ERME_SACEN
ID ERME_SACEN Reviewed; 381 AA.
AC P07287; A4F7Q0; Q54094;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=rRNA adenine N-6-methyltransferase;
DE Short=NMT;
DE EC=2.1.1.184;
DE AltName: Full=Erythromycin resistance protein;
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein;
GN Name=ermE; OrderedLocusNames=SACE_0733;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3934045; DOI=10.1016/0378-1119(85)90208-2;
RA Uchiyama H., Weisblum B.;
RT "N-methyl transferase of Streptomyces erythraeus that confers resistance to
RT the macrolide-lincosamide-streptogramin B antibiotics: amino acid sequence
RT and its homology to cognate R-factor enzymes from pathogenic bacilli and
RT cocci.";
RL Gene 38:103-110(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2335200; DOI=10.1016/0014-5793(90)80186-m;
RA Dhillon N., Leadlay P.F.;
RT "A repeated decapeptide motif in the C-terminal domain of the ribosomal RNA
RT methyltransferase from the erythromycin producer Saccharopolyspora
RT erythraea.";
RL FEBS Lett. 262:189-193(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-133.
RX PubMed=2998943; DOI=10.1016/0378-1119(85)90220-3;
RA Bibb M.J., Janssen G.R., Ward J.M.;
RT "Cloning and analysis of the promoter region of the erythromycin resistance
RT gene (ermE) of Streptomyces erythraeus.";
RL Gene 38:215-226(1985).
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; M11200; AAA26492.1; -; Genomic_DNA.
DR EMBL; AM420293; CAM00074.1; -; Genomic_DNA.
DR EMBL; X51891; CAB60001.1; -; Genomic_DNA.
DR PIR; A91534; XYSMRE.
DR RefSeq; WP_009950391.1; NZ_PDBV01000001.1.
DR RefSeq; WP_063844770.1; NG_047821.1.
DR PDB; 6NVM; X-ray; 1.75 A; A=1-290.
DR PDBsum; 6NVM; -.
DR AlphaFoldDB; P07287; -.
DR SMR; P07287; -.
DR STRING; 405948.SACE_0733; -.
DR EnsemblBacteria; CAM00074; CAM00074; SACE_0733.
DR KEGG; ag:CAB60001; -.
DR KEGG; sen:SACE_0733; -.
DR eggNOG; COG0030; Bacteria.
DR HOGENOM; CLU_041220_3_1_11; -.
DR OMA; AIHRREH; -.
DR OrthoDB; 2030110at2; -.
DR BioCyc; MetaCyc:MON-17659; -.
DR Proteomes; UP000006728; Chromosome.
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; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..381
FT /note="rRNA adenine N-6-methyltransferase"
FT /id="PRO_0000101677"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01026"
FT CONFLICT 71
FT /note="G -> V (in Ref. 1; AAA26492)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..201
FT /note="Missing (in Ref. 1; AAA26492)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="L -> F (in Ref. 1; AAA26492)"
FT /evidence="ECO:0000305"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:6NVM"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:6NVM"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:6NVM"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6NVM"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 219..234
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6NVM"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:6NVM"
SQ SEQUENCE 381 AA; 43001 MW; 17A7C78CAD865FA9 CRC64;
MSSSDEQPRP RRRNQDRQHP NQNRPVLGRT ERDRNRRQFG QNFLRDRKTI ARIAETAELR
PDLPVLEAGP GEGLLTRELA DRARQVTSYE IDPRLAKSLR EKLSGHPNIE VVNADFLTAE
PPPEPFAFVG AIPYGITSAI VDWCLEAPTI ETATMVTQLE FARKRTGDYG RWSRLTVMTW
PLFEWEFVEK VDRRLFKPVP KVDSAIMRLR RRAEPLLEGA ALERYESMVE LCFTGVGGNI
QASLLRKYPR RRVEAALDHA GVGGGAVVAY VRPEQWLRLF ERLDQKNEPR GGQPQRGRRT
GGRDHGDRRT GGQDRGDRRT GGRDHRDRQA SGHGDRRSSG RNRDDGRTGE REQGDQGGRR
GPSGGGRTGG RPGRRGGPGQ R
