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Information on EC 2.1.1.179 - 16S rRNA (guanine1405-N7)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.179
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.179 16S rRNA (guanine1405-N7)-methyltransferase
IUBMB Comments
The enzyme from the antibiotic-producing bacterium Micromonospora zionensis specifically methylates guanine1405 at N7 in 16S rRNA, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins .
The enzyme appears in viruses and cellular organisms
- 2.1.1.179
- aminoglycoside
- drug development
-
esbls
- micromonospora
-
extended-spectrum
- carbapenemases
-
aminoglycoside-resistant
-
4,6-disubstituted
-
carbapenem-resistant
-
plazomicin
-
methyltranferase
-
aac6\'-ib
-
worrisome
-
carbapenemase-producing
- blakpc-2
- fosfomycin
-
blatem-1b
-
aminoglycoside-producing
-
deoxystreptamine
- tigecycline
- mtases
Reaction Schemes
show+
=
+
+
guanine1405 in 16S rRNA
=
+
N7-methylguanine1405 in 16S rRNA
Synonyms
16s-rmtase, rmtd2, methyltransferase rmtc, sisomicin-gentamicin resistance methylase, sgm mtase, sgm methyltransferase, methyltransferase sgm, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
16S rRNA (guanine(1405)-N(7))-methyltransferase
16S rRNA (m7G1405) methyltransferase
16S rRNA methyltransferase
16S rRNA N7 G1405 methyltransferase
16S-RMTase
Arm methyltransferase
ArmA
G1405 methyltransferase ArmA
Krm
methyltransferase RmtC
N7-G1405 16S-RMTase
RmtB
RmtC
RmtD
RmtD2
RmtF
RmtF
RmtF protein has 25 to 46% identity with members of the N7 G1405 family of aminoglycoside resistance 16S rRNA methyltransferases
RmtF
RmtF protein has 25 to 46% identity with members of the N7 G1405 family of aminoglycoside resistance 16S rRNA methyltransferases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1405 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
S-adenosyl-L-methionine + guanine1405 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
the mechanism of methylation of G1405 by Sgm is proposed and compared with other m7G methyltransferases
S-adenosyl-L-methionine + guanine1405 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
-
-
-
S-adenosyl-L-methionine + guanine1405 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
analysis of sequencefunction relationships of Sgm MTase by limited proteolysis and site-directed and random mutagenesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine1405-N7)-methyltransferase
The enzyme from the antibiotic-producing bacterium Micromonospora zionensis specifically methylates guanine1405 at N7 in 16S rRNA, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins [2].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
-
Substrates: post-transcriptional methylation of N7-G1405 in 16S rRNA of 30S ribosomal subunits
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates G1405 in 16S rRNA to m7G, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: methylation site is experimentally determined as G1405 by MALDI-ToF mass spectrometry
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates G1405 in 16S rRNA to m7G, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: methylation site is experimentally determined as G1405 by MALDI-ToF mass spectrometry
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates G1405 in 16S rRNA to m7G, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
-
Substrates: the enzyme gives resistance to kanamycin plus gentamicin by converting residue C-1405 to 7-methylguanosine
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: methylation site is experimentally determined as G1405 by MALDI-ToF mass spectrometry
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme encodes an enzyme that modifies 16S rRNA and thereby confers resistance to 4,6-disubstituted deoxystreptamine aminoglycosides
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme confers resistance to aminoglycosides like gentamicin and sisomicin by specifically methylating G1405 in bacterial 16S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates guanine1405 in 16S rRNA to 7-methylguanine, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: methylation site is experimentally determined as guanine1405 by MALDI-ToF mass spectrometry
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
plasmid pAT780
-
Substrates: methylation at guanine1405 mediates cellular resistance by blocking aminoglycoside binding by ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
plasmid pAT780
-
Substrates: the ArmA methylation reaction is specific for the 30S ribosomal subunit. Neither 16S rRNA alone nor the 70S ribosome is a substrate for this reaction under experimental conditions, implicating ribosomal proteins in substrate recognition
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
plasmid pIP1206
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: RmtC can confer high-level resistance to gentamicin and kanamycin in Bacillus subtilis and Staphylococcus aureus
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: RmtC has an MTase activity specific for the bacterial 30S ribosomal subunit consisting of 16S rRNA and several ribosomal proteins, but not for the naked 16S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: RmtC can confer high-level resistance to gentamicin and kanamycin in Bacillus subtilis and Staphylococcus aureus
