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Information on EC 2.1.1.226 - 23S rRNA (cytidine1920-2'-O)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.226
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.226 23S rRNA (cytidine1920-2'-O)-methyltransferase
IUBMB Comments
The bifunctional enzyme from Mycobacterium tuberculosis 2′-O-methylates cytidine1920 in helix 69 of 23S rRNA and cytidine1409 in helix 44 of 16S rRNA (cf. EC 2.1.1.227, 16S rRNA (cytidine1409-2′-O)-methyltransferase). These methylations result in increased susceptibility to the antibiotics capreomycin and viomycin.
The enzyme appears in viruses and cellular organisms
- 2.1.1.226
- aminoglycosides
- amikacin
- carbapenemase
-
extended-spectrum
-
plasmid-mediated
-
esbls
-
carbapenem-resistant
-
aminoglycoside-modifying
-
methylase-producing
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blactx-m
-
aac6\'-ib
-
aac6\'-ib-cr
-
blatem
- blactx-m-15
-
aminoglycoside-resistant
- arbekacin
- blakpc-2
-
macrolide-lincosamide-streptogramin
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ndm-1-producing
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carbapenemase-producing
-
amikacin-resistant
-
carbapenemase-encoding
Reaction Schemes
show+
=
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+
cytidine1920 in 23S rRNA
=
+
2'-O-methylcytidine1920 in 23S rRNA
Synonyms
rrna methylase, cj0588, tlyaii, rrna 2'-o-methyltransferase, rrna methylase tlya, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-O-methyltransferase
23S rRNA (cytidine-2'-O)-methyltransferase
Cj0588
rRNA 2'-O-methyltransferase
rRNA methylase
rRNA methylase TlyA
TlyA
TlyAI
TlyAII
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (cytidine1920-2'-O)-methyltransferase
The bifunctional enzyme from Mycobacterium tuberculosis 2'-O-methylates cytidine1920 in helix 69 of 23S rRNA and cytidine1409 in helix 44 of 16S rRNA (cf. EC 2.1.1.227, 16S rRNA (cytidine1409-2'-O)-methyltransferase). These methylations result in increased susceptibility to the antibiotics capreomycin and viomycin.
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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 + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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Substrates: the bifunctional enzyme modifies nucleotide C1409 in helix 44 of 16S rRNA and nucleotide C1920 in helix 69 of 23S rRNA
Products: the exact position of the methyl group in the wild-type rRNAs is verified by MALDI quadrupole-TOF tandem MS analysis
Products: the exact position of the methyl group in the wild-type rRNAs is verified by MALDI quadrupole-TOF tandem MS analysis
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 50S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: 50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
Products: -
Products: -
?
additional information
?
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Substrates: 50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
Products: -
Products: -
?
additional information
?
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Substrates: 50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
Products: -
Products: -
?
additional information
?
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Substrates: the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
Products: -
Products: -
?
additional information
?
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Substrates: the purified recombinant enzyme TlyA efficiently 2'-O-methylates C1920 in vitro at a molar enzyme to substrate ratio of 1:10
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional enzyme exhibits the activities of EC 2.1.1.226 and EC 2.1.1.227
Products: -
Products: -
?
additional information
?
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Substrates: the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
Products: -
Products: -
?
additional information
?
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Substrates: the purified recombinant enzyme TlyA efficiently 2'-O-methylates C1920 in vitro at a molar enzyme to substrate ratio of 1:10
Products: -
Products: -
?
additional information
?
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Substrates: the bifunctional enzyme exhibits the activities of EC 2.1.1.226 and EC 2.1.1.227
Products: -
Products: -
?
additional information
?
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Substrates: the TlyAII enzyme methylates efficiently at C1920 in 50S subunits in vitro, although weaker activity is also detected on 70S ribosome and 23S rRNA substrates
Products: -
Products: -
?
additional information
?
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Substrates: the TlyAII enzyme methylates efficiently at C1920 in 50S subunits in vitro, although weaker activity is also detected on 70S ribosome and 23S rRNA substrates
Products: -
Products: -
?
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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 + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: the 50S subunit is the preferred substrate, a modest amount of methylation is seen with free 23S rRNA and 70S ribosomes
Products: -
Products: -
?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 50S rRNA
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
Products: -
Products: -
?
additional information
?
-
Substrates: the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hematologic Neoplasms
Balanoposthitis caused by Pseudomonas aeruginosa co-producing metallo-beta-lactamase and 16S rRNA methylase in children with hematological malignancies.
Infections
Balanoposthitis caused by Pseudomonas aeruginosa co-producing metallo-beta-lactamase and 16S rRNA methylase in children with hematological malignancies.
Infections
Coexistence of blaOXA-23 and armA in multidrug-resistant Acinetobacter baumannii isolated from hospital in South Korea.
