ERMC1_STAAU
ID ERMC1_STAAU Reviewed; 244 AA.
AC P02979;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=rRNA adenine N-6-methyltransferase;
DE EC=2.1.1.184;
DE AltName: Full=Erythromycin resistance protein;
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN Name=ermC;
OS Staphylococcus aureus.
OG Plasmid pE194, Plasmid pT48, and Plasmid pA22.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pE194;
RX PubMed=6162157; DOI=10.1093/nar/8.24.6081;
RA Gryczan T.J., Grandi G., Hahn J., Grandi R., Dubnau D.;
RT "Conformational alteration of mRNA structure and the posttranscriptional
RT regulation of erythromycin-induced drug resistance.";
RL Nucleic Acids Res. 8:6081-6097(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pE194;
RX PubMed=6938954; DOI=10.1073/pnas.77.12.7079;
RA Horinouchi S., Weisblum B.;
RT "Posttranscriptional modification of mRNA conformation: mechanism that
RT regulates erythromycin-induced resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:7079-7083(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
RC PLASMID=pT48;
RX PubMed=3141573; DOI=10.1099/00221287-134-3-697;
RA Catchpole I., Thomas C., Davies A., Dyke K.G.H.;
RT "The nucleotide sequence of Staphylococcus aureus plasmid pT48 conferring
RT inducible macrolide-lincosamide-streptogramin B resistance and comparison
RT with similar plasmids expressing constitutive resistance.";
RL J. Gen. Microbiol. 134:697-709(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC PLASMID=pA22;
RX PubMed=2116351; DOI=10.1016/0378-1097(90)90410-r;
RA Catchpole I., Dyke K.G.H.;
RT "A Staphylococcus aureus plasmid that specifies constitutive macrolide-
RT lincosamide-streptogramin B resistance contains a novel deletion in the
RT ermC attenuator.";
RL FEMS Microbiol. Lett. 57:43-47(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC PLASMID=pE194;
RX PubMed=2414456; DOI=10.1016/0022-2836(85)90061-0;
RA Mayford M., Weisblum B.;
RT "Messenger RNA from Staphylococcus aureus that specifies macrolide-
RT lincosamide-streptogramin resistance. Demonstration of its conformations
RT and of the leader peptide it encodes.";
RL J. Mol. Biol. 185:769-780(1985).
CC -!- FUNCTION: This protein produces a dimethylation of the adenine residue
CC at position 2085 in 23S rRNA, resulting in reduced affinity between
CC ribosomes and macrolide-lincosamide-streptogramin B antibiotics.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2
CC H(+) + N(6)-dimethyladenosine(2085) in 23S rRNA + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:42784, Rhea:RHEA-COMP:10237, Rhea:RHEA-
CC COMP:10238, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.184;
CC -!- INDUCTION: By erythromycin.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01026}.
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DR EMBL; V01278; CAA24591.1; -; Genomic_DNA.
DR EMBL; M37841; AAA98226.1; -; Genomic_DNA.
DR EMBL; X54338; CAA38227.1; -; Genomic_DNA.
DR PIR; A93717; YESA9E.
DR RefSeq; WP_007410443.1; NZ_VRQI01000067.1.
DR RefSeq; YP_009060503.1; NC_024964.1.
DR RefSeq; YP_025321.1; NC_005908.1.
DR AlphaFoldDB; P02979; -.
DR SMR; P02979; -.
DR BindingDB; P02979; -.
DR ChEMBL; CHEMBL4295563; -.
DR GO; GO:0052910; F:23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.100; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; PTHR11727; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Methyltransferase; Plasmid; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..244
FT /note="rRNA adenine N-6-methyltransferase"
FT /id="PRO_0000101682"
FT BINDING 11
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 244 AA; 28861 MW; 3CA9A267C4FE3C30 CRC64;
MNEKNIKHSQ NFITSKHNID KIMTNIRLNE HDNIFEIGSG KGHFTLELVK RCNFVTAIEI
DHKLCKTTEN KLVDHDNFQV LNKDILQFKF PKNQSYKIYG NIPYNISTDI IRKIVFDSIA
NEIYLIVEYG FAKRLLNTKR SLALLLMAEV DISILSMVPR EYFHPKPKVN SSLIRLSRKK
SRISHKDKQK YNYFVMKWVN KEYKKIFTKN QFNNSLKHAG IDDLNNISFE QFLSLFNSYK
LFNK
