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P06572 (ERMM_STAEP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
rRNA adenine N-6-methyltransferase

EC=2.1.1.184
Alternative name(s):
Erythromycin resistance protein
Macrolide-lincosamide-streptogramin B resistance protein
Gene names
Name:ermM
Encoded onPlasmid pNE131
OrganismStaphylococcus epidermidis
Taxonomic identifier1282 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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.

Catalytic activity

2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(2085) in 23S rRNA.

Sequence similarities

Belongs to the methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termPlasmid
Gene Ontology (GO)
   Biological processresponse to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

rRNA (adenine-N6,N6-)-dimethyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244rRNA adenine N-6-methyltransferase
PRO_0000101685

Sites

Binding site111S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site131S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site381S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site591S-adenosyl-L-methionine By similarity
Binding site841S-adenosyl-L-methionine By similarity
Binding site1011S-adenosyl-L-methionine By similarity

Sequences

Sequence LengthMass (Da)Tools
P06572 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 765404D860B6D620

FASTA24428,941
        10         20         30         40         50         60 
MNEKNIKHSQ NFITSKHNID KIMTNIRLNE HDNIFEIGSG KGHFTLELVQ RCNFVTAIEI 

        70         80         90        100        110        120 
DHKLCKTTEN KLVDHDNFQV LNKDILQFKF PKNQSYKIFG NIPYNISTDI IRKIVFDSIA 

       130        140        150        160        170        180 
DEIYLIVEYG FAKRLLNTKR SFALFLMAEV DISILSMVPR EYFHPKPKVN SSLIRLNRKK 

       190        200        210        220        230        240 
SRISHKDKQK YNYFVMKWVN KEYKKIFTKN QFNNSLKHAG IDDLNNISFE QFLSLFNSYK 


LFNK 

« Hide

References

[1]"Nucleotide sequence of the constitutive macrolide-lincosamide-streptogramin B resistance plasmid pNE131 from Staphylococcus epidermidis and homologies with Staphylococcus aureus plasmids pE194 and pSN2."
Lampson B.C., Parisi J.T.
J. Bacteriol. 167:888-892(1986) [PubMed: 3091582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Naturally occurring Staphylococcus epidermidis plasmid expressing constitutive macrolide-lincosamide-streptogramin B resistance contains a deleted attenuator."
Lampson B.C., Parisi J.T.
J. Bacteriol. 166:479-483(1986) [PubMed: 3084450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12730 Genomic DNA. Translation: AAA98296.1.
PIRA24497.

3D structure databases

ProteinModelPortalP06572.
SMRP06572. Positions 9-244.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

ProtClustDBCLSK884354.

Family and domain databases

InterProIPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR001737. rRNA_Ade_methylase_transferase.
IPR020598. rRNA_Ade_methylase_Trfase_N.
[Graphical view]
Gene3DG3DSA:1.10.8.100. rRNA_Ade_diMease-like. 1 hit.
PANTHERPTHR11727. RRNA_meth_trans. 1 hit.
PfamPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTSM00650. rADc. 1 hit.
[Graphical view]
PROSITEPS01131. RRNA_A_DIMETH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameERMM_STAEP
AccessionPrimary (citable) accession number: P06572
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 31, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families