Protein exporter function and in vitro ATPase activity are correlated in ABC‐domain mutants of HlyB

Summary The Escherichia coli toxin exporter HlyB comprises an integral membrane domain fused to a cytoplasmic domain of the ATP‐binding casette (ABC) super‐family, and it directs translocation of the 110kDa haemolysin protein out of the bacterial cell without using an N‐terminal secretion signal pep...

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Veröffentlicht in:	Molecular microbiology 1995-04, Vol.16 (1), p.87-96
Hauptverfasser:	Koronakis, Eva, Hughes, Colin, Milisav, Irina, Koronakis, Vassilis
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Amino Acid Sequence ATP-Binding Cassette Transporters Endopeptidase K Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Hemolysin Proteins - chemistry Hemolysin Proteins - genetics Hemolysin Proteins - metabolism Kinetics Molecular Sequence Data Mutagenesis, Site-Directed Mutation Protein Conformation Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Restriction Mapping Serine Endopeptidases - metabolism Structure-Activity Relationship
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