Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Molecular and functional characterization of the Salmonella typhimurium invasion genes invB and invC: homology of InvC to the F0F1 ATPase family of proteins.
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Purified InvC has ATPase activity; mutation of the catalytic P-loop residue (K165E) abolishes activity and complementation. invC mutants cannot invade cultured epithelial cells. InvC is similar to the F0F1 ATPase beta subunit.
"purified preparations of InvC showed significant ATPase activity"
Disruption of type III secretion in Salmonella enterica serovar Typhimurium by external guide sequences.
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Knockdown of invC mRNA depletes InvC protein and reduces type III secretion and host cell invasion.
"expression in Salmonella results in invC mRNA and InvC protein depletion, decreased type III secretion and interference with host cell invasion"
Genetic analysis of the Salmonella enterica type III secretion-associated ATPase InvC defines discrete functional domains.
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Active-site mutants of InvC lack ATPase activity and act as dominant negatives. InvC fractionates with the membrane as a peripheral protein, forms oligomers consistent with a hexamer, and interacts with OrgB.
"InvC was localized almost exclusively in the membrane fraction"
Chaperone release and unfolding of substrates in type III secretion.
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InvC recognizes secretion substrates and drives ATP-dependent chaperone release and unfolding of the cognate effector, as AAA+ disassembly machines do.
"InvC induces chaperone release from and unfolding of the cognate secreted protein in an ATP-dependent manner"
Salmonella pathogenicity island 1 (SPI-1) type III secretion of SopD involves N- and C-terminal signals and direct binding to the InvC ATPase.
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SopD binds the SPI-1 ATPase InvC; its secretion depends on N-terminal and C-terminal signals.
"we have identified an association between SopD and the SPI-1 T3S system ATPase, InvC"
Structural Features Reminiscent of ATP-Driven Protein Translocases Are Essential for the Function of a Type III Secretion-Associated ATPase.
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A two-helix-finger motif and a pore loop of the hexameric InvC ring, motifs typical of ATP-driven translocases and unfoldases, are essential for InvC function.
"a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase are essential for InvC function"
In Situ Molecular Architecture of the Salmonella Type III Secretion Machine.
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Cryo-electron tomography places InvC in the hexameric nave of the cytoplasmic sorting platform, C terminus toward the InvA cytoplasmic domain; deleting invC destabilizes the platform.
"InvC was located within the hexameric nave of the wheel with its carboxy-terminus facing the toroidal-shape structure formed by the cytoplasmic domain of InvA"
Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes.
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Soluble SpaO/SpaOC/OrgB/InvC complexes were reconstituted and their stoichiometry and L-shaped organization determined, matching the sorting platform pods seen in situ.
"Here we reconstitute soluble complexes of the Salmonella Typhimurium sorting platform proteins including the ATPase InvC, the regulator OrgB, the protein SpaO and a recently identified subunit SpaOC"
Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.
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Crystal structures of InvC lacking the oligomerization domain, alone and with ATPgammaS or ADP, define the nucleotide site and show ATP-dependent remodelling of two pore-facing loops that are essential for function.
"Both loops face the central pore of the predicted InvC cylinder and are essential for the function of the T3SS ATPase"
Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium.
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The homologous flagellar export ATPase FliI is a Mg2+-dependent ATPase whose activity is unaffected by F-, V- and P-type ATPase inhibitors.
"The activity was not affected by inhibitors of the F-, V- or P-type ATPases"
An energy transduction mechanism used in bacterial flagellar type III protein export.
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In the flagellar type III system the membrane export gate complex is itself a proton-protein antiporter; the soluble ATPase complex acts upstream of that step.
"the export gate complex by itself is a proton-protein antiporter"
Energy source of flagellar type III secretion.
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The flagellar type III secretion apparatus is a proton-driven protein exporter; ATP hydrolysis by the export ATPase is not the force that drives translocation.
"the flagellar secretion apparatus functions as a proton-driven protein exporter"
Falcon deep research report for Salmonella SPI-1 T3SS ATPase InvC (sctN1)
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Correctly identifies P0A1B9 as the SPI-1 injectisome ATPase InvC/SctN1 and concludes that it is a soluble peripheral cytoplasmic component of the sorting platform rather than a membrane transporter subunit.
"InvC is not a membrane transporter subunit and is not itself secreted."
Curation notes for Salmonella SPI-1 T3SS ATPase InvC (SctN1)
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PANTHER node analysis: the GO:0046933/GO:0045259 IBDs sit at PTN008558586, a duplication node above the split between the F1-beta clade (PTN008558588) and the bacterial export-ATPase clade (PTN000390097, subfamilies SF9/SF62/SF81).
"PTN008558586 is a **DUPLICATION** node"