Literature summary for 2.1.1.224 extracted from

Kaminska, K.H.; Purta, E.; Hansen, L.H.; Bujnicki, J.M.; Vester, B.; Long, K.S.
Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria (2009), Nucleic Acids Res., 38, 1652-1663.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C105A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
C110A	mutation does not affect Cfr activity	Escherichia coli
C112A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
C116A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
C119A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
C338A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
E91A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
F118A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
H214A	moderately decreased resistance to both florfenicol and tiamulin	Escherichia coli
Q28A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli
R25A	mutation lowers the resistance to both florfenicol and tiamulin considerably	Escherichia coli
S189A	mutation lowers the resistance to both florfenicol and tiamulin considerably	Escherichia coli
S212A	mutation eliminates the resistance to both florfenicol and tiamulin	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe-S-clusters	contains a 4Fe-4S cluster. Radical-SAM enzymes contain a [4Fe-4S]+ cluster that is coordinated by the three conserved cysteine thiolate side chains in the CX3CX2C motif and one molecule of S-adenosyl-L-methionine	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	Cfr is plasmid-encoded, the Escherichia coli JW2501-1 strain, that does not contain the RlmN MTase that normally mediates the m2A2503 modification, is used as the host for plasmids expressing the mutated Cfr proteins and isolation of total RNA. This is done to avoid the weak primer extension stop from the m2A2503 methylation that overlaps the Cfr-mediated m8A2503 stop and therefore interferes with assessment of the activity of the mutated Cfr proteins	-

Synonyms

Synonyms	Comment	Organism
Cfr methyltransferase	-	Escherichia coli

General Information

General Information	Comment	Organism
evolution	bioinformatics analysis of the Cfr/RlmN family establishes their significant evolutionary link with radical-S-adenosyl-L-methionine enzymes. The RlmN subfamily is likely the ancestral form, whereas the Cfr subfamily arose via duplication and horizontal gene transfer	Escherichia coli

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Release 2023.1 (January 2023)