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: RmtC has an MTase activity specific for the bacterial 30S ribosomal subunit consisting of 16S rRNA and several ribosomal proteins, but not for the naked 16S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: RmtC in the presence of aminoglycosides impedes methylation at the N5 position of nucleotide C1407 when the N7 position of G1405 is methylated, MALDI mass spectrometry product analysis, mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). RmtB also cannot methylate G1405 in ribosomes containing the G1491U mutation. Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). RmtB also cannot methylate G1405 in ribosomes containing the G1491U mutation. Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). RmtB also cannot methylate G1405 in ribosomes containing the G1491U mutation. Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). RmtB also cannot methylate G1405 in ribosomes containing the G1491U mutation. Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes. Structure-function analysis, functional differences between Sgm and RmtC methyltransferases , overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes. Structure-function analysis, functional differences between Sgm and RmtC methyltransferases , overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes. Structure-function analysis, functional differences between Sgm and RmtC methyltransferases , overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes. Structure-function analysis, functional differences between Sgm and RmtC methyltransferases , overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains re able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains re able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains re able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains re able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview
Products: -
Products: -
-
additional information
?
-
-
Substrates: RmtC in the presence of aminoglycosides impedes methylation at the N5 position of nucleotide C1407 when the N7 position of G1405 is methylated, MALDI mass spectrometry product analysis, mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Sgm methyltransferase is unable to methylate G1405 in ribosomes containing A1408G, G1491U, or U1495A mutations. Structure-function analysis, overview
Products: -
Products: -
-
additional information
?
-
Substrates: substrates are wild-type and mutant rRNA and ribosomes from Escherichia coli strains, substrate specificity, overview. Arm methyltransferases isolated from clinical bacterial strains are able to methylate their target nucleotide, G1405, on most mutant ribosomes, but methyltransferases RmtB, ArmA, and RmtC are unable to methylate G1405 on ribosomes with the U1406A mutation (RmtB, ArmA) or the A1408G mutation (RmtC). Structure-function analysis, functional differences between Sgm and RmtC methyltransferases, overview
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
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Substrates: post-transcriptional methylation of N7-G1405 in 16S rRNA of 30S ribosomal subunits
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates G1405 in 16S rRNA to m7G, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates G1405 in 16S rRNA to m7G, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates G1405 in 16S rRNA to m7G, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
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Substrates: the enzyme gives resistance to kanamycin plus gentamicin by converting residue C-1405 to 7-methylguanosine
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme encodes an enzyme that modifies 16S rRNA and thereby confers resistance to 4,6-disubstituted deoxystreptamine aminoglycosides
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme confers resistance to aminoglycosides like gentamicin and sisomicin by specifically methylating G1405 in bacterial 16S rRNA
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates guanine1405 in 16S rRNA to 7-methylguanine, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
plasmid pAT780
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Substrates: methylation at guanine1405 mediates cellular resistance by blocking aminoglycoside binding by ribosomes
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
plasmid pIP1206
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: RmtC can confer high-level resistance to gentamicin and kanamycin in Bacillus subtilis and Staphylococcus aureus
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
Substrates: RmtC can confer high-level resistance to gentamicin and kanamycin in Bacillus subtilis and Staphylococcus aureus
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
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Substrates: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
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Substrates: -
Products: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
Substrates: -
Products: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
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Substrates: -
Products: -
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S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
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Substrates: -
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additional information
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Substrates: RmtC in the presence of aminoglycosides impedes methylation at the N5 position of nucleotide C1407 when the N7 position of G1405 is methylated, MALDI mass spectrometry product analysis, mechanism, overview
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additional information
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-
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Substrates: RmtC in the presence of aminoglycosides impedes methylation at the N5 position of nucleotide C1407 when the N7 position of G1405 is methylated, MALDI mass spectrometry product analysis, mechanism, overview
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Aminoglycoside Resistance: The Emergence of Acquired 16S Ribosomal RNA Methyltransferases.
