BRENDA - Enzyme Database show
show all sequences of 4.6.1.21

CdiA from enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria

Beck, C.; Morse, R.; Cunningham, D.; Iniguez, A.; Low, D.; Goulding, C.; Hayes, C.; Structure 22, 707-718 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
cloning of cdiA-CTECL under the control of an arabinose-inducible promoter and expression in Escherichia coli, which leads to growth inhibition of the bacterial cells
Enterobacter cloacae
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
CdiA-CT toxins are specifically neutralized by cognate CdiI immunity proteins to protect toxin-producing cells from autoinhibition
Enterobacter cloacae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Enterobacter cloacae
the CdiA-CTECL toxin has 16S rRNase activity
?
-
-
-
additional information
Enterobacter cloacae ATCC 13047
the CdiA-CTECL toxin has 16S rRNase activity
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Enterobacter cloacae
-
-
-
Enterobacter cloacae ATCC 13047
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the CdiA-CTECL toxin has 16S rRNase activity
730982
Enterobacter cloacae
?
-
-
-
-
additional information
the CdiA-CTECL toxin has 16S rRNase activity
730982
Enterobacter cloacae ATCC 13047
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
cloning of cdiA-CTECL under the control of an arabinose-inducible promoter and expression in Escherichia coli, which leads to growth inhibition of the bacterial cells
Enterobacter cloacae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
CdiA-CT toxins are specifically neutralized by cognate CdiI immunity proteins to protect toxin-producing cells from autoinhibition
Enterobacter cloacae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Enterobacter cloacae
the CdiA-CTECL toxin has 16S rRNase activity
?
-
-
-
additional information
Enterobacter cloacae ATCC 13047
the CdiA-CTECL toxin has 16S rRNase activity
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the CdiA-CTECL toxin has 16S rRNase activity
730982
Enterobacter cloacae
?
-
-
-
-
additional information
the CdiA-CTECL toxin has 16S rRNase activity
730982
Enterobacter cloacae ATCC 13047
?
-
-
-
-
General Information
General Information
Commentary
Organism
additional information
the three-dimensional structure of enzyme CdiA-CTECL reveals similarity to the C-terminal nuclease domain of colicin E3. The resolved C-terminal domain of enzyme CdiA-CTECL consists of an N-terminal alpha helix, followed by a twisted five-stranded antiparallel beta sheet. The domain contains two long loops, L2 and L4, which connect beta1 to beta2 and beta3 to beta4, respectively
Enterobacter cloacae
physiological function
the 16S rRNase enzyme is a contact-dependent growth inhibition toxin unvolved in inter-bacterial competition. CdiA-CTECL cleaves 16S rRNA in vivo to inhibit cell growth, overview
Enterobacter cloacae
General Information (protein specific)
General Information
Commentary
Organism
additional information
the three-dimensional structure of enzyme CdiA-CTECL reveals similarity to the C-terminal nuclease domain of colicin E3. The resolved C-terminal domain of enzyme CdiA-CTECL consists of an N-terminal alpha helix, followed by a twisted five-stranded antiparallel beta sheet. The domain contains two long loops, L2 and L4, which connect beta1 to beta2 and beta3 to beta4, respectively
Enterobacter cloacae
physiological function
the 16S rRNase enzyme is a contact-dependent growth inhibition toxin unvolved in inter-bacterial competition. CdiA-CTECL cleaves 16S rRNA in vivo to inhibit cell growth, overview
Enterobacter cloacae
Other publictions for EC 4.6.1.21
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
730982
Beck
CdiA from enterobacter cloacae ...
Enterobacter cloacae, Enterobacter cloacae ATCC 13047
Structure
22
707-718
2014
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134565
Karpetsky
Covalent linkage of poly(A) to ...
Enterobacter sp.
J. Biol. Chem.
255
2713-2721
1980
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134566
Frank
Peptides isolated from Enterob ...
Enterobacter sp.
Biochim. Biophys. Acta
432
369-380
1976
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134067
Krishna
On the localization of ribonuc ...
Enterobacter sp.
FEBS Lett.
29
105-108
1973
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134567
Marotta
Preferred sites of digestion o ...
Enterobacter sp.
Biochemistry
12
2901-2904
1973
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134568
Levy
Enterobacter ribonuclease. II. ...
Enterobacter sp.
Biochim. Biophys. Acta
246
476-486
1971
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134569
Levy
Residue specificity of a ribon ...
Enterobacter sp.
J. Biol. Chem.
245
3257-3262
1970
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