Mastitis
Prevalence of 16S rRNA Methylase Gene rmtB Among Escherichia coli Isolated from Bovine Mastitis in Ningxia, China.
Pneumonia
Molecular epidemiology of aminoglycosides resistance on Klebsiella pneumonia in a hospital in China.
Tuberculosis
Virulence properties of Campylobacter jejuni are enhanced by displaying a mycobacterial TlyA methylation pattern in its rRNA.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic analysis
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
37
assay at with Mycobacterium smegmatis ribosomal substrates
37
-
assay at with Mycobacterium smegmatis ribosomal substrates
37
assay at with Mycobacterium smegmatis ribosomal substrates
50
assay at with Thermus thermophilus ribosomal substrates
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
-
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
-
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
evolution
-
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
-
evolution
-
TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
-
evolution
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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TlyA orthologues occur in diverse bacteria and fall into two distinct groups. One group, termed TlyAI, has shorter N- and C-termini and methylates only C1920. The second group, TlyAII, includes the mycobacterial enzyme, and these longer orthologues methylate at both C1409 (c.f. EC 2.1.1.227), and C1920
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malfunction
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the bifunctional enzyme modifies nucleotide C1409 in helix 44 of 16S rRNA and nucleotide C1920 in helix 69 of 23S rRNA. Loss of these rRNA methylations confers resistance to capreomycin and viomycin
malfunction
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disruption of the tlyA ORF can confer capreomycin resistance
malfunction
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
malfunction
deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored
malfunction
loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. Alterations of tlyA gene expression affect both antibiotic drug susceptibility and fitness cost of drug resistance. In particular, the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene. This gene encodes an enzyme that methylates neighboring 16S rRNA position C1409, and as a result of increased TlyA expression the fitness cost of the A1408G mutation is significantly reduced
malfunction
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
-
malfunction
-
loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. Alterations of tlyA gene expression affect both antibiotic drug susceptibility and fitness cost of drug resistance. In particular, the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene. This gene encodes an enzyme that methylates neighboring 16S rRNA position C1409, and as a result of increased TlyA expression the fitness cost of the A1408G mutation is significantly reduced
-
malfunction
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
-
malfunction
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
inactivation of TlyA and loss of its activity confer resistance to capreomycin and viomycin
-
malfunction
-
deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored
-
malfunction
-
deletion of the cj0588 gene in Campylobacter jejuni or substitution with alanine of K80, D162, or K188 in the catalytic center of the enzyme cause complete loss of 2'-O-methylation activity. Campylobacter jejuni strains expressing catalytically inactive versions of Cj0588 have the same phenotype as cj0588-null mutants, and show altered tolerance to capreomycin due to perturbed ribosomal subunit association, reduced motility and impaired ability to form biofilms. These functions are reestablished when methyltransferase activity is restored
-
metabolism
antibiotic resistance mechanisms frequently confer a fitness cost, and these costs can be genetically ameliorated by intra- or extragenic second-site mutations, often without loss of resistance. Another mechanism by which the fitness cost of antibiotic resistance can be reduced is via a regulatory response where the deleterious effect of the resistance mechanism is lowered by a physiological alteration that buffers the mutational effect. In mycobacteria, resistance to the clinically used tuberactinomycin antibiotic capreomycin involves loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. In mycobacteria, this nonmutational mechanism (i.e. gene regulatory) can restore fitness to genetically resistant bacteria. Incubation with capreomycin during bacterial growth resulted in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S), cf. EC 2.1.1.226
metabolism
-
antibiotic resistance mechanisms frequently confer a fitness cost, and these costs can be genetically ameliorated by intra- or extragenic second-site mutations, often without loss of resistance. Another mechanism by which the fitness cost of antibiotic resistance can be reduced is via a regulatory response where the deleterious effect of the resistance mechanism is lowered by a physiological alteration that buffers the mutational effect. In mycobacteria, resistance to the clinically used tuberactinomycin antibiotic capreomycin involves loss-of-function mutations in rRNA methylase TlyA or point mutations in 16S rRNA, in particular the A1408G mutation. Both of these alterations result in resistance by reducing drug binding to the ribosome. In mycobacteria, this nonmutational mechanism (i.e. gene regulatory) can restore fitness to genetically resistant bacteria. Incubation with capreomycin during bacterial growth resulted in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S), cf. EC 2.1.1.226
