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.
Younis
Rasha
R
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom.
Bingle
Lewis E H
LE
Rollauer
Sarah
S
Munera
Diana
D
Busby
Stephen J
SJ
Johnson
Steven
S
Deane
Janet E
JE
Lea
Susan M
SM
Frankel
Gad
G
Pallen
Mark J
MJ
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D011485:Protein Binding; D021382:Protein Sorting Signals; D021381:Protein Transport; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D021382:Protein Sorting Signals; C416081:SepL protein, E coli