Clusters of charged residues at the C terminus of MotA and N terminus of MotB are important for function of the Escherichia coli flagellar motor.
MotA contains a conserved C-terminal cluster of negatively charged residues, and MotB contains a conserved N-terminal cluster of positively charged residues. Charge-altering mutations affecting these residues impair motility but do not diminish Mot protein levels. The motility defects are reversed by second-site mutations targeting the same or partner protein.
Hosking
Edan R
ER
Department of Biology, Texas A&M University, College Station, TX 77843-3258, USA.
Manson
Michael D
MD
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution / Q000235:genetics; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D017124:Conserved Sequence; D004926:Escherichia coli / Q000235:genetics / Q000502:physiology*; D005407:Flagella / Q000235:genetics / Q000502:physiology*; D008124:Locomotion; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D016415:Sequence Alignment; D013489:Suppression, Genetic
D001426:Bacterial Proteins; C063010:MotA protein, Bacteria; C064779:MotB protein, Bacteria