Abstract
Here we show that the type III secretion gatekeeper protein SepL resembles an aberrant effector protein in binding to a class 1 type III secretion chaperone (Orf12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Escherichia coli / metabolism*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Molecular Chaperones / metabolism*
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Molecular Sequence Data
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Protein Binding
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Protein Sorting Signals
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Protein Transport
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Escherichia coli Proteins
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Molecular Chaperones
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Protein Sorting Signals
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SepL protein, E coli