Pneumonia
Clonal Spread of 16S rRNA Methyltransferase-Producing Klebsiella pneumoniae ST37 with High Prevalence of ESBLs from Companion Animals in China.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene rmtF encoded on a non-self-transferable plasmid pIP849
UniProt
brenda
gene rmtF encoded on a non-self-transferable plasmid pIP849
UniProt
brenda
-
UniProt
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
RmtF is a member of the aminoglycoside resistance 16S rRNA N7 G1405 methyltransferase family
evolution
RmtA shows aquired N7-G1405 16S-RMTase activity
evolution
RmtD shows aquired N7-G1405 16S-RMTase activity
evolution
FmrO shows intrinsic N7-G1405 16S-RMTase activity
evolution
-
RmtF is a member of the aminoglycoside resistance 16S rRNA N7 G1405 methyltransferase family
-
metabolism
the ribosomal A site binding patterns of Arm methyltransferases from clinical pathogens (ArmA, RmtB, RmtC, and RmtD) with those of the Sgm methyltransferase from a natural aminoglycoside producer. Sgm methyltransferase exhibited a distinct methylation pattern compared to Arm methyltransferases from clinical strains. Structural comparisons of Sgm, RmtB, and RmtC reveal different spatial orientations of key amino acids involved in ribosomal binding, highlighting evolutionary differences
metabolism
the ribosomal A site binding patterns of Arm methyltransferases from clinical pathogens (ArmA, RmtB, RmtC, and RmtD) with those of the Sgm methyltransferase from a natural aminoglycoside producer. Sgm methyltransferase exhibited a distinct methylation pattern compared to Arm methyltransferases from clinical strains. Structural comparisons of Sgm, RmtB, and RmtC reveal different spatial orientations of key amino acids involved in ribosomal binding, highlighting evolutionary differences
metabolism
the ribosomal A site binding patterns of Arm methyltransferases from clinical pathogens (ArmA, RmtB, RmtC, and RmtD) with those of the Sgm methyltransferase from a natural aminoglycoside producer. Sgm methyltransferase exhibited a distinct methylation pattern compared to Arm methyltransferases from clinical strains. Structural comparisons of Sgm, RmtB, and RmtC reveal different spatial orientations of key amino acids involved in ribosomal binding, highlighting evolutionary differences
physiological function
encodes an enzyme that modifies 16S rRNA and thereby confers resistance to 4,6-disubstituted deoxystreptamine aminoglycosides. The expression of the sgm gene is regulated by the translational autorepression
physiological function
the enzyme produced by the antibiotic-producing bacterium Micromonospora zionensis methylates guanine1405 in 16S rRNA to 7-methylguanine, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins
physiological function
-
the enzyme gives resistance to kanamycin plus gentamicin by converting guanine1405 to 7-methylguanine
physiological function
rmtC is responsible for resistance of strain ARS68 and its transformant to various aminoglycoside antibiotics
physiological function
plasmid pAT780
-
G1405 methylation produces aminoglycoside resistance by diminishing the affinity of the ribosome for gentamicin
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis. These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis. These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis. These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis. These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis. These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
-
the enzyme confers high-level resistance to 4,6-disubstituted aminoglycosides through methylation of the G1405 residue in the 16S rRNA. RmtC impedes methylation by the housekeeping methyltransferase RsmF, EC 2.1.1.178, at position C1407
physiological function
methylation of C1405, involved in the binding of aminoglycosides to 16S rRNA, can lead to loss of affinity and to resistance of the host. Resistance conferred by RmtF cannot be transferred to Escherichia coli via transfer of plasmid pIP849
physiological function
the enzyme adds the methyl group of S-adenosyl-L-methionine to the specific nucleotides at the A-site of 16S rRNA, which interferes with aminoglycoside binding to the target. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
the enzyme adds the methyl group of S-adenosyl-L-methionine to the specific nucleotides at the A-site of 16S rRNA, which interferes with aminoglycoside binding to the target. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
the enzyme adds the methyl group of S-adenosyl-L-methionine to the specific nucleotides at the A-site of 16S rRNA, which interferes with aminoglycoside binding to the target. Pseudomonas aeruginosa clinical isolates show high-level resistance to clinically useful aminoglycosides through the production of acquired 16S-RMTase. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
