ERM_STREE
ID ERM_STREE Reviewed; 245 AA.
AC P21236;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=rRNA adenine N-6-methyltransferase;
DE EC=2.1.1.184;
DE AltName: Full=ErmAM;
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN Name=erm;
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn1545;
RX PubMed=2163525; DOI=10.1093/nar/18.12.3660;
RA Trieu-Cuot P., Poyart-Salmeron C., Carlier C., Courvalin P.;
RT "Nucleotide sequence of the erythromycin resistance gene of the conjugative
RT transposon Tn1545.";
RL Nucleic Acids Res. 18:3660-3660(1990).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=9187657; DOI=10.1038/nsb0697-483;
RA Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K.,
RA Holzman T.F., Fesik S.W.;
RT "Solution structure of an rRNA methyltransferase (ErmAM) that confers
RT macrolide-lincosamide-streptogramin antibiotic resistance.";
RL Nat. Struct. Biol. 4:483-489(1997).
RN [3]
RP ERRATUM OF PUBMED:9187657.
RA Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K.,
RA Holzman T.F., Fesik S.W.;
RL Nat. Struct. Biol. 4:592-592(1997).
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; X52632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S12727; S12727.
DR PDB; 1YUB; NMR; -; A=1-245.
DR PDBsum; 1YUB; -.
DR AlphaFoldDB; P21236; -.
DR SMR; P21236; -.
DR BindingDB; P21236; -.
DR ChEMBL; CHEMBL2757; -.
DR EvolutionaryTrace; P21236; -.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Methyltransferase; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Transposable element.
FT CHAIN 1..245
FT /note="rRNA adenine N-6-methyltransferase"
FT /id="PRO_0000101690"
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"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 45..50
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1YUB"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1YUB"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1YUB"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1YUB"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:1YUB"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:1YUB"
SQ SEQUENCE 245 AA; 28783 MW; 5E3AB1BAAA6511C5 CRC64;
MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI SKQVTSIELD
SHLFNLSSEK LKLNIRVTLI HQDILQFQFP NKQRYKIVGS IPYHLSTQII KKVVFESHAS
DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT
DVPDKYWKLY TYFVSKWVNR EYRQLFTKNQ FHQAMKHAKV NNLSTITYEQ VLSIFNSYLL
FNGRK
