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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.

Original publication

DOI

10.1128/JB.00760-10

Type

Journal article

Journal

J Bacteriol

Publication Date

11/2010

Volume

192

Pages

6093 - 6098

Keywords

Amino Acid Sequence, Escherichia coli, Escherichia coli Proteins, Molecular Chaperones, Molecular Sequence Data, Protein Binding, Protein Sorting Signals, Protein Transport, Sequence Alignment, Sequence Homology, Amino Acid