ID   ERMK_BACLI              Reviewed;         287 AA.
AC   P45438;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=ermK;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EMR-1;
RX   PubMed=1713206; DOI=10.1128/jb.173.15.4725-4735.1991;
RA   Kwak J.-H., Choi E.-C., Weisblum B.;
RT   "Transcriptional attenuation control of ermK, a macrolide-lincosamide-
RT   streptogramin B resistance determinant from Bacillus licheniformis.";
RL   J. Bacteriol. 173:4725-4735(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; M77505; AAA22595.1; -; Genomic_DNA.
DR   RefSeq; WP_003183781.1; NZ_RSBF01000009.1.
DR   AlphaFoldDB; P45438; -.
DR   SMR; P45438; -.
DR   PRIDE; P45438; -.
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.
FT   CHAIN           1..287
FT                   /note="rRNA adenine N-6-methyltransferase"
FT                   /id="PRO_0000101670"
FT   BINDING         25
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         52
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   287 AA;  32835 MW;  84A9E590ACC8179E CRC64;
     MKKKNHKYRG KKLNRGEYPN FSGQHLMHNK KLIEEIVDRA NISIDDTVLE LGAGKGALTT
     MLSQKAGKVL AVENDSKFVA ILTRKTAQHP NTKIIHQDIM KIHLPKEKFV VVSNIPYAIT
     TPIMKMLLNN PASGFQKGII VMEKGAAKRF TSKFIKNSYV LAWRMWFDIG IVREISKEHF
     SPPPKVDSAM VRITRKKDAP LSHKHYIAFL GLAEYALKEP QAPFCVALRG IFTPRQMKHL
     RKSLKINNEK TVGTLTENQW AVIFNTMTQY VMHHKWPRAN KRKPGEI