AVRA_STRVR
ID AVRA_STRVR Reviewed; 250 AA.
AC Q9F5K5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=23S rRNA (guanine(2535)-N(1))-methyltransferase;
DE EC=2.1.1.209;
DE AltName: Full=Avilamycin resistance protein A;
GN Name=aviRa;
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 (1.50 ANGSTROMS).
RC STRAIN=Tu57;
RX PubMed=12742024; DOI=10.1016/s0022-2836(03)00407-8;
RA Mosbacher T.G., Bechthold A., Schulz G.E.;
RT "Crystal structure of the avilamycin resistance-conferring
RT methyltransferase AviRa from Streptomyces viridochromogenes.";
RL J. Mol. Biol. 329:147-157(2003).
CC -!- FUNCTION: Specifically methylates the guanine-2535 in 23S ribosomal
CC RNA. Confers resistance to antibiotic avilamycin, an orthosomycin
CC antibiotic. {ECO:0000269|PubMed:11181344, ECO:0000269|PubMed:12828631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(2535) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(1)-methylguanosine(2535) in 23S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43096, Rhea:RHEA-COMP:10337, Rhea:RHEA-COMP:10338,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.209;
CC Evidence={ECO:0000269|PubMed:12828631};
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DR EMBL; AF333038; AAG32067.2; -; Genomic_DNA.
DR PDB; 1O9G; X-ray; 1.50 A; A=1-250.
DR PDB; 1O9H; X-ray; 2.40 A; A=1-250.
DR PDBsum; 1O9G; -.
DR PDBsum; 1O9H; -.
DR AlphaFoldDB; Q9F5K5; -.
DR SMR; Q9F5K5; -.
DR KEGG; ag:AAG32067; -.
DR BioCyc; MetaCyc:MON-16329; -.
DR BRENDA; 2.1.1.209; 6116.
DR EvolutionaryTrace; Q9F5K5; -.
DR GO; GO:0008989; F:rRNA (guanine-N1-)-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; 3.40.50.150; -; 1.
DR InterPro; IPR024268; AviRa.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF11599; AviRa; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..250
FT /note="23S rRNA (guanine(2535)-N(1))-methyltransferase"
FT /id="PRO_0000418460"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1O9G"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1O9H"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:1O9G"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:1O9G"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:1O9G"
SQ SEQUENCE 250 AA; 26636 MW; E2F972770DA5A853 CRC64;
MSAYRHAVER IDSSDLACGV VLHSAPGYPA FPVRLATEIF QRALARLPGD GPVTLWDPCC
GSGYLLTVLG LLHRRSLRQV IASDVDPAPL ELAAKNLALL SPAGLTAREL ERREQSERFG
KPSYLEAAQA ARRLRERLTA EGGALPCAIR TADVFDPRAL SAVLAGSAPD VVLTDLPYGE
RTHWEGQVPA QPVAGLLRSL ASALPAHAVI AVTDRSRKIP VAPVKALERL KIGTRSAVLV
RAADVLEAGP
