RMTB_SERMA
ID RMTB_SERMA Reviewed; 251 AA.
AC Q76G15;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=16S rRNA (guanine(1405)-N(7))-methyltransferase;
DE EC=2.1.1.179;
DE AltName: Full=16S rRNA m7G1405 methyltransferase;
GN Name=rmtB;
OS Serratia marcescens.
OG Plasmid pKRC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A METHYLTRANSFERASE AND
RP IN ANTIBIOTIC RESISTANCE.
RC STRAIN=S-95; PLASMID=pKRC;
RX PubMed=14742200; DOI=10.1128/aac.48.2.491-496.2004;
RA Doi Y., Yokoyama K., Yamane K., Wachino J., Shibata N., Yagi T.,
RA Shibayama K., Kato H., Arakawa Y.;
RT "Plasmid-mediated 16S rRNA methylase in Serratia marcescens conferring
RT high-level resistance to aminoglycosides.";
RL Antimicrob. Agents Chemother. 48:491-496(2004).
CC -!- FUNCTION: Specifically methylates the N(7) position of guanine 1405 in
CC 16S rRNA (By similarity). Confers resistance to various
CC aminoglycosides, including kanamycin, tobramycin, amikacin, arbekacin,
CC gentamicin, sisomicin and isepamicin. {ECO:0000250,
CC ECO:0000269|PubMed:14742200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(1405) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42772, Rhea:RHEA-COMP:10225, Rhea:RHEA-COMP:10226,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.179;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Aminoglycoside resistance family. {ECO:0000305}.
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DR EMBL; AB103506; BAC81971.1; -; Genomic_DNA.
DR RefSeq; WP_012372818.1; NG_048058.1.
DR AlphaFoldDB; Q76G15; -.
DR SMR; Q76G15; -.
DR KEGG; ag:BAC81971; -.
DR BRENDA; 2.1.1.179; 5690.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025981; rRNA_MeTrfase.
DR InterPro; IPR010769; rRNA_MeTrfase_GmN_bac.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07091; FmrO; 1.
DR PIRSF; PIRSF015852; RRNA_mtase_Grm; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Methyltransferase; Plasmid; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..251
FT /note="16S rRNA (guanine(1405)-N(7))-methyltransferase"
FT /id="PRO_0000416818"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 81..83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 157..158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 27408 MW; 8D5464F4B4D60B50 CRC64;
MNINDALTSI LASKKYRALC PDTVRRILTE EWGRHKSPKQ TVEAARTRLH GICGAYVTPE
SLKAAAAALS AGDVKKALSL HASTKERLAE LDTLYDFIFS AETPRRVLDI ACGLNPLALY
ERGIASVWGC DIHQGLGDVI TPFAREKDWD FTFALQDVLC APPAEAGDLA LIFKLLPLLE
REQAGSAMAL LQSLNTPRMA VSFPTRSLGG RGKGMEANYA AWFEGGLPAE FEIEDKKTIG
TELIYLIKKN G