the enzyme adds the methyl group of S-adenosyl-L-methionine to the specific nucleotides at the A-site of 16S rRNA, which interferes with aminoglycoside binding to the target. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis, These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
most aminoglycosides bind to the decoding aminoacyl-tRNA recognition site (A-site) of the 16S rRNA that composes bacterial 30S ribosome, and subsequently interfere with bacterial growth through blocking of protein synthesis. These aminoglycoside-producing actinomycetes are inherently resistant to aminoglycosides, because they harbor intrinsic 16S rRNA methyltransferase genes, that can confer aminoglycoside resistance to bacteria by modifying specific nucleotide residues in the aminoglycoside binding site of 16S rRNA. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
physiological function
-
the enzyme confers high-level resistance to aminoglycosides
physiological function
acquired ribosomal RNA (rRNA) methylation has emerged as a significant mechanism of aminoglycoside resistance in pathogenic bacterial infections. Modification of a single nucleotide in the ribosome decoding center by the aminoglycoside-resistance 16S rRNA (m7G1405) methyltransferases effectively blocks the action of all 4,6-deoxystreptamine ring-containing aminoglycosides, including the latest generation of drugs. Methylation of G1405 or A1408 within the h44 aminoglycoside-binding site to produce m7G1405 or m1A1408, respectively, blocks drug binding and thus the resulting effect on translation
physiological function
-
the enzyme confers high-level resistance to 4,6-disubstituted aminoglycosides through methylation of the G1405 residue in the 16S rRNA. RmtC impedes methylation by the housekeeping methyltransferase RsmF, EC 2.1.1.178, at position C1407
-
physiological function
-
rmtC is responsible for resistance of strain ARS68 and its transformant to various aminoglycoside antibiotics
-
physiological function
-
the enzyme adds the methyl group of S-adenosyl-L-methionine to the specific nucleotides at the A-site of 16S rRNA, which interferes with aminoglycoside binding to the target. Aminoglycoside resistance profile provided by N7-G1405 16S-RMTases, overview
-
physiological function
-
methylation of C1405, involved in the binding of aminoglycosides to 16S rRNA, can lead to loss of affinity and to resistance of the host. Resistance conferred by RmtF cannot be transferred to Escherichia coli via transfer of plasmid pIP849
-
physiological function
-
the enzyme confers high-level resistance to aminoglycosides
-
additional information
Smr1 shows intrinsic N7-G1405 16S-RMTase activity
additional information
GrmA shows intrinsic N7-G1405 16S-RMTase activity
additional information
Sgm shows intrinsic N7-G1405 16S-RMTase activity
additional information
NbrB shows intrinsic N7-G1405 16S-RMTase activity
additional information
Kmr shows intrinsic N7-G1405 16S-RMTase activity
additional information
-
acquisition of rmtC does not entail a fitness cost for the bacterium
additional information
GrmB shows intrinsic N7-G1405 16S-RMTase activity
additional information
comparison of the 3D structures of Escherichia coli and a member of the aminoglycoside-producing genera Micromonospora sp. 16S rRNA by aligning the 16S rRNA from the known crystal structure of the small ribosomal subunit of Escherichia coli with a model of Micromonospora sp. 16S rRNA
additional information
molecular basis of 30S subunit recognition and G1405 modification, docking and structure analysis of the m7G1405 methyltransferase RmtC bound to the mature Escherichia coli 30S ribosomal subunit, detailed overview. The RmtC N-terminal domain is critical for recognition and docking of the enzyme on a conserved 16S rRNA tertiary surface adjacent to G1405 in 16S rRNA helix 44 (h44). To access the G1405 N7 position for modification, a collection of residues across one surface of RmtC, including a loop that undergoes a disorder-to-order transition upon 30S subunit binding, induces significant distortion of h44. This distortion flips G1405 into the enzyme active site where it is positioned for modification by two almost universally conserved RmtC residues. The two highly conserved N1 domain residues, Lys20 and Arg50, are previously shown to be essential for 30S subunit binding and m7G1405 modification
additional information
-
acquisition of rmtC does not entail a fitness cost for the bacterium
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Show AA Sequence and Transmembrane Helices (221 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29500
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified Sgm is complexed with 5 mM of the cofactors S-adenosylmethionine/S-adenosylhomocysteine. Crystallization trials are carried out at room temperature by hanging-drop vapor-diffusion method, structure of Sgm in complex with cofactors S-adenosylmethionine and S-adenosylhomocysteine is determined at 2.0 A and 2.1 A resolution, respectively
