The SorC family is a large group of bacterial transcription regulators involved in controlling carbohydrate catabolism and quorum sensing. SorC proteins consist of a conserved C-terminal effector-binding domain and an N-terminal DNA-binding domain, whose type divides the family into two subfamilies: SorC/DeoR and SorC/CggR. Proteins of the SorC/CggR subfamily are known to regulate the key node of glycolysis-triose phosphate interconversion. On the other hand, SorC/DeoR proteins are involved in a variety of peripheral carbohydrate catabolic pathways and quorum sensing functions, including virulence. Despite the abundance and importance of this family, SorC proteins seem to be on the periphery of scientific interest, which might be caused by the fragmentary information about its representatives. This review aims to compile the existing knowledge and provide material to inspire future questions about the SorC protein family.

• Keywords
• SorC family, bacterial transcription regulation, carbohydrate metabolism, quorum sensing,
• MeSH
• Bacteria * metabolism   genetics   MeSH
• Bacterial Proteins * metabolism   chemistry   genetics   MeSH
• Quorum Sensing MeSH
• Gene Expression Regulation, Bacterial MeSH
• Transcription Factors * metabolism   chemistry   genetics   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH
• Names of Substances
• Bacterial Proteins * MeSH
• Transcription Factors * MeSH

The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics.

• MeSH
• Bacillus subtilis * genetics   metabolism   MeSH
• Bacterial Proteins * chemistry   metabolism   genetics   MeSH
• DNA, Bacterial metabolism   chemistry   genetics   MeSH
• DNA-Binding Proteins chemistry   metabolism   genetics   MeSH
• DNA chemistry   metabolism   MeSH
• Cryoelectron Microscopy * MeSH
• Fructosediphosphates MeSH
• Crystallography, X-Ray MeSH
• Models, Molecular * MeSH
• Protein Multimerization MeSH
• Operon genetics   MeSH
• Gene Expression Regulation, Bacterial MeSH
• Repressor Proteins * chemistry   metabolism   genetics   MeSH
• Protein Binding MeSH
• Binding Sites MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Bacterial Proteins * MeSH
• DNA, Bacterial MeSH
• DNA-Binding Proteins MeSH
• DNA MeSH
• fructose-1,6-diphosphate MeSH Browser
• Fructosediphosphates MeSH
• Repressor Proteins * MeSH