ID   TSNR_STRLU              Reviewed;         270 AA.
AC   P52393;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=23S rRNA (adenosine(1067)-2'-O)-methyltransferase;
DE            EC=2.1.1.230 {ECO:0000250|UniProtKB:P18644};
DE   AltName: Full=23S rRNA [AM1067] 2'-O-methyltransferase;
DE            Short=23S rRNA methylase;
DE   AltName: Full=Thiostrepton-resistance methylase;
DE   AltName: Full=rRNA (adenosine-2'-O)-methyltransferase;
GN   Name=tsnR {ECO:0000303|PubMed:7590303};
OS   Streptomyces laurentii.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=39478;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7590303; DOI=10.1016/0378-1119(95)00442-9;
RA   Smith T.M., Jiang Y.F., Shipley P., Floss H.G.;
RT   "The thiostrepton-resistance-encoding gene in Streptomyces laurentii is
RT   located within a cluster of ribosomal protein operons.";
RL   Gene 164:137-142(1995).
CC   -!- FUNCTION: Specifically methylates the adenosine-1067 in 23S ribosomal
CC       RNA. Confers resistance to antibiotic thiostrepton.
CC       {ECO:0000250|UniProtKB:P18644}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1067) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC         methyladenosine(1067) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43212, Rhea:RHEA-COMP:10409, Rhea:RHEA-COMP:10410,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74477; EC=2.1.1.230;
CC         Evidence={ECO:0000250|UniProtKB:P18644};
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TsnR/AvirB family. {ECO:0000305}.
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DR   EMBL; L39157; AAA99931.1; -; Genomic_DNA.
DR   PIR; JC4350; JC4350.
DR   RefSeq; WP_063856492.1; NG_048322.1.
DR   AlphaFoldDB; P52393; -.
DR   SMR; P52393; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0030743; F:rRNA (adenosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR006795; Thiostrepton-R_Mease_TSNR_N.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF04705; TSNR_N; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..270
FT                   /note="23S rRNA (adenosine(1067)-2'-O)-methyltransferase"
FT                   /id="PRO_0000065670"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P18644"
FT   BINDING         165
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P18644"
FT   BINDING         218..220
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P18644"
FT   BINDING         238
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P18644"
FT   BINDING         246..247
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P18644"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P18644"
SQ   SEQUENCE   270 AA;  28723 MW;  298E871C3D8BCDCE CRC64;
     MANLDVIVDR SDPAVQRIVD VTKHSRSVVR TVLIEDIEPL TQSIRAGVEF TEVYGLDTVP
     FPGDLLAACE KRGIRVRLLS AAVANQVFKT EKKPKVFGIA KVPPAGRFAD LESLSGDVVL
     LDGVKIVGNI GAIVRTRSAL GAAGIVLVDS GLGTIADRRL IRASRGYVFS LPIVLATRDE
     ALAFFRDGGM RPVVFEADGK LSIGELDGID ERLVLVFGSE KTGPSGEFAG VATESVSIPM
     NPAAESLNVS VSAGIALHRR ARRNLSRPRG