ID   ERMU_BACFG              Reviewed;         266 AA.
AC   Q02607;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=rRNA adenine N-6-methyltransferase;
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01026};
DE   AltName: Full=Erythromycin resistance protein;
DE   AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN   Name=ermFU;
OS   Bacteroides fragilis.
OG   Plasmid V503.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1905805; DOI=10.1093/nar/19.12.3453;
RA   Halula M., Manning S., Macrina F.L.;
RT   "Nucleotide sequence of ermFU, a macrolide-lincosamide-streptogramin (MLS)
RT   resistance gene encoding an RNA methylase from the conjugal element of
RT   Bacteroides fragilis V503.";
RL   Nucleic Acids Res. 19:3453-3453(1991).
CC   -!- FUNCTION: Involved in erythromycin resistance.
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; M62487; AAA63165.1; -; Genomic_DNA.
DR   RefSeq; WP_063844771.1; NG_047823.1.
DR   AlphaFoldDB; Q02607; -.
DR   SMR; Q02607; -.
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; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..266
FT                   /note="rRNA adenine N-6-methyltransferase"
FT                   /id="PRO_0000101672"
FT   BINDING         14
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         16
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         41
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         87
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   266 AA;  30424 MW;  B9F2ABD4B1AFE9C0 CRC64;
     MTKKKLPLRF TGQHFTIDKV LIKDAIRQAN ISNQDTVLDI GAGKGFLTVH LLKIANNVVA
     IENDTALVEH LRKLFSDARN VQVVGCDFRN FAVPKFPFKV VSNIPYGITS DIFKILMFEN
     LENFLGGSIV LQFEPTQKLF SRKLYNPYTV FYHTFFDLKL VYEVGPESFL PPPTVKSALL
     NIKRKHLFFD FKIKAKYLAF ISCLLEKPDL SVKTALKSIF RKSQVRTISE KFGLNLNAQI
     VCLSPSQWLN CFLEMLEVVP EKFHPS