ID Q799N2_STAAU Unreviewed; 245 AA.
AC Q799N2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 08-NOV-2023, entry version 116.
DE RecName: Full=rRNA adenine N-6-methyltransferase {ECO:0000256|ARBA:ARBA00016505};
DE EC=2.1.1.184 {ECO:0000256|ARBA:ARBA00012304};
DE AltName: Full=Erythromycin resistance protein {ECO:0000256|ARBA:ARBA00030809};
DE AltName: Full=Macrolide-lincosamide-streptogramin B resistance protein {ECO:0000256|ARBA:ARBA00029941};
GN Name=ORF245 {ECO:0000313|EMBL:CAA73921.1};
GN Synonyms=ermB {ECO:0000313|EMBL:ABQ00061.1};
GN ORFNames=SAP013A_023 {ECO:0000313|EMBL:ADA61298.1};
OS Staphylococcus aureus.
OG Plasmid p45547X {ECO:0000313|EMBL:AHJ80338.1}, and
OG Plasmid pI258 {ECO:0000313|EMBL:ADA61298.1}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:CAA73921.1};
RN [1] {ECO:0000313|EMBL:CAA73921.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=COL {ECO:0000313|EMBL:CAA73921.1};
RX PubMed=10332716;
RA Wu S., de Lencastre H.;
RT "The Staphylococcus aureus transposon Tn551: complete nucleotide sequence
RT and transcriptional analysis of the expression of the erythromycin
RT resistance gene.";
RL Microb. Drug Resist. 5:1-7(1999).
RN [2] {ECO:0000313|EMBL:ABQ00061.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CM05 {ECO:0000313|EMBL:ABQ00061.1};
RX PubMed=17555436; DOI=10.1111/j.1365-2958.2007.05744.x;
RA Toh S.M., Xiong L., Arias C.A., Villegas M.V., Lolans K., Quinn J.,
RA Mankin A.S.;
RT "Acquisition of a natural resistance gene renders a clinical strain of
RT methicillin-resistant Staphylococcus aureus resistant to the synthetic
RT antibiotic linezolid.";
RL Mol. Microbiol. 64:1506-1514(2007).
RN [3] {ECO:0000313|EMBL:BAF82031.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1 {ECO:0000313|EMBL:BAF82031.1};
RA Yamamoto T.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:BAF82031.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1 {ECO:0000313|EMBL:BAF82031.1};
RX PubMed=18086843; DOI=10.1128/AAC.01001-07;
RA Takano T., Higuchi W., Otsuka T., Baranovich T., Enany S., Saito K.,
RA Isobe H., Dohmae S., Ozaki K., Takano M., Iwao Y., Shibuya M., Okubo T.,
RA Yabe S., Shi D., Reva T., Teng L.J., Yamamoto T.;
RT "Novel characteristics of community-acquired methicillin-resistant
RT Staphylococcus aureus strains belonging to multilocus sequence type 59 in
RT Taiwan.";
RL Antimicrob. Agents Chemother. 52:837-845(2008).
RN [5] {ECO:0000313|EMBL:ADA61298.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRS128 {ECO:0000313|EMBL:ADA61298.1};
RC PLASMID=pI258 {ECO:0000313|EMBL:ADA61298.1};
RA Gill J., Borman J., Shetty J., Hostetler J., Durkin S., Montgomery B.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:ADA61298.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRS128 {ECO:0000313|EMBL:ADA61298.1};
RC PLASMID=pI258 {ECO:0000313|EMBL:ADA61298.1};
RA Summers A.O., Shearer J., Wireman J.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AET37215.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CM05 {ECO:0000313|EMBL:AET37215.1};
RX PubMed=22024827; DOI=10.1128/AAC.05420-11;
RA Locke J.B., Rahawi S., Lamarre J., Mankin A.S., Shaw K.J.;
RT "Genetic Environment and Stability of cfr in Methicillin-Resistant
RT Staphylococcus aureus CM05.";
RL Antimicrob. Agents Chemother. 56:332-340(2012).
RN [8] {ECO:0000313|EMBL:BAM37214.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PM1 {ECO:0000313|EMBL:BAM37214.1};
RX PubMed=23071689; DOI=10.1371/journal.pone.0046987;
RA Hung W.-C., Takano T., Higuchi W., Iwao Y., Khokhlova O., Teng L.-J.,
RA Yamamoto T.;
RT "Comparative Genomics of Community-Acquired ST59 Methicillin-Resistant
RT Staphylococcus aureus in Taiwan: Novel Mobile Resistance Structures with
RT IS1216V.";
RL PLoS ONE 7:e46987-e46987(2012).
RN [9] {ECO:0000313|EMBL:AHJ80338.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=048-45547X {ECO:0000313|EMBL:AHJ80338.1};
RC PLASMID=p45547X {ECO:0000313|EMBL:AHJ80338.1};
RX PubMed=25261421;
RA Gales A.C., Deshpande L.M., de Souza A.G., Pignatari A.C., Mendes R.E.;
RT "MSSA ST398/t034 carrying a plasmid-mediated Cfr and Erm(B) in Brazil.";
RL J. Antimicrob. Chemother. 70:303-305(2015).
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 {ECO:0000256|ARBA:ARBA00003100}.
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 Evidence={ECO:0000256|ARBA:ARBA00001449};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF450709; ABQ00061.1; -; Genomic_DNA.
DR EMBL; GQ900378; ADA61298.1; -; Genomic_DNA.
DR EMBL; JN849634; AET37215.1; -; Genomic_DNA.
DR EMBL; JN849634; AET37218.1; -; Genomic_DNA.
DR EMBL; KJ192337; AHJ80338.1; -; Genomic_DNA.
DR EMBL; AB300568; BAF82031.1; -; Genomic_DNA.
DR EMBL; AB699882; BAM37214.1; -; Genomic_DNA.
DR EMBL; Y13600; CAA73921.1; -; Genomic_DNA.
DR RefSeq; WP_001038790.1; NZ_WTUM01000074.1.
DR RefSeq; YP_006937611.1; NC_013319.1.
DR AlphaFoldDB; Q799N2; -.
DR SMR; Q799N2; -.
DR GeneID; 81710842; -.
DR PATRIC; fig|1280.3524.peg.2645; -.
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-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; DIMETHYLADENOSINE TRANSFERASE; 1.
DR PANTHER; PTHR11727:SF7; DIMETHYLADENOSINE TRANSFERASE-RELATED; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Plasmid {ECO:0000313|EMBL:ADA61298.1};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}.
FT DOMAIN 17..179
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 12
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 245 AA; 28796 MW; FFFEBA441C8511D0 CRC64;
MNKNIKYSQN FLTSEKVLNQ IIKQLNLKET DTVYEIGTGK GHLTTKLAKI SKQVTSIELD
SHLFNLSSEK LKLNIRVTLI HQDILQFQFP NKQRYKIVGN IPYHLSTQII KKVVFESHAS
DIYLIVEEGF YKRTLDIHRT LGLLLHTQVS IQQLLKLPAE CFHPKPKVNS VLIKLTRHTT
DVPDKYWKLY TYFVSKWVNR EYRQLFTKNQ FHQAMKHAKV NNLSTVTYEQ VLSIFNSYLL
FNGRK
//
