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T3SS EscN ATPase C-terminal domain
This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone [1]. [1]. 17237797. Structural analysis of a prototypical ATPase from the type III. secretion system.. Zarivach R, Vuckovic M, Deng W, Finlay BB, Strynadka NC;. Nat Struct Mol Biol. 2007;14:131-137.. [2]. 17202259. Structural similarity between the flagellar type III ATPase FliI. and F1-ATPase subunits.. Imada K, Minamino T, Tahara A, Namba K;. Proc Natl Acad Sci U S A. 2007;104:485-490. (from Pfam)
ATP synthase alpha/beta family, nucleotide-binding domain
This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho. [1]. 8065448. Structure at 2.8 A resolution of F1-ATPase from bovine heart. mitochondria.. Abrahams JP, Leslie AG, Lutter R, Walker JE;. Nature 1994;370:621-628.. [2]. 9261073. The crystal structure of the nucleotide-free alpha 3 beta 3. subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a. symmetric trimer.. Shirakihara Y, Leslie AG, Abrahams JP, Walker JE, Ueda T,. Sekimoto Y, Kambara M, Saika K, Kagawa Y, Yoshida M;. Structure 1997;5:825-836. (from Pfam)
flagellar protein export ATPase FliI
Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively.
flagellar protein export ATPase FliI is the catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum
FliI/YscN family ATPase
This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins.
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