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Literature summary extracted from

  • Minamino, T.
    Protein export through the bacterial flagellar type III export pathway (2014), Biochim. Biophys. Acta, 1843, 1642-1648.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.4.2.8 PDB ID 2DPY Salmonella enterica
7.4.2.8 structure analysis Aquifex aeolicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.4.2.8 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

EC Number Localization Comment Organism GeneOntology No. Textmining
7.4.2.8 additional information assembly of the ATPase complex to the export gate, model, overview Salmonella enterica
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.4.2.8 Mg2+ required Salmonella enterica
7.4.2.8 Mg2+ required Aquifex aeolicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.4.2.8 ATP + H2O Salmonella enterica
-
ADP + phosphate
-
?
7.4.2.8 ATP + H2O Aquifex aeolicus
-
ADP + phosphate
-
?
7.4.2.8 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

EC Number Organism UniProt Comment Textmining
7.4.2.8 Aquifex aeolicus O67531
-
-
7.4.2.8 Salmonella enterica Q8Z5R8 subsp. enterica serovar Typhimurium
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.4.2.8 ATP + H2O
-
Salmonella enterica ADP + phosphate
-
?
7.4.2.8 ATP + H2O
-
Aquifex aeolicus ADP + phosphate
-
?
7.4.2.8 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

EC Number Subunits Comment Organism
7.4.2.8 homohexamer fully active enzyme form Salmonella enterica
7.4.2.8 homohexamer fully active enzyme form, FliI forms hetero-trimers along with the FliH dimer Aquifex aeolicus

Synonyms

EC Number Synonyms Comment Organism
7.4.2.8 FliI
-
Salmonella enterica
7.4.2.8 FliI
-
Aquifex aeolicus
7.4.2.8 More cf. EC 3.6.3.14 Salmonella enterica
7.4.2.8 More cf. EC 3.6.3.14 Aquifex aeolicus

General Information

EC Number General Information Comment Organism
7.4.2.8 evolution enzyme FliI is a member of the Walker-type ATPase family Salmonella enterica
7.4.2.8 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
7.4.2.8 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
7.4.2.8 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
7.4.2.8 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