ERMA_STAAN
ID ERMA_STAAN Reviewed; 243 AA.
AC P0A0H2; P06699;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=ermA1; OrderedLocusNames=SA0048;
GN and
GN Name=ermA2; OrderedLocusNames=SA1480;
GN and
GN Name=ermA3; OrderedLocusNames=SA0766;
GN and
GN Name=ermA4; OrderedLocusNames=SA1951;
GN and
GN Name=ermA5; OrderedLocusNames=SA2384;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10348769; DOI=10.1128/aac.43.6.1449;
RA Ito T., Katayama Y., Hiramatsu K.;
RT "Cloning and nucleotide sequence determination of the entire mec DNA of
RT pre-methicillin-resistant Staphylococcus aureus N315.";
RL Antimicrob. Agents Chemother. 43:1449-1458(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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 {ECO:0000250}.
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; D86934; BAA82205.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB41266.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB42003.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB42746.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB43235.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB43689.1; -; Genomic_DNA.
DR RefSeq; WP_001072201.1; NC_002745.2.
DR RefSeq; YP_006958113.1; NC_019144.1.
DR AlphaFoldDB; P0A0H2; -.
DR SMR; P0A0H2; -.
DR BindingDB; P0A0H2; -.
DR ChEMBL; CHEMBL4295568; -.
DR EnsemblBacteria; BAB41266; BAB41266; BAB41266.
DR EnsemblBacteria; BAB42003; BAB42003; BAB42003.
DR EnsemblBacteria; BAB42746; BAB42746; BAB42746.
DR EnsemblBacteria; BAB43235; BAB43235; BAB43235.
DR EnsemblBacteria; BAB43689; BAB43689; BAB43689.
DR GeneID; 42043719; -.
DR GeneID; 58051003; -.
DR KEGG; sau:SA0048; -.
DR KEGG; sau:SA0766; -.
DR KEGG; sau:SA1480; -.
DR KEGG; sau:SA1951; -.
DR KEGG; sau:SA2384; -.
DR HOGENOM; CLU_041220_3_3_9; -.
DR OMA; RHEHGQN; -.
DR Proteomes; UP000000751; Chromosome.
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 1: Evidence at protein level;
KW Antibiotic resistance; Methyltransferase; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..243
FT /note="rRNA adenine N-6-methyltransferase"
FT /id="PRO_0000101679"
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
