ID   ERMA_STAAU              Reviewed;         243 AA.
AC   P0A0H3; P06699;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=ermA;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TRANSPOSON=Tn554;
RX   PubMed=3004956; DOI=10.1002/j.1460-2075.1985.tb04089.x;
RA   Murphy E., Huwyler L., Do Carno de Freire Bastos M.;
RT   "Transposon Tn554: complete nucleotide sequence and isolation of
RT   transposition-defective and antibiotic-sensitive mutants.";
RL   EMBO J. 4:3357-3365(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2985541; DOI=10.1128/jb.162.2.633-640.1985;
RA   Murphy E.;
RT   "Nucleotide sequence of ermA, a macrolide-lincosamide-streptogramin B
RT   determinant in Staphylococcus aureus.";
RL   J. Bacteriol. 162:633-640(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   -!- 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; X03216; CAA26964.1; -; Genomic_DNA.
DR   PIR; E24584; A25101.
DR   RefSeq; WP_001072201.1; NZ_WWCF01000004.1.
DR   RefSeq; YP_006958113.1; NC_019144.1.
DR   AlphaFoldDB; P0A0H3; -.
DR   SMR; P0A0H3; -.
DR   GeneID; 42043719; -.
DR   GeneID; 58051003; -.
DR   KEGG; ag:CAA26964; -.
DR   OMA; RHEHGQN; -.
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   3: Inferred from homology;
KW   Antibiotic resistance; Methyltransferase; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; Transposable element.
FT   CHAIN           1..243
FT                   /note="rRNA adenine N-6-methyltransferase"
FT                   /id="PRO_0000101681"
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   243 AA;  28408 MW;  03DDAFABE867525A CRC64;
     MNQKNPKDTQ NFITSKKHVK EILNHTNISK QDNVIEIGSG KGHFTKELVK MSRSVTAIEI
     DGGLCQVTKE AVNPSENIKV IQTDILKFSF PKHINYKIYG NIPYNISTDI VKRITFESQA
     KYSYLIVEKG FAKRLQNLQR ALGLLLMVEM DIKMLKKVPP LYFHPKPSVD SVLIVLERHQ
     PLISKKDYKK YRSFVYKWVN REYRVLFTKN QFRQALKHAN VTNINKLSKE QFLSIFNSYK
     LFH