P02979 (ERMC1_STAAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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 on

Plasmid pE194 Ref.1 Ref.2 Ref.5
Plasmid pT48 Ref.3
Plasmid pA22 Ref.4

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Catalytic activity	2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(2085) in 23S rRNA.
Induction	By erythromycin.
Sequence similarities	Belongs to the methyltransferase superfamily. 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	response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 244	244	rRNA adenine N-6-methyltransferase		PRO_0000101682
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

	Sequence		Length	Mass (Da)
	P02979 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 3CA9A267C4FE3C30	FASTA	244	28,861
	10 20 30 40 50 60 MNEKNIKHSQ NFITSKHNID KIMTNIRLNE HDNIFEIGSG KGHFTLELVK RCNFVTAIEI 70 80 90 100 110 120 DHKLCKTTEN KLVDHDNFQV LNKDILQFKF PKNQSYKIYG NIPYNISTDI IRKIVFDSIA 130 140 150 160 170 180 NEIYLIVEYG FAKRLLNTKR SLALLLMAEV DISILSMVPR EYFHPKPKVN SSLIRLSRKK 190 200 210 220 230 240 SRISHKDKQK YNYFVMKWVN KEYKKIFTKN QFNNSLKHAG IDDLNNISFE QFLSLFNSYK LFNK

References

[1]	"Conformational alteration of mRNA structure and the posttranscriptional regulation of erythromycin-induced drug resistance." Gryczan T.J., Grandi G., Hahn J., Grandi R., Dubnau D. Nucleic Acids Res. 8:6081-6097(1980) [PubMed: 6162157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Posttranscriptional modification of mRNA conformation: mechanism that regulates erythromycin-induced resistance." Horinouchi S., Weisblum B. Proc. Natl. Acad. Sci. U.S.A. 77:7079-7083(1980) [PubMed: 6938954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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] OF 1-48.
[4]	"A Staphylococcus aureus plasmid that specifies constitutive macrolide-lincosamide-streptogramin B resistance contains a novel deletion in the ermC attenuator." Catchpole I., Dyke K.G.H. FEMS Microbiol. Lett. 57:43-47(1990) [PubMed: 2116351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[5]	"Messenger RNA from Staphylococcus aureus that specifies macrolide-lincosamide-streptogramin resistance. Demonstration of its conformations and of the leader peptide it encodes." Mayford M., Weisblum B. J. Mol. Biol. 185:769-780(1985) [PubMed: 2414456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	V01278 Genomic DNA. Translation: CAA24591.1. M37841 Genomic DNA. Translation: AAA98226.1. X54338 Genomic DNA. Translation: CAA38227.1.
PIR	YESA9E. A93717.
RefSeq	YP_025321.1. NC_005908.1.
3D structure databases
ProteinModelPortal	P02979.
SMR	P02979. Positions 9-244.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3284064.
Phylogenomic databases
ProtClustDB	CLSK884354.
Family and domain databases
InterPro	IPR023165. rRNA_Ade_diMease-like. IPR020596. rRNA_Ade_Mease_Trfase_CS. IPR001737. rRNA_Ade_methylase_transferase. IPR020598. rRNA_Ade_methylase_Trfase_N. [Graphical view]
Gene3D	G3DSA:1.10.8.100. rRNA_Ade_diMease-like. 1 hit.
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

ERMC1_STAAU

Accession

Primary (citable) accession number: P02979

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 31, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program