ID   ERM1_CLOPF              Reviewed;         245 AA.
AC   P0A4D6; P12038;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ermBP;
OS   Clostridium perfringens.
OG   Plasmid pIP401.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pIP401;
RX   PubMed=1513878; DOI=10.1016/0147-619x(92)90023-4;
RA   Sloan J., Warner T.A., Scott P.T., Bannam T.L., Berryman D.I., Rood J.I.;
RT   "Construction of a sequenced Clostridium perfringens-Escherichia coli
RT   shuttle plasmid.";
RL   Plasmid 27:207-219(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CP592;
RX   PubMed=7486927; DOI=10.1128/aac.39.8.1830;
RA   Berryman D.I., Rood J.I.;
RT   "The closely related ermB-ermAM genes from Clostridium perfringens,
RT   Enterococcus faecalis (pAM beta 1), and Streptococcus agalactiae (pIP501)
RT   are flanked by variants of a directly repeated sequence.";
RL   Antimicrob. Agents Chemother. 39:1830-1834(1995).
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; L02938; AAC36955.1; -; Genomic_DNA.
DR   EMBL; U18931; AAC43480.1; -; Genomic_DNA.
DR   EMBL; X58285; CAA41221.1; -; Genomic_DNA.
DR   PIR; S16033; S16033.
DR   RefSeq; WP_002292226.1; NZ_PJSU01000021.1.
DR   AlphaFoldDB; P0A4D6; -.
DR   SMR; P0A4D6; -.
DR   GeneID; 64019358; -.
DR   GeneID; 66816186; -.
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; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..245
FT                   /note="rRNA adenine N-6-methyltransferase"
FT                   /id="PRO_0000101687"
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;  28756 MW;  4ABC65D91EFF097C CRC64;
     MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI SKQVTSIELD
     SHLFNLSSEK LKLNTRVTLI HQDILQFQFP NKQRYKIVGS IPYHLSTQII KKVVFESHAS
     DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT
     DVPDKYWKLY TYFVSKWVNR EYRQLFTKNQ FHQAMKHAKV NNLSTVTYEQ VLSIFNSYLL
     FNGRK