in complex with S-adenosylhomocysteine. An N-terminal domain surface within RmtC, comprising basic residues from both the N1 and N2 subdomains, directly contributes to 30S-binding affinity. Additional residues lining a contiguous adjacent surface on the C-terminal domain are critical for 16S rRNA modification but do not directly contribute to the binding affinity
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H81A
-
tobramycin MIC is identical with that of wild-type RmtB. No change in methylation activity compared to wild-type enzyme
K14A
-
tobramycin MIC is identical with that of wild-type RmtB. 36% of the methylation activity compared to wild-type enzyme
K174A
-
tobramycin MIC is drastically reduced compared to wild-type enzyme. 0.7% of the methylation activity compared to wild-type enzyme
K236E
site-directed mutagenesis, the K236E substitution reduces the MIC of both tested aminoglycosides
K43E
site-directed mutagenesis, the substitution has a more modest impact on RmtC activity, only measurably decreasing the MIC for gentamicin, which has a lower activity in the presence of the wild-type enzyme compared to kanamycin
K47E
site-directed mutagenesis, the K47E substitution dramatically reduces the MIC for both aminoglycosides, indicating that these interactions with h44 and h27 are also essential for docking on the 30S subunit
K67E
site-directed mutagenesis, K67E or K71E substitutions result in a moderate reduction in resistance conferred by RmtC, whereas a K67E/K71E double substitution completely restores susceptibility to both aminoglycosides
K67E/K71E
site-directed mutagenesis, K67E or K71E substitutions result in a moderate reduction in resistance conferred by RmtC, whereas a K67E/K71E double substitution completely restores susceptibility to both aminoglycosides
K71E
site-directed mutagenesis, K67E or K71E substitutions result in a moderate reduction in resistance conferred by RmtC, whereas a K67E/K71E double substitution completely restores susceptibility to both aminoglycosides
N248A
site-directed mutagenesis, the N248A substitution has only limited or no impact on the MIC for gentamycin and kanamycin and thus does not appear individually critical for RmtC activity
R211E
site-directed mutagenesis, the R211E substitution significantly reduces the conferred MIC for gentamycin and kanamycin, while not contributing measurably to RmtC-30S subunit-binding affinity
R241E
site-directed mutagenesis, the R241E substitution abolishes RmtC activity
R39E
site-directed mutagenesis, the R39E substitution dramatically reduces the MIC for both aminoglycosides, indicating that these interactions with h44 and h27 are also essential for docking on the 30S subunit
S239A
site-directed mutagenesis, the S239A substitution results in a small reduction in MIC for gentamicin only, consistent with its weaker conservation in only acquired enzymes, with glycine most predominant including for all drug-producer (intrinsic) homologues
S83A
-
tobramycin MIC is identical with that of wild-type RmtB. 18% of the methylation activity compared to wild-type enzyme
T207A
site-directed mutagenesis, the T207A substitution has only limited or no impact on the MIC for gentamycin and kanamycin and thus does not appear individually critical for RmtC activity
Y21F
site-directed mutagenesis, the Y21F substitution dramatically reduces the MICs for both kanamycin and gentamicin for enzyme RmtC
Y60A
site-directed mutagenesis, the Y60A substitution completely abolishes enzyme activity
D156A
D158A
mutant with drastically increased sensitivity to kanamycin
D182A
E205A
E267A
G135A
K199A
K54A
mutant with drastically increased sensitivity to kanamycin
R108A
mutant with drastically increased sensitivity to kanamycin
R187S
mutant with drastically increased sensitivity to kanamycin
R236A
R433A
mutant with drastically increased sensitivity to kanamycin
H54A
inactive. Mutation dos not impact 30S binding affinity. Mutant strain is sensitive to kanamycin and gentamicin
H54E
inactive. Mutation dos not impact 30S binding affinity. Mutant strain is sensitive to kanamycin and gentamicin
K20E
mutation eliminates 30S binding affinity, mutant strain is sensitive to kanamycin and gentamicin
K72E
mutation reduces 30S binding affinity about 5fold, resistance to kanamycin and gentamcin is reduced
R50E
mutation reduces 30S binding affinity about 11-13fold. Mutant strain is sensitive to kanamycin and gentamicin
R68E
mutation reduces 30S binding affinity about 11-13fold, resistance to kanamycin and gentamcin is reduced
additional information
D156A
mutant with drastically increased sensitivity to kanamycin
D182A
mutant with drastically increased sensitivity to kanamycin
E205A
mutant with drastically increased sensitivity to kanamycin
E267A
