ERMB_ENTFA
ID ERMB_ENTFA Reviewed; 245 AA.
AC P20173;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=rRNA adenine N-6-methyltransferase;
DE EC=2.1.1.184;
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN Name=ermB; OrderedLocusNames=EF_A0007;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OG Plasmid pTEF1, and Plasmid pAD2.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS16; PLASMID=pAD2; TRANSPOSON=Tn917;
RX PubMed=2997130; DOI=10.1128/jb.164.2.782-796.1985;
RA Shaw J.H., Clewell D.B.;
RT "Complete nucleotide sequence of macrolide-lincosamide-streptogramin B-
RT resistance transposon Tn917 in Streptococcus faecalis.";
RL J. Bacteriol. 164:782-796(1985).
RN [2]
RP SEQUENCE REVISION TO 14.
RA Flannagan S.E., Clewell D.B.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583; PLASMID=pTEF1;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; M11180; AAA27452.2; -; Genomic_DNA.
DR EMBL; AE016833; AAO83009.1; -; Genomic_DNA.
DR PIR; B25028; B25028.
DR RefSeq; NP_816938.1; NC_004669.1.
DR RefSeq; WP_001038790.1; NZ_KE136530.1.
DR AlphaFoldDB; P20173; -.
DR SMR; P20173; -.
DR EnsemblBacteria; AAO83009; AAO83009; EF_A0007.
DR GeneID; 60887343; -.
DR GeneID; 67042603; -.
DR KEGG; ag:AAA27452; -.
DR KEGG; efa:EFA0007; -.
DR PATRIC; fig|226185.45.peg.2807; -.
DR HOGENOM; CLU_041220_3_3_9; -.
DR OMA; RHEHGQN; -.
DR PRO; PR:P20173; -.
DR Proteomes; UP000001415; Plasmid pTEF1.
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; Plasmid; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; Transposable element.
FT CHAIN 1..245
FT /note="rRNA adenine N-6-methyltransferase"
FT /id="PRO_0000101689"
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 12
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 245 AA; 28796 MW; FFFEBA441C8511D0 CRC64;
MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI SKQVTSIELD
SHLFNLSSEK LKLNIRVTLI HQDILQFQFP NKQRYKIVGN IPYHLSTQII KKVVFESHAS
DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT
DVPDKYWKLY TYFVSKWVNR EYRQLFTKNQ FHQAMKHAKV NNLSTVTYEQ VLSIFNSYLL
FNGRK
