Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein.
The seven conserved motifs typical of the helicase superfamily II have been identified in the sequences of Escherichia coli protein SecA, an ATPase mediating protein translocation across the inner membrane of the bacterium, and its Bacillus subtilis homolog Div. It is hypothesized that SecA and Div possess an RNA helicase activity and may couple ATP hydrolysis both to membrane translocation of proteins, and to hairpin unwinding in their own mRNAs, leading to the known autogenous regulation of translation.
Koonin
E V
EV
Institute of Microbiology, Academy of Sciences, Moscow, Russia.
Gorbalenya
A E
AE
D000251:Adenosine Triphosphatases / Q000235:genetics*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D026901:Membrane Transport Proteins; D008969:Molecular Sequence Data; D014176:Protein Biosynthesis; D020365:RNA Helicases; D012316:RNA Nucleotidyltransferases / Q000502:physiology*; D000069816:SEC Translocation Channels; D000081416:SecA Proteins
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; D012316:RNA Nucleotidyltransferases; D000251:Adenosine Triphosphatases; D020365:RNA Helicases; D000081416:SecA Proteins