mutant with drastically increased sensitivity to kanamycin
G135A
mutant with drastically increased sensitivity to kanamycin
K199A
mutant with drastically increased sensitivity to kanamycin
R236A
mutant with drastically increased sensitivity to kanamycin
additional information
-
construction of a series of in-frame knockout and knock-in mutants of Escherichia coli, corresponding to the genotypes rsmF+, DELTArsmF, rsmF+ rmtC+, and DELTArsmF rmtC+, mutant strain growth kinetics, overview
additional information
introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes
additional information
introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes
additional information
introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes
additional information
introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes
additional information
-
construction of a series of in-frame knockout and knock-in mutants of Escherichia coli, corresponding to the genotypes rsmF+, DELTArsmF, rsmF+ rmtC+, and DELTArsmF rmtC+, mutant strain growth kinetics, overview
-
additional information
analysis of sequencefunction relationships of Sgm MTase by limited proteolysis and site-directed and random mutagenesis
additional information
introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes
additional information
replacement of the RmtC loop with four Ala residues (Loop237-246 ->A4) ablates the enzyme's ability to confer resistance to kanamycin and gentamicin. Conserved C-terminal domain residues surrounding the SAM-binding pocket are functionally critical but do not contribute to 30S binding affinity
additional information
introduction of single mutations at the ribosomal A site near the G1405 nucleotide in helix 44 of 16S rRNA to assess their impact on the methylation ability of the Arm methyltransferase in Escherichia coli cells with homogeneous mutant ribosomes
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 50
Sgm is fully stable up to 45 to 50°C, after which point the spectra become progressively more like those of an unstructured random coil. No further change is observed beyond 65°C, where all secondary structure appears to be lost
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned in Streptomyces lividans. The sgm gene is expressed in Micromonospora melanosporea, where its own promoter is active, and also in Escherichia coli under the control of the lacZ promoter
cloning of the sgm gene into pET-25b (+) vector with the addition of N-terminal non-cleavable His6 tag, as well as alanine mutagenesis of residues D156, D182 and R108. The constructs are co-transformed along with pGroESL into the strain BL21 (DE3) of Escherichia coli for protein expression
expression in Escherichia coli, Bacillus subtilis or Staphylococcus aureus
gene armA, recombinant expression in Escherichia coli strain MC338
gene rmtB, recombinant expression in Escherichia coli strain MC338
gene rmtD, recombinant expression in Escherichia coli strain MC338
gene rmtF encoded on a non-self-transferable plasmid pIP849, cotranscribed with the upstream aac(6')-Ib gene, DNA and amino acid sequence determination, analysis, and comparisons, overview. Genetic structure and phylogenetic tree
gene sgm, recombinant expression in Escherichia coli strain MC338
introduction of a recombinant version of the Sgm methyltransferase gene from Micromonospora zionensis into an Escherichia coli strain that has a full complement of housekeeping methyltransferases. Analyses of the 16S rRNA shows that the m5C1407-specific housekeeping methyltransferase RsmF (YebU) is outcompeted by Sgm as the resistance methyltransferase gains access to its own m7G1405 target on the 30S ribosomal subunit. A single amino acid change in Sgm, which lowers the level of conferred resistance, reduces the ability of Sgm to interfere with RsmF methylation on the 30S subunit
sgm is cloned into a yeast expression vector to test whether the prokaryotic methylases can modify the 18S rRNA A-site and thus confer resistance to the aminoglycoside antibiotic G-418. Sgm does not provide resistant phenotypes to yeast cells. Despite all similarities in the antibiotic binding site, methylation by Sgm does not occur in yeast, suggesting that the recognition site for these methylases could be different in 30S and 40S subunits
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
development of strategies to inhibit m7G1405 modification to resensitize bacterial pathogens to aminoglycosides
drug development
medicine
development of strategies to inhibit m7G1405 modification to resensitize bacterial pathogens to aminoglycosides
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
drug development
-
development of potent agents against 16S-RMTase producers as targets for treatment of multidrug resistant bacteria
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maravic Vlahovicek, G.; Cubrilo, S.; Tkaczuk, K.L.; Bujnicki, J.M.
