ERMJ_BACAN
ID ERMJ_BACAN Reviewed; 287 AA.
AC Q04720;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-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=ermJ;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=590;
RX PubMed=8473865; DOI=10.1099/00221287-139-3-601;
RA Kim H.-S., Choi E.-C., Kim B.-K.;
RT "A macrolide-lincosamide-streptogramin B resistance determinant from
RT Bacillus anthracis 590: cloning and expression of ermJ.";
RL J. Gen. Microbiol. 139:601-607(1993).
CC -!- FUNCTION: Involved in erythromycin resistance.
CC -!- SUBUNIT: Homodimer.
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; L08389; AAA22597.1; -; Genomic_DNA.
DR PIR; A47697; A47697.
DR RefSeq; WP_063844769.1; NG_047819.1.
DR AlphaFoldDB; Q04720; -.
DR SMR; Q04720; -.
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_0000101668"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 32883 MW; CAF27F2549619073 CRC64;
MKKKNHKYRG KKLNRGESPN FSGQHLMHNK KLIEEIVDRA NISIDDTVLE LGAGKGALTT
VLSQKAGKVL AVENDSKFVD ILTRKTAQHS NTKIIHQDIM KIHLPKEKFV VVSNIPYAIT
TPIMKMLLNN PASGFQKGII VMEKGAAKRF TSKFIKNSYV LAWRMWFDIG IVREISKEHF
SPPPKVDSAM VRITRKKDAP LSHKHYIAFR GLAEYALKEP NIPLCVRLRG IFTPRQMKHL
RKSLKINNEK TVGTLTENQW AVIFNTMTQY VMHHKWPRAN KRKPGEI