Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cardiolipin | stimulates, K417 and K419 contribute to EpsE's ability to be stimulated by cardiolipin | Vibrio cholerae serotype O1 |
Protein Variants | Comment | Organism |
---|---|---|
K417A/K419A | site-directed mutagenesis, the double lysine mutation in the EpsE zinc-binding domain highly reduces stimulated ATPase activity compared to wild-type by reducing the stimulation through cardiolipin | Vibrio cholerae serotype O1 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Vibrio cholerae serotype O1 | |
Zn2+ | required, residues K417 and K419 are in volved in zinc binding | Vibrio cholerae serotype O1 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Vibrio cholerae serotype O1 | - |
ADP + phosphate | - |
? | |
ATP + H2O | Vibrio cholerae serotype O1 El Tor Inaba N16961 | - |
ADP + phosphate | - |
? | |
ATP + H2O | Vibrio cholerae serotype O1 ATCC 39315 | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio cholerae serotype O1 | P37093 | - |
- |
Vibrio cholerae serotype O1 ATCC 39315 | P37093 | - |
- |
Vibrio cholerae serotype O1 El Tor Inaba N16961 | P37093 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Vibrio cholerae serotype O1 | ADP + phosphate | - |
? | |
ATP + H2O | - |
Vibrio cholerae serotype O1 El Tor Inaba N16961 | ADP + phosphate | - |
? | |
ATP + H2O | - |
Vibrio cholerae serotype O1 ATCC 39315 | ADP + phosphate | - |
? | |
additional information | basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours | Vibrio cholerae serotype O1 | ? | - |
- |
|
additional information | basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours | Vibrio cholerae serotype O1 El Tor Inaba N16961 | ? | - |
- |
|
additional information | basic assay developemnt for quantitatively measuring the in vitro activity of purified ATPases for functional characterization by detecting free phosphate through biding of malachite green molybdate, in vitro activity of the T2S ATPase EpsE can be stimulated by copurification of EpsE with the cytoplasmic domain of EpsL (EpsE-cytoEpsL) and addition of the acidic phospholipid cardiolipin. The assay consists of only one phosphate release measurement step, is highly sensitive, and can typically be performed within a few hours | Vibrio cholerae serotype O1 ATCC 39315 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
AAA+ ATPase | - |
Vibrio cholerae serotype O1 |
adenosine triphosphate-hydrolyzing enzyme | - |
Vibrio cholerae serotype O1 |
EpsE | - |
Vibrio cholerae serotype O1 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Vibrio cholerae serotype O1 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Vibrio cholerae serotype O1 |
General Information | Comment | Organism |
---|---|---|
evolution | EpsE is a AAA+ ATPase and member of the bacterial Type II/IV secretion subfamily of NTPases | Vibrio cholerae serotype O1 |
additional information | enzyme residues K417 and K419 do not contribute to EpsE's basal activity but rather to the ability of the protein to be stimulated by cardiolipin | Vibrio cholerae serotype O1 |
physiological function | adenosine triphosphate-hydrolyzing enzymes, or ATPases, play a critical role in a diverse array of cellular functions. These dynamic proteins can generate energy for mechanical work, such as protein trafficking and degradation, solute transport, and cellular movements. EpsE powers type II secretion (T2S) in Vibrio cholerae, the causative agent of cholera. The T2S system is responsible for the secretion of a wide variety of proteins | Vibrio cholerae serotype O1 |