Any feedback?
Literature summary for 7.4.2.8 extracted from
- Protein export through the bacterial flagellar type III export pathway (2014), Biochim. Biophys. Acta, 1843, 1642-1648.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| PDB ID 2DPY | Salmonella enterica |
| structure analysis | Aquifex aeolicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| FliH | Because FliH suppresses ATP hydrolysis by FliI, FliH coordinates ATP hydrolysis by FliI with protein export. The first 20 residues of FliI (FliIEN) not only regulate FliI ring formation but also are involved in the interaction with FliH | Salmonella enterica |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | assembly of the ATPase complex to the export gate, model, overview | Salmonella enterica | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Salmonella enterica |  |
| Mg2+ | required | Aquifex aeolicus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Salmonella enterica | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Aquifex aeolicus | - |
ADP + phosphate | - |
? | |
| additional information | Salmonella enterica | FliI is the ATPase energy donor of the flagellar type III export apparatus, interactions of flagellar chaperones with ATPase FliI, overview. FliT and the FliT-FliD complex bind to FliI | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aquifex aeolicus | O67531 | - |
- |
| Salmonella enterica | Q8Z5R8 | subsp. enterica serovar Typhimurium | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Salmonella enterica | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Aquifex aeolicus | ADP + phosphate | - |
? | |
| additional information | FliI is the ATPase energy donor of the flagellar type III export apparatus, interactions of flagellar chaperones with ATPase FliI, overview. FliT and the FliT-FliD complex bind to FliI | Salmonella enterica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homohexamer | fully active enzyme form | Salmonella enterica |
| homohexamer | fully active enzyme form, FliI forms hetero-trimers along with the FliH dimer | Aquifex aeolicus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FliI | - |
Salmonella enterica |
| FliI | - |
Aquifex aeolicus |
| More | cf. EC 3.6.3.14 | Salmonella enterica |
| More | cf. EC 3.6.3.14 | Aquifex aeolicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme FliI is a member of the Walker-type ATPase family | Salmonella enterica |
| additional information | flagellar type III export apparatus structure analysis, structure-function relationship, overview. Because FliI binds to FlhAC and the C-terminal domain of FlhB (FlhBC), the FliI6-FliJ ring complex is formed on the FlhAC-FlhBC platform and is stably anchored to the platform through the interaction between FliHEN and FlhATM | Salmonella enterica |
| additional information | flagellar type III export apparatus structure analysis, structure-function relationship, overview. Because FliI binds to FlhAC and the C-terminal domain of FlhB (FlhBC), the FliI6-FliJ ring complex is formed on the FlhAC-FlhBC platform and is stably anchored to the platform through the interaction between FliHEN and FlhATM | Aquifex aeolicus |
| physiological function | the flagellar type III export apparatus consists of a proton-driven export gate and an ATPase complex. The export process is well regulated by dynamic, specific and cooperative interactions among export components, chaperones, and export substrates in a timely manner | Aquifex aeolicus |
| physiological function | the flagellar type III export apparatus consists of a proton-driven export gate and an ATPase complex. The export process is well regulated by dynamic, specific and cooperative interactions among export components, chaperones, and export substrates in a timely manner. Chaperone FliD binds to FliI and significantly enhances or stabilizes the weak interaction between the C-terminal ATPase domain FliICAT and flagellar chaperone FliT94 presumably through cooperative interactions among FliICAT, FliD and FliT94. Because FliH suppresses ATP hydrolysis by FliI, FliH coordinates ATP hydrolysis by FliI with protein export | Salmonella enterica |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
