The Canonical and Accessory Sec System of Gram-positive BacteriaPrabudiansyah, I. & Driessen, A. J. M., 2017, Protein and Sugar Export and Assembly in Gram-positive Bacteria . Bagnoli, F. & Rappuoli, R. (eds.). Cham, Switzerland: Springer International Publishing, p. 45-67 23 p. (Current Topics in Microbiology and Immunology; vol. 404).
Research output: Chapter in Book/Report/Conference proceeding › Chapter › Academic
The Sec system is present in all bacteria and responsible for the translocation of the majority of proteins across the cytoplasmic membrane. The system consists of two principal components: the ATPase motor protein, SecA, and the protein-conducting channel, SecYEG. In addition to this canonical Sec system, several Gram-positive bacteria also possess a so-called accessory Sec system. This is a specialized translocation system that is responsible for the export of a subset of secretory proteins, including virulence factors. The accessory Sec system consists of a second SecA paralog, termed SecA2, with or without a second SecY paralog, termed SecY2. In some bacteria, the accessory Sec system is dependent on the canonical Sec system for functionality, while in other bacteria, they can function independently. In this review, we provide an overview of the current knowledge of the canonical and accessory Sec system of Gram-positive bacteria with a focus on the primary component of the Sec translocase, SecA and SecYEG.
|Title of host publication||Protein and Sugar Export and Assembly in Gram-positive Bacteria|
|