adenine N-6-methyltransferase | PRO_0000101684 | |||||
Sites | |||||||||
| Binding site | 11 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
| Binding site | 13 | 1 | S-adenosyl-L-methionine; via amide nitrogen By similarity | ||||||
| Binding site | 38 | 1 | S-adenosyl-L-methionine; via carbonyl oxygen By similarity | ||||||
| Binding site | 59 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 84 | 1 | S-adenosyl-L-methionine By similarity | ||||||
| Binding site | 101 | 1 | S-adenosyl-L-methionine By similarity | ||||||
Sequences
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References
| [1] | "The nucleotide sequence of Staphylococcus aureus plasmid pT48 conferring inducible macrolide-lincosamide-streptogramin B resistance and comparison with similar plasmids expressing constitutive resistance." Catchpole I., Thomas C., Davies A., Dyke K.G.H. J. Gen. Microbiol. 134:697-709(1988) [PubMed: 3141573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| M19652 Unassigned DNA. Translation: AAA20192.1. | |
| PIR | B46568. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1QAN based on UniProtKB P13956. |
| SMR | P13978. Positions 10-244. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.1.1.48. 95. |
Family and domain databases | |
| InterPro | IPR001737. RRNA_Ade_Mease_Trfase. [Graphical view] |
| PANTHER | PTHR11727. RRNA_meth_trans. 1 hit. |
| Pfam | PF00398. RrnaAD. 1 hit. [Graphical view] |
| SMART | SM00650. rADc. 1 hit. [Graphical view] |
| PROSITE | PS01131. RRNA_A_DIMETH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ERMC3_STAAU | ||||||||
| Accession | Primary (citable) accession number: P13978 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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