TSNR_STRAJ
ID TSNR_STRAJ Reviewed; 269 AA.
AC P18644;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=23S rRNA (adenosine(1067)-2'-O)-methyltransferase {ECO:0000305};
DE EC=2.1.1.230 {ECO:0000269|PubMed:6806287};
DE AltName: Full=23S rRNA [AM1067] 2'-O-methyltransferase;
DE Short=23S rRNA methylase;
DE AltName: Full=Thiostrepton-resistance methylase {ECO:0000303|Ref.3};
DE AltName: Full=rRNA (adenosine-2'-O)-methyltransferase;
GN Name=tsnR; Synonyms=tsr {ECO:0000303|PubMed:2987648};
OS Streptomyces azureus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=146537;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14921 / DSM 40106 / CBS 467.68 / ETH 28555 / JCM 4564 / NBRC
RC 12744 / NRRL B-2655 / VKM Ac-719;
RX PubMed=2987648; DOI=10.1007/bf00327505;
RA Bibb M.J., Bibb M.J., Ward J.M., Cohen S.N.;
RT "Nucleotide sequences encoding and promoting expression of three antibiotic
RT resistance genes indigenous to Streptomyces.";
RL Mol. Gen. Genet. 199:26-36(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC STRAIN=ATCC 14921 / DSM 40106 / CBS 467.68 / ETH 28555 / JCM 4564 / NBRC
RC 12744 / NRRL B-2655 / VKM Ac-719;
RX PubMed=2381416; DOI=10.1007/bf00259397;
RA Janssen G.R., Bibb M.J.;
RT "Tandem promoters, tsrp1 and tsrp2, direct transcription of the
RT thiostrepton resistance gene (tsr) of Streptomyces azureus: transcriptional
RT initiation from tsrp2 occurs after deletion of the -35 region.";
RL Mol. Gen. Genet. 221:339-346(1990).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1099/00221287-124-2-291;
RA Thompson J., Cundliffe E.;
RT "Purification and properties of an RNA methylase produced by Streptomyces
RT azureus and involved in resistance to thiostrepton.";
RL J. Gen. Microbiol. 124:291-297(1981).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6806287; DOI=10.1016/s0021-9258(18)34268-6;
RA Thompson J., Schmidt F., Cundliffe E.;
RT "Site of action of a ribosomal RNA methylase conferring resistance to
RT thiostrepton.";
RL J. Biol. Chem. 257:7915-7917(1982).
RN [5] {ECO:0007744|PDB:3GYQ}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, SUBUNIT, AND MUTAGENESIS OF PHE-88.
RX PubMed=19369248; DOI=10.1074/jbc.m901618200;
RA Dunstan M.S., Hang P.C., Zelinskaya N.V., Honek J.F., Conn G.L.;
RT "Structure of the thiostrepton resistance methyltransferase.S-adenosyl-L-
RT methionine complex and its interaction with ribosomal RNA.";
RL J. Biol. Chem. 284:17013-17020(2009).
CC -!- FUNCTION: Specifically methylates the adenosine-1067 in 23S ribosomal
CC RNA. Confers resistance to antibiotic thiostrepton.
CC {ECO:0000269|PubMed:6806287, ECO:0000269|Ref.3}.
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:0000269|PubMed:6806287};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.15 mM for S-adenosyl-L-methionine {ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 7.5-7.6. {ECO:0000269|Ref.3};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19369248}.
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; X02392; CAA26234.1; -; Genomic_DNA.
DR EMBL; X54219; CAA38132.1; -; Genomic_DNA.
DR PIR; S28369; S28369.
DR RefSeq; WP_059415847.1; NZ_DF968219.1.
DR PDB; 3GYQ; X-ray; 2.45 A; A/B=1-269.
DR PDBsum; 3GYQ; -.
DR AlphaFoldDB; P18644; -.
DR SMR; P18644; -.
DR BioCyc; MetaCyc:MON-16697; -.
DR BRENDA; 2.1.1.230; 5982.
DR EvolutionaryTrace; P18644; -.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..269
FT /note="23S rRNA (adenosine(1067)-2'-O)-methyltransferase"
FT /id="PRO_0000065669"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT BINDING 218..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT BINDING 238
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT BINDING 246..247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3GYQ"
FT MUTAGEN 88
FT /note="F->A: Defective in RNA binding."
FT /evidence="ECO:0000269|PubMed:19369248"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 49..59
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3GYQ"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:3GYQ"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:3GYQ"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:3GYQ"
SQ SEQUENCE 269 AA; 28901 MW; 66B1976014A05636 CRC64;
MTELDTIANP SDPAVQRIID VTKPSRSNIK TTLIEDVEPL MHSIAAGVEF IEVYGSDSSP
FPSELLDLCG RQNIPVRLID SSIVNQLFKG ERKAKTFGIA RVPRPARFGD IASRRGDVVV
LDGVKIVGNI GAIVRTSLAL GASGIILVDS DITSIADRRL QRASRGYVFS LPVVLSGREE
AIAFIRDSGM QLMTLKADGD ISVKELGDNP DRLALLFGSE KGGPSDLFEE ASSASVSIPM
MSQTESLNVS VSLGIALHER IDRNLAANR
