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Literature summary for 7.4.2.8 extracted from

  • Barta, M.L.; Battaile, K.P.; Lovell, S.; Hefty, P.S.
    Hypothetical protein CT398 (CdsZ) interacts with sigma(54) (RpoN)-holoenzyme and the type III secretion export apparatus in Chlamydia trachomatis (2015), Protein Sci., 24, 1617-1632.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.4.2.8

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Chlamydia trachomatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Chlamydia trachomatis
-
 ADP + phosphate
-
 ?
ATP + H2O Chlamydia trachomatis 434/Bu
-
 ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Chlamydia trachomatis
-
 serovar L2
-
Chlamydia trachomatis A0A0H3MJU0 serovar L2
-
Chlamydia trachomatis 434/Bu
-
 serovar L2
-
Chlamydia trachomatis 434/Bu A0A0H3MJU0 serovar L2
-

Source Tissue

Source Tissue Comment Organism Textmining
flagellum
-
 Chlamydia trachomatis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Chlamydia trachomatis ADP + phosphate
-
 ?
ATP + H2O
-
 Chlamydia trachomatis 434/Bu ADP + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
flagellar ATPase
-
 Chlamydia trachomatis
flagellar T3SS ATPase
-
 Chlamydia trachomatis
FliI
-
 Chlamydia trachomatis
NF-T3SS ATPase
-
 Chlamydia trachomatis
nonflagellar ATPase
-
 Chlamydia trachomatis
T3SS ATPase
-
 Chlamydia trachomatis

General Information

General Information Comment Organism
metabolism type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection Chlamydia trachomatis
additional information protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview Chlamydia trachomatis
physiological function proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia Chlamydia trachomatis
physiological function proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia, interactions between the flagellar ATPase (FliI) and the NF-T3SS ATPase regulator (CdsL) Chlamydia trachomatis