Staphylococcus ores is a grand positive bacterium that is about 2 micrometers in size and can be found on the skin of about 30% of the population. Although often benign, it can cause endocratitis, toxic shock syndrome, skin infections, sepsis and other illnesses. Staphylococcus ores is also common foodborne pathogen found in meat and meat products. Whites-preyte methods to preserve foods are the use of excess amounts of sugar or salt to dehydrate the products. This can prevent bacterial growth and hence the transmission of foods for the organisms. Staphylococcus ores, however, is exceptionally resistant to high cell concentrations and therefore can survive these processes better than many other organisms. Recent work in Staphylococcus ores has revealed a second messenger called cyclic-diampt that interacts with several proteins that target early salt tolerance genes. These are KTRA, a potassium transporter, KTPD, a sensor-histoding kinase potentially involved in potassium-uptake, CPAA, another protein supposedly involved in cation transport, but also PSDA, a protein of unknown function. In our recent study, we were able to identify an additional target of cyclic-diampt in Staphylococcus ores, the ABC transporter component OPUCA. The OPUCABC transporter consists of OPUCA, the ADPAA's component that provides energy for the transport. OPUCB and OPUCD, the main transporter components involved in translocation of the substrates, and OPUCC, the substrate binding protein responsible for the specificity. This transporter is supposedly involved in the uptake of voidsmalites, and this can help Staphylococcus ores to cope with osmotic stresses. Binding of cycidiampt occurs via the CBS domain of OPUCA and this binding is specific for a nucleotide cycidiampt. Other nucleotides, such as ATP, AMP, or cyclic-AMP, are unable to outcompete binding of cycidiampt. With the help of x-ray crystallography, we were able to elucidate a structure of OPUCA as depicted here. By comparison to MJ01000, the structure related protein colored in blue, we can make educated guesses where a cyclic-diampt could be binding. Exchange of important amino acids and subsequent binding testing revealed that a proposed binding site is likely the functional region. Further experiments revealed that the OPUCC transporter is able to transport carnitin, whereas glycinebadian and choline are not taken up in significant amounts. When cyclic-dimpt levels were increased in the cell, the uptake of carnitin was reduced compared to wild-type cells. Taking together, our research highlights the world of cyclic-diampt as a regulator for somatic stresses. This knowledge may help in the future to prevent foodborne stuff or as infections. More information can be found in the paper. The second messenger of cyclic-diampt inhibits the awesome late-optic system OPUC in Staphyl-oxorius. By Schuster and Bellisidol, published in Science Sikling, Volume 9, issue 441 on August 16, 2016. Thank you for watching.