ID   ERMA_CORDP              Reviewed;         253 AA.
AC   P16898;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=ermA;
OS   Corynebacterium diphtheriae.
OG   Plasmid pNG2.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2110657; DOI=10.1093/nar/18.7.1891;
RA   Hodgson A.L.M., Krywult J., Radford A.J.;
RT   "Nucleotide sequence of the erythromycin resistance gene from the
RT   Corynebacterium plasmid pNG2.";
RL   Nucleic Acids Res. 18:1891-1891(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S601;
RA   Serwold-Davis T.M., Groman N.B.;
RT   "Identification of a methylase gene for erythromycin resistance within the
RT   sequence of a spontaneously deleting fragment of Corynebacterium
RT   diphtheriae plasmid pNG2.";
RL   FEMS Microbiol. Lett. 46:7-14(1988).
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; X51472; CAA35836.1; -; Genomic_DNA.
DR   EMBL; M36726; AAA98484.1; -; Genomic_DNA.
DR   PIR; S09215; S09215.
DR   RefSeq; WP_032488331.1; NG_047847.1.
DR   AlphaFoldDB; P16898; -.
DR   SMR; P16898; -.
DR   PRIDE; P16898; -.
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..253
FT                   /note="rRNA adenine N-6-methyltransferase"
FT                   /id="PRO_0000101667"
FT   REGION          229..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         61
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT   BINDING         85
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"
FT   CONFLICT        6
FT                   /note="H -> Q (in Ref. 2; AAA98484)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="S -> T (in Ref. 2; AAA98484)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244..253
FT                   /note="TPTTGSISSR -> YTNDWIDLFQVTGSSLPHHRPISPSGSSQRPPQRKNRS
FT                   RRR (in Ref. 2; AAA98484)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   253 AA;  27812 MW;  FCAA0B44D497F2C1 CRC64;
     MSAYGHGRHE HGQNFLTNHK IINSIIDLVK QTSGPIIEIG PGSGALTHPM AHLGRAITAV
     EVDAKLAAKI TQETSSAAVE VVHDDFLNFR LPATPCVIVG NIPFHLTTAI LRKLLHAPAW
     TDAVLLMQWE VARRRAGVGA STMMTAQWSP WFTFHLGSRV PRSAFRPQPN VDGGILVIRR
     VGDPKIPIEQ RKAFQAMVHT VFTARGRGIG EILRRQGCFH HVQKHNHGCA REESTPRPYL
     PDCTPTTGSI SSR