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P13956 (ERM_BACIU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:ermC'
Encoded onPlasmid pIM13
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.3 Ref.4

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 class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.

Caution

In the genome of Neisseria meningitidis (serogroup B), the gene for this protein is present (NMB0066). It was introduced as part of a construct built to neutralize the virulence of the bacterium.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244rRNA adenine N-6-methyltransferase
PRO_0000101674

Sites

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

Experimental info

Mutagenesis111N → A: Reduces activity about 3-fold.
Mutagenesis1011N → A: Decreases affinity for S-adenosyl-L-methionine 4-fold. Reduces activity by 90%. Ref.3
Mutagenesis1041Y → A: Loss of activity. Ref.3
Mutagenesis1081T → A: Decreases affinity for S-adenosyl-L-methionine 8-fold. Reduces activity by 99%. Ref.4
Mutagenesis1121R → A: Reduces activity by 90%. Ref.4
Mutagenesis1121R → D: Decreases affinity for S-adenosyl-L-methionine 5-fold. Decreases affinity for RNA 6-fold. Reduces activity by 99%. Ref.4
Mutagenesis1331K → A: Reduces activity by about 80%. Ref.4
Mutagenesis1341R → A: Decreases affinity for S-adenosyl-L-methionine 7-fold. Decreases affinity for RNA about 4-fold. Reduces activity by over 99%. May severely impair protein folding. Ref.4
Mutagenesis1401R → A: Decreases affinity for S-adenosyl-L-methionine 7-fold. Reduces activity by about 85%. Ref.4
Mutagenesis1651P → A: Decreases affinity for S-adenosyl-L-methionine 6-fold. Reduces activity by about 96%. Ref.3
Mutagenesis1661K → A: Decreases affinity for RNA about 6-fold. Ref.3

Secondary structure

............................................ 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13956 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: FC7CA6524034D820

FASTA24428,907
        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 SLALFLMAEV DISILSMVPR EYFHPKPKVN SSLIRLNRKK 

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


LFNK 

« Hide

References

[1]"Sequence and properties of pIM13, a macrolide-lincosamide-streptogramin B resistance plasmid from Bacillus subtilis."
Monod M., Denoya C., Dubnau D.
J. Bacteriol. 167:138-147(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Substrate requirements for ErmC' methyltransferase activity."
Zhong P., Pratt S.D., Edalji R.P., Walter K.A., Holzman T.F., Shivakumar A.G., Katz L.
J. Bacteriol. 177:4327-4332(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC'."
Maravic G., Feder M., Pongor S., Floegel M., Bujnicki J.M.
J. Mol. Biol. 332:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-101; TYR-104; PRO-165 AND LYS-166, RNA-BINDING, FUNCTION.
[4]"Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions."
Maravic G., Bujnicki J.M., Feder M., Pongor S., Floegel M.
Nucleic Acids Res. 31:4941-4949(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF THR-108; ARG-112; LYS-133; ARG-134 AND ARG-140, RNA-BINDING, FUNCTION.
[5]"Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria."
Bussiere D.E., Muchmore S.W., Dealwis C.G., Schluckebier G., Nienaber V.L., Edalji R.P., Walter K.A., Ladror U.S., Holzman T.F., Abad-Zapatero C.
Biochemistry 37:7103-7112(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-244.
Strain: BD1109.
[6]"The 2.2-A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism."
Schluckebier G., Zhong P., Stewart K.D., Kavanaugh T.J., Abad-Zapatero C.
J. Mol. Biol. 289:277-291(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-METHIONINE AND SUBSTRATE ANALOGS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13761 Genomic DNA. Translation: AAA98136.1.
PIRB25233.
RefSeqNP_040407.1. NC_001376.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QAMX-ray2.20A1-244[»]
1QANX-ray2.40A1-244[»]
1QAOX-ray2.70A1-244[»]
1QAQX-ray2.80A1-244[»]
2ERCX-ray3.03A/B1-244[»]
ProteinModelPortalP13956.
SMRP13956. Positions 9-244.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP13956.
ChEMBLCHEMBL4251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1263203.

Family and domain databases

Gene3D1.10.8.100. 1 hit.
3.40.50.150. 1 hit.
InterProIPR023165. rRNA_Ade_diMease-like.
IPR020596. rRNA_Ade_Mease_Trfase_CS.
IPR001737. rRNA_Ade_methylase_transferase.
IPR020598. rRNA_Ade_methylase_Trfase_N.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR11727. PTHR11727. 1 hit.
PfamPF00398. RrnaAD. 1 hit.
[Graphical view]
SMARTSM00650. rADc. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS01131. RRNA_A_DIMETH. 1 hit.
PS51689. SAM_RNA_A_N6_MT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13956.

Entry information

Entry nameERM_BACIU
AccessionPrimary (citable) accession number: P13956
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 11, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references