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The phosphotransferase system (PTS) is involved in the use of carbon sources in bacteria.  Bacillus sphaericus , a bacterium with the ability to produce insecticidal proteins, is unable to use hexoses and pentoses as the sole carbon source, but it has  ptsHI  genes encoding the two general proteins of the PTS: enzyme I (EI) and the histidine phosphocarrier (HPr). In this work, we describe the biophysical and structural properties of HPr from  B. sphaericus , HPr bs , and its affinity towards EI of other species to find out whether there is inter-species binding. Conversely to what happens to other members of the HPr family, HPr bs  forms several self-associated species. The conformational stability of the protein is low, and it unfolds irreversibly during heating. The protein binds to the N-terminal domain of EI from  Streptomyces coelicolor , EIN sc , with a higher affinity than that of the natural partner of EIN sc , HPr sc . Modelling of the complex between EIN sc  and HPr bs  suggests that binding occurs similarly to that observed in other HPr species. We discuss the functional implications of the oligomeric states of HPr bs  for the glycolytic activity of  B. sphaericus , as well as a strategy to inhibit binding between HPr sc  and EIN sc .

The Histidine-Phosphocarrier Protein of the Phosphoenolpyruvate: Sugar Phosphotransferase System of Bacillus sphaericus Self-Associates