AVRB_STRVR
ID AVRB_STRVR Reviewed; 287 AA.
AC Q9F5K6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=23S rRNA (uridine(2479)-2'-O)-methyltransferase;
DE EC=2.1.1.208;
DE AltName: Full=Avilamycin resistance protein B;
GN Name=aviRb;
OS Streptomyces viridochromogenes.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1938;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Tu57;
RX PubMed=11181344; DOI=10.1128/aac.45.3.690-695.2001;
RA Weitnauer G., Gaisser S., Trefzer A., Stockert S., Westrich L.,
RA Quiros L.M., Mendez C., Salas J.A., Bechthold A.;
RT "An ATP-binding cassette transporter and two rRNA methyltransferases are
RT involved in resistance to avilamycin in the producer organism Streptomyces
RT viridochromogenes Tu57.";
RL Antimicrob. Agents Chemother. 45:690-695(2001).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Tu57;
RX PubMed=12828631; DOI=10.1046/j.1365-2958.2003.03558.x;
RA Treede I., Jakobsen L., Kirpekar F., Vester B., Weitnauer G., Bechthold A.,
RA Douthwaite S.;
RT "The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA
RT at the guanosine 2535 base and the uridine 2479 ribose.";
RL Mol. Microbiol. 49:309-318(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, SUBUNIT, AND MUTAGENESIS OF THR-135; ASN-139;
RP ARG-145; GLU-234 AND ASN-262.
RC STRAIN=Tu57;
RX PubMed=15581897; DOI=10.1016/j.jmb.2004.10.051;
RA Mosbacher T.G., Bechthold A., Schulz G.E.;
RT "Structure and function of the antibiotic resistance-mediating
RT methyltransferase AviRb from Streptomyces viridochromogenes.";
RL J. Mol. Biol. 345:535-545(2005).
CC -!- FUNCTION: Specifically methylates the 2'-O-ribose position of uridine-
CC 2479 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin,
CC an orthosomycin antibiotic. {ECO:0000269|PubMed:11181344,
CC ECO:0000269|PubMed:12828631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(2479) in 23S rRNA = 2'-O-
CC methyluridine(2479) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43092, Rhea:RHEA-COMP:10335, Rhea:RHEA-COMP:10336,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.208;
CC Evidence={ECO:0000269|PubMed:12828631};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15581897}.
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; AF333038; AAG32066.1; -; Genomic_DNA.
DR PDB; 1X7O; X-ray; 2.37 A; A/B=1-287.
DR PDB; 1X7P; X-ray; 2.55 A; A/B=1-287.
DR PDBsum; 1X7O; -.
DR PDBsum; 1X7P; -.
DR AlphaFoldDB; Q9F5K6; -.
DR SMR; Q9F5K6; -.
DR KEGG; ag:AAG32066; -.
DR BioCyc; MetaCyc:MON-16328; -.
DR BRENDA; 2.1.1.208; 6116.
DR EvolutionaryTrace; Q9F5K6; -.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR GO; GO:0031167; P:rRNA methylation; IDA:UniProtKB.
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; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF55315; SSF55315; 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..287
FT /note="23S rRNA (uridine(2479)-2'-O)-methyltransferase"
FT /id="PRO_0000418461"
FT BINDING 210..211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:15581897"
FT BINDING 252..254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT MUTAGEN 135
FT /note="T->V: Slightly increases catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT MUTAGEN 139
FT /note="N->A: Almost abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT MUTAGEN 145
FT /note="R->A: Almost abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT MUTAGEN 234
FT /note="E->A: Strongly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT MUTAGEN 234
FT /note="E->Q: Slightly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT MUTAGEN 262
FT /note="N->A: Almost abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT MUTAGEN 262
FT /note="N->Q: Slightly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:15581897"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1X7P"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:1X7O"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1X7O"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:1X7O"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1X7O"
FT HELIX 263..278
FT /evidence="ECO:0007829|PDB:1X7O"
SQ SEQUENCE 287 AA; 31215 MW; 27E742DB22E19DBE CRC64;
MARSRGERTP AARRITSRNA RFQQWQALLG NRNKRTRAGE FLVMGVRPIS LAVEHGWPVR
TLLYDGQREL SKWARELLRT VRTEQIAMAP DLLMELGEKN EAPPEVVAVV EMPADDLDRI
PVREDFLGVL FDRPTSPGNI GSIIRSADAL GAHGLIVAGH AADVYDPKSV RSSTGSLFSL
PAVRVPSPGE VMDWVEARRA AGTPIVLVGT DEHGDCDVFD FDFTQPTLLL IGNETAGLSN
AWRTLCDYTV SIPMAGSASS LNAANAATAI LYEAVRQRIS GRTATTP
