Abstract
An essential component of all type III secretion systems is a highly conserved ATPase that shares significant amino acid sequence similarity to the beta subunit of the F(0)F(1) ATPases and is thought to provide the energy for the secretion process. We have performed a genetic and functional analysis of InvC, the ATPase associated with the Salmonella enterica type III secretion system encoded within its pathogenicity island 1. Through a mutagenesis analysis, we have identified amino acid residues that are essential for specific activities of InvC, such as nucleotide hydrolysis and membrane binding. This has allowed us to define discrete domains of InvC that are specifically associated with different essential activities of this protein.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Catalytic Domain / genetics
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DNA Mutational Analysis
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DNA, Bacterial / genetics*
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Models, Molecular
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Molecular Sequence Data
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Nucleotides / metabolism
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Protein Structure, Tertiary
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Proton-Translocating ATPases / chemistry
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Proton-Translocating ATPases / genetics*
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Proton-Translocating ATPases / metabolism
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Salmonella typhimurium / genetics*
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Salmonella typhimurium / metabolism
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Salmonella typhimurium / pathogenicity
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Sequence Alignment
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Virulence / genetics
Substances
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Bacterial Proteins
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DNA, Bacterial
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Nucleotides
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invC protein, Salmonella typhimurium
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Proton-Translocating ATPases