SPSED: A Signal Peptide Secretion Efficiency Database
Chong Peng, Yixue Guo, Shaodong Ren, Cen Li, Fufeng Liu, Fuping Lu
Abstract
Signal peptides (SPs) are short amino acid sequences that direct the linked proteins into the secretory pathway. SPs are found in the N-terminus of proteins in virtually all organisms. Signal peptidases will remove signal peptides after the protein translocation. Signal peptides are usually 16-30 amino acids long and consist of a positively charged n-region, a hydrophobic h-region, and a c-region. The c-region contains the signal peptidase recognition site Signal peptides are important in diverse fields that range from protein secretion mechanisms to disease diagnosis, especially in recombinant protein production For industrial enzymes production in bacterial cell factories, secreting the synthesized target proteins by the guidance of signal peptides will provide active and stable enzymes and a cost-effective downstream recovery process. In practice, different signal peptides show considerable differences in their ability to drive the secretion of the target protein.