SepL Resembles an Aberrant Effector in Binding to a Class 1 Type III Secretion Chaperone and Carrying an N-Terminal Secretion Signal

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.