Modeling and experimental analyses reveal a two-domain structure and amino acids important for the activity of aminoglycoside resistance methyltransferase Sgm
Biochim. Biophys. Acta
1784
582-590
2008
Micromonospora zionensis (Q7M0R2)
brenda
Kojic, M.; Topisirovic, L.; Vasiljevic, B.
Cloning and characterization of an aminoglycoside resistance determinant from Micromonospora zionensis
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174
7868-7872
1992
Micromonospora zionensis (Q7M0R2), Micromonospora zionensis
brenda
Kojic, M.; Topisirovic, L.; Vasiljevic, B.
Translational autoregulation of the sgm gene from Micromonospora zionensis
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178
5493-5498
1996
Micromonospora zionensis (Q7M0R2), Micromonospora zionensis
brenda
Savic, M.; Ilic-Tomic, T.; Macmaster, R.; Vasiljevic, B.; Conn, G.L.
Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm
J. Bacteriol.
190
5855-5861
2008
Micromonospora zionensis (Q7M0R2)
brenda
Beauclerk, A.A.; Cundliffe, E.
Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides
J. Mol. Biol.
193
661-671
1987
Micromonospora echinospora
brenda
Savic, M.; Lovric, J.; Tomic, T.I.; Vasiljevic, B.; Conn, G.L.
Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics
Nucleic Acids Res.
37
5420-5431
2009
Frankia sp. (Q2J7L5), Frankia sp. CcI3 (Q2J7L5), Micromonospora echinospora (Q70KC8), Micromonospora zionensis (Q7M0R2)
brenda
Husain, N.; Tkaczuk, K.L.; Tulsidas, S.R.; Kaminska, K.H.; Cubrilo, S.; Maravic-Vlahovicek, G.; Bujnicki, J.M.; Sivaraman, J.
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases
Nucleic Acids Res.
38
4120-4132
2010
Micromonospora zionensis (Q7M0R2), Micromonospora zionensis
brenda
Tomic, T.I.; Moric, I.; Conn, G.L.; Vasiljevic, B.
Aminoglycoside resistance genes sgm and kgmB protect bacterial but not yeast small ribosomal subunits in vitro despite high conservation of the rRNA A-site
Res. Microbiol.
159
658-662
2008
Micromonospora zionensis (Q7M0R2)
brenda
Cubrilo, S.; Babic, F.; Douthwaite, S.; Maravic Vlahovicek, G.
The aminoglycoside resistance methyltransferase Sgm impedes RsmF methylation at an adjacent rRNA nucleotide in the ribosomal A site
RNA
15
1492-1497
2009
Micromonospora zionensis (Q7M0R2)
brenda
Wachino, J.; Yamane, K.; Shibayama, K.; Kurokawa, H.; Shibata, N.; Suzuki, S.; Doi, Y.; Kimura, K.; Ike, Y.; Arakawa, Y.
Novel plasmid-mediated 16S rRNA methylase, RmtC, found in a proteus mirabilis isolate demonstrating extraordinary high-level resistance against various aminoglycosides
Antimicrob. Agents Chemother.
50
178-184
2006
Proteus mirabilis (Q33DX5), Proteus mirabilis ARS68 (Q33DX5)
brenda
Prichon, B.; Courvalin, P.; Galimand, M.
Transferable resistance to aminoglycosides by methylation of G1405 in 16S rRNA and to hydrophilic fluoroquinolones by QepA-mediated efflux in Escherichia coli
Antimicrob. Agents Chemother.
51
2464-2469
2007
plasmid pIP1206
brenda
Wachino, J.; Shibayama, K.; Kimura, K.; Yamane, K.; Suzuki, S.; Arakawa, Y.
RmtC introduces G1405 methylation in 16S rRNA and confers high-level aminoglycoside resistance on Gram-positive microorganisms
FEMS Microbiol. Lett.
311
56-60
2010
Proteus mirabilis (Q33DX5), Proteus mirabilis ARS68 (Q33DX5)
brenda
Liou, G.F.; Yoshizawa, S.; Courvalin, P.; Galimand, M.