-
physiological function
bacterial 2'-O-methyltransferase TlyA methylates either both nucleotide C1409 of 16S rRNA and C1920 of 23S rRNA. Both ribosomal methylations increase bacterial susceptibility to ribosome targeting antibiotics capreomycin and viomycin. The enzyme also function as a hemolysin, but increased bacterial hemolytic function is not likely a consequence of TlyA-mediated methylations of the ribosome
physiological function
the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA
physiological function
TlyA methylase modifies the rRNA position 1409, reducing the cost of the A1408G mutation while concomitantly also reducing the antibiotic resistance level, e.g. against capreomycin and viomycin. In response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S rRNA resulting in decreased drug susceptibility. Increased TlyA expression reduces resistance in the A1408G mutant and concomitantly increases fitness
physiological function
-
when Mycobacterium smegmatis bifunctional TlyA-II catalyzing reaction of EC 2.1.1.226 and 2.1.1.227 is expressed in Campylobacter jejuni lacking monofunctional TlyA (which catalyzes the reaction of EC 2.1.1.226), motility, biofilm formation, adhesion to and invasion of human epithelial cells and stimulation of IL-8 production are enhanced above wild-type level
physiological function
inactivation of TlyA methyltransferase reduces the pathogen s ability to form biofilms, to attach, invade and survive in host cells, and to provoke the innate immune response. TlyA-minus strains show reduced amounts of the cytolethal distending toxin (CdtC) and the MlaEFD proteins connected with outer membrane vesicle production
physiological function
-
bacterial 2'-O-methyltransferase TlyA methylates either both nucleotide C1409 of 16S rRNA and C1920 of 23S rRNA. Both ribosomal methylations increase bacterial susceptibility to ribosome targeting antibiotics capreomycin and viomycin. The enzyme also function as a hemolysin, but increased bacterial hemolytic function is not likely a consequence of TlyA-mediated methylations of the ribosome
-
physiological function
-
TlyA methylase modifies the rRNA position 1409, reducing the cost of the A1408G mutation while concomitantly also reducing the antibiotic resistance level, e.g. against capreomycin and viomycin. In response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S rRNA resulting in decreased drug susceptibility. Increased TlyA expression reduces resistance in the A1408G mutant and concomitantly increases fitness
-
physiological function
-
the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA
-
physiological function
-
the enzyme TlyA is an rRNA 2'-O-methyltransferase associated with resistance to cyclic peptide antibiotics such as capreomycin. The bacterial pathogen Campylobacter jejuni possesses the TlyA homologue Cj0588, which contributes to virulence, and is a type I homologue of TlyA that 2'-O-methylates 23S rRNA nucleotide C1920. The contribution of Cj0588 to virulence is a consequence of the enzyme's ability to methylate its rRNA
-
physiological function
-
inactivation of TlyA methyltransferase reduces the pathogen s ability to form biofilms, to attach, invade and survive in host cells, and to provoke the innate immune response. TlyA-minus strains show reduced amounts of the cytolethal distending toxin (CdtC) and the MlaEFD proteins connected with outer membrane vesicle production
-
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
additional information
the S4-type RNA recognition domain (residues 5-64), S-adenosyl-methionine binding domain (residues 84-153), SAM-interacting residues (residues 90-94), and four catalytic residues (K69-D154-K182-E238) are conserved in 2'-O-methyltrasferases TlyA
additional information
mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
-
additional information
-
the S4-type RNA recognition domain (residues 5-64), S-adenosyl-methionine binding domain (residues 84-153), SAM-interacting residues (residues 90-94), and four catalytic residues (K69-D154-K182-E238) are conserved in 2'-O-methyltrasferases TlyA
-
additional information
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
-
additional information
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the cyclic peptide antibiotics capreomycin and viomycin bind on the ribosomal S70 subunit interface close to nucleotides C1409 in 16S rRNA and C1920 in 23S rRNA
-
additional information
-
mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center
-
additional information
-
mechanism of Cj0588 action, overview. Homology modelling of the tertiary structure of the Cj0588 catalytic domain using Mycobacterium tuberculosis TlyA structure (PDB ID 5EOV) as a template. The HhaI methyltransferase structure (PDB ID 2HMY) is used to superimpose the AdoMet cofactor. Three-dimensional modeling of the catalytic domain of Cj0588 reveals a structure typical for 2'-O-methyltransferases with a seven-stranded beta-sheet between five alpha-helix layers and four residues K80, D162, K188 and E245 that comprise the catalytic center
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TLYA_CAMJJ
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
253
0
29175
Swiss-Prot
-
TLYA_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
268
0
28074
Swiss-Prot
-
TLYA_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
268
0
28074
Swiss-Prot
-
A0QYR0_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
269
0
28359
TrEMBL
other Location (Reliability: 2)
HLYA_BRAHO
240
0
26881
Swiss-Prot
Secretory Pathway (Reliability: 3)
Q0PAS9_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
253
0
29213
TrEMBL
other Location (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D162A
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
K188A
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
K80A
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
D162A
-
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
-
K188A
-
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
-
K80A
-
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
-
D162A
-
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
-
K188A
-
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
-
K80A
-
site-directed mutagenesis, inactive enzyme due to impaired rRNA binding, SAM binding is similar to wild-type
-
additional information
additional information
generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview
additional information
-
generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview
-
additional information
-
generation of an inactive Cj0588 deletion mutant. The Campylobacter jejuni 4051cj0588 null-mutant is complemented in trans with plasmid-encoded versions of the cj0588 gene. Inactivation of Cj0588 hinders Campylobacter jejuni motility and impairs biofilm formation, phenotype, overview
-
additional information
generation of a tlyA deletion mutant
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of recombinant tlyA in Escherichia coli markedly increases susceptibility to the drugs capreomycin and viomycin
-
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
gene tlyA, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli
gene tlyA, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
-
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
-
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
-
gene tlyA, DNA and amino acid sequence determination, analysis and comparison, expression in Escherichia coli strain DH1
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S (cf. EC 2.1.1.226) rRNA resulting in decreased drug susceptibility. Incubation with capreomycin during bacterial growth results in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S)
the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene
in response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S (cf. EC 2.1.1.226) rRNA resulting in decreased drug susceptibility. Incubation with capreomycin during bacterial growth results in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S)
in response to capreomycin, cells downregulate TlyA-mediated methylation of 16S and 23S (cf. EC 2.1.1.226) rRNA resulting in decreased drug susceptibility. Incubation with capreomycin during bacterial growth results in a reduced post-transcriptional modification of rRNA at TlyA-dependent sites (1409 in 16S and 1920 in 23S)
-
-
the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene
the common resistance mutation A1408G is accompanied by a physiological change that involves increased expression of the tlyA gene
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maus, C.E.; Plikaytis, B.B.; Shinnick, T.M.
Mutation of tlyA confers capreomycin resistance in Mycobacterium tuberculosis
Antimicrob. Agents Chemother.
49
571-577
2005
Mycobacterium tuberculosis
brenda
Johansen, S.K.; Maus, C.E.; Plikaytis, B.B.; Douthwaite, S.
Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2'-O-methylations in 16S and 23S rRNAs
Mol. Cell
23
173-182
2006
Mycobacterium tuberculosis
brenda
Monshupanee, T.; Johansen, S.K.; Dahlberg, A.E.; Douthwaite, S.
Capreomycin susceptibility is increased by TlyA-directed 2-O-methylation on both ribosomal subunits
Mol. Microbiol.
85
1194-1203
2012
Brachyspira hyodysenteriae (Q06803), Geobacillus stearothermophilus, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis (A0QYR0), no activity in Escherichia coli, Streptomyces coelicolor, Thermus thermophilus, Mycolicibacterium smegmatis mc(2)155 (A0QYR0), Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Monshupanee, T.
Increased bacterial hemolytic activity is conferred by expression of TlyA methyltransferase but not by its 2'-O-methylation of the ribosome
Curr. Microbiol.
67
61-68
2013
Mycobacterium tuberculosis (P9WJ63), Mycobacterium tuberculosis H37Rv (P9WJ63)
brenda
Salamaszynska-Guz, A.; Rose, S.; Lykkebo, C.; Taciak, B.; Bacal, P.; Uspienski, T.; Douthwaite, S.
Biofilm formation and motility are promoted by Cj0588-directed methylation of rRNA in Campylobacter jejuni
Front. Cell. Infect. Microbiol.
7
533
2018
Campylobacter jejuni subsp. jejuni (Q0PAS9), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0PAS9), Campylobacter jejuni subsp. jejuni NCTC 11168 (Q0PAS9)
brenda
Freihofer, P.; Akbergenov, R.; Teo, Y.; Juskeviciene, R.; Andersson, D.; Boettger, E.
Nonmutational compensation of the fitness cost of antibiotic resistance in mycobacteria by overexpression of tlyA rRNA methylase
RNA
22
1836-1843
2016
Mycobacterium tuberculosis (P9WJ63), Mycobacterium tuberculosis H37Rv (P9WJ63)
brenda
Salamaszynska-Guz, A.; Serafinska, I.; Bacal, P.; Douthwaite, S.
Virulence properties of Campylobacter jejuni are enhanced by displaying a mycobacterial TlyA methylation pattern in its rRNA
Cell. Microbiol.
22
e13199
2020
Mycolicibacterium smegmatis
brenda
Salamaszynska-Guz, A.; Rasmussen, P.K.; Murawska, M.; Douthwaite, S.
Campylobacter jejuni virulence factors identified by modulating their synthesis on ribosomes with altered rRNA methylation
Front. Cell. Infect. Microbiol.
11
803730
2021
Campylobacter jejuni subsp. jejuni (A0A0H3PEK7), Campylobacter jejuni subsp. jejuni 81-176 (A0A0H3PEK7)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.226)
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