NSHR_STRAS
ID NSHR_STRAS Reviewed; 274 AA.
AC P52391;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=23S rRNA (adenosine(1067)-2'-O)-methyltransferase {ECO:0000305};
DE EC=2.1.1.230 {ECO:0000269|PubMed:20550164};
DE AltName: Full=Nosiheptide-resistance methyltransferase {ECO:0000303|PubMed:20445264, ECO:0000303|PubMed:20550164};
DE Short=NHR {ECO:0000303|PubMed:20550164};
DE Short=NSR {ECO:0000303|PubMed:20445264};
GN Name=nshR {ECO:0000312|EMBL:AAB17875.1};
OS Streptomyces actuosus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25421 / DSM 40337 / JCM 4445 / NBRC 13009 / NRRL 2954 / VKM
RC Ac-1274;
RX PubMed=2401410; DOI=10.1016/0378-1119(90)90156-l;
RA Li Y., Dosch D.C., Strohl W.R., Floss H.G.;
RT "Nucleotide sequence and transcriptional analysis of the nosiheptide-
RT resistance gene from Streptomyces actuosus.";
RL Gene 91:9-17(1990).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=20445264; DOI=10.1107/s1744309110011395;
RA Yang H., Wang P., Dong Z., Li X., Gong R., Yang Y., Li Z., Xu Y., Xu Y.;
RT "Crystallization and preliminary crystallographic analysis of nosiheptide-
RT resistance methyltransferase from Streptomyces actuosus in complex with
RT SAM.";
RL Acta Crystallogr. F 66:579-582(2010).
RN [3] {ECO:0007744|PDB:3NK6, ECO:0007744|PDB:3NK7}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF GLU-35; ASP-36; PHE-88; GLU-91; ARG-92; ARG-135; ARG-165;
RP SER-219 AND GLU-220.
RX PubMed=20550164; DOI=10.1021/bi1005915;
RA Yang H., Wang Z., Shen Y., Wang P., Jia X., Zhao L., Zhou P., Gong R.,
RA Li Z., Yang Y., Chen D., Murchie A.I., Xu Y.;
RT "Crystal structure of the nosiheptide-resistance methyltransferase of
RT Streptomyces actuosus.";
RL Biochemistry 49:6440-6450(2010).
CC -!- FUNCTION: Specifically methylates the adenosine-1067 in 23S ribosomal
CC RNA. Confers resistance to antibiotic nosiheptide.
CC {ECO:0000269|PubMed:20550164}.
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:20550164};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20550164}.
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; U75434; AAB17875.1; -; Genomic_DNA.
DR PIR; JQ0686; JQ0686.
DR RefSeq; WP_063854493.1; NZ_CP029788.1.
DR PDB; 3NK6; X-ray; 2.00 A; A/B=1-274.
DR PDB; 3NK7; X-ray; 2.10 A; A/B=1-274.
DR PDBsum; 3NK6; -.
DR PDBsum; 3NK7; -.
DR AlphaFoldDB; P52391; -.
DR SMR; P52391; -.
DR KEGG; ag:AAB17875; -.
DR BRENDA; 2.1.1.230; 12393.
DR EvolutionaryTrace; P52391; -.
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..274
FT /note="23S rRNA (adenosine(1067)-2'-O)-methyltransferase"
FT /id="PRO_0000096811"
FT BINDING 165
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3NK7"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3NK7"
FT BINDING 218..220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3NK7"
FT BINDING 238..240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3NK7"
FT BINDING 247..252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:3NK7"
FT MUTAGEN 35
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 36
FT /note="D->A: Significantly decreases activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 88
FT /note="F->A: Significantly decreases activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 91
FT /note="E->A: Significantly decreases activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 92
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 135
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 165
FT /note="R->A: Significantly decreases activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 219
FT /note="S->A: Slightly decreases activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT MUTAGEN 220
FT /note="E->Q: Significantly decreases activity."
FT /evidence="ECO:0000269|PubMed:20550164"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3NK6"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3NK7"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:3NK6"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3NK6"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:3NK6"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:3NK6"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:3NK6"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:3NK6"
SQ SEQUENCE 274 AA; 29184 MW; 9FA2C12B2E8BF24D CRC64;
MTEPAIITNA SDPAVQRIID VTKHSRASIK TTLIEDTEPL MECIRAGVQF IEVYGSSGTP
LDPALLDLCR QREIPVRLID VSIVNQLFKA ERKAKVFGIA RVPRPARLAD IAERGGDVVV
LDGVKIVGNI GAIVRTSLAL GAAGIVLVDS DLATIADRRL LRASRGYVFS LPVVLADREE
AVSFLRDNDI ALMVLDTDGD LGVKDLGDRA DRMALVFGSE KGGPSGLFQE ASAGTVSIPM
LSSTESLNVS VSVGIALHER SARNFAVRRA AAQA
