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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
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.
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This record set is specific for:
UNIPROT: Q0PAS9
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Word Map
  • 2.1.1.226
  • aminoglycosides
  • amikacin
  • carbapenemase
  • extended-spectrum
  • plasmid-mediated
  • esbls
  • carbapenem-resistant
  • aminoglycoside-modifying
  • methylase-producing
  • blactx-m
  • aac6\'-ib
  • aac6\'-ib-cr
  • blatem
  • blactx-m-15
  • aminoglycoside-resistant
  • arbekacin
  • blakpc-2
  • macrolide-lincosamide-streptogramin
  • ndm-1-producing
  • carbapenemase-producing
  • amikacin-resistant
  • carbapenemase-encoding
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
rrna methylase, cj0588, tlyaii, rrna methylase tlya, rrna 2'-o-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
rRNA 2'-O-methyltransferase
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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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
show the reaction diagram
-
-
-
?
additional information
?
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50S rRNA is used as substrate in activity assays. Mass spectrometric analyses of Campylobacter jejuni 23S rRNA
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
kinetic analysis
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
serotype O:2
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
polysome profiles
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q0PAS9_CAMJE
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
253
0
29213
TrEMBL
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene tlyA, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 NCTC 11168 (Q0PAS9), Campylobacter jejuni subsp. jejuni ATCC 700819 (Q0PAS9)
Manually annotated by BRENDA team