Aminoglycoside resistance by ArmA-mediated ribosomal 16S methylation in human bacterial pathogens
J. Mol. Biol.
359
358-364
2006
plasmid pAT780
brenda
Schmitt, E.; Galimand, M.; Panvert, M.; Courvalin, P.; Mechulam, Y.
Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases
J. Mol. Biol.
388
570-582
2009
Escherichia coli
brenda
Gutierrez, B.; Escudero, J.A.; San Millan, A.; Hidalgo, L.; Carrilero, L.; Ovejero, C.M.; Santos-Lopez, A.; Thomas-Lopez, D.; Gonzalez-Zorn, B.
Fitness cost and interference of Arm/Rmt aminoglycoside resistance with the RsmF housekeeping methyltransferases
Antimicrob. Agents Chemother.
56
2335-2341
2012
Escherichia coli, Escherichia coli BW25113
brenda
Galimand, M.; Courvalin, P.; Lambert, T.
RmtF, a new member of the aminoglycoside resistance 16S rRNA N7 G1405 methyltransferase family
Antimicrob. Agents Chemother.
56
3960-3962
2012
Klebsiella pneumoniae (I1YZZ5), Klebsiella pneumoniae BM4686 (I1YZZ5), Klebsiella pneumoniae BM4686
brenda
Wachino, J.; Arakawa, Y.
Exogenously acquired 16S rRNA methyltransferases found in aminoglycoside-resistant pathogenic Gram-negative bacteria: an update
Drug Resist. Updat.
15
133-148
2012
Citrobacter freundii (E9N3S1), Micromonospora echinospora (Q70KC8), Micromonospora inyonensis (Q5Y813), Micromonospora olivasterospora (Q08325), Micromonospora rosea (P24619), Micromonospora zionensis (Q7M0R2), Proteus mirabilis (Q33DX5), Proteus mirabilis ARS68 (Q33DX5), Pseudomonas aeruginosa (Q8GRA1), Pseudomonas aeruginosa (A0MK31), Serratia marcescens (Q76G15), Streptoalloteichus hindustanus (O52472), Streptomyces kanamyceticus (Q75PS4)
brenda
Correa, L.L.; Witek, M.A.; Zelinskaya, N.; Picao, R.C.; Conn, G.L.
Heterologous expression and functional characterization of the exogenously acquired aminoglycoside resistance methyltransferases RmtD, RmtD2, and RmtG
Antimicrob. Agents Chemother.
60
699-702
2015
Escherichia coli, Micromonospora zionensis (Q7M0R2)
brenda
Gutierrez, B.; Douthwaite, S.; Gonzalez-Zorn, B.
Indigenous and acquired modifications in the aminoglycoside binding sites of Pseudomonas aeruginosa rRNAs
RNA Biol.
10
1324-1332
2013
Pseudomonas aeruginosa, Pseudomonas aeruginosa BB1285
brenda
Lioy, V.S.; Goussard, S.; Guerineau, V.; Yoon, E.J.; Courvalin, P.; Galimand, M.; Grillot-Courvalin, C.
Aminoglycoside resistance 16S rRNA methyltransferases block endogenous methylation, affect translation efficiency and fitness of the host
RNA
20
382-391
2014
Escherichia coli, Escherichia coli MM294
brenda
Nosrati, M.; Dey, D.; Mehrani, A.; Strassler, S.E.; Zelinskaya, N.; Hoffer, E.D.; Stagg, S.M.; Dunham, C.M.; Conn, G.L.
Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition
J. Biol. Chem.
294
17642-17653
2019
Proteus mirabilis (Q33DX5)
brenda
Obranic, S.; Babic, F.; Mocibob, M.; Maravic-Vlahovicek, G.
Ribosomal A site binding pattern differs between Arm methyltransferases from clinical pathogens and a natural producer of aminoglycosides
Int. J. Biol. Macromol.
282
137015
2024
Escherichia coli (B8YJJ8), Escherichia coli (Q763K9), Escherichia coli (M4TDG9), Escherichia coli (G4WZ44), Micromonospora zionensis (Q7M0R2), Proteus mirabilis (Q33DX5)
brenda
Srinivas, P.; Nosrati, M.; Zelinskaya, N.; Dey, D.; Comstock, L.R.; Dunham, C.M.; Conn, G.L.
30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC
Proc. Natl. Acad. Sci. USA
120
e2304128120
2023
Escherichia coli (G4WZ44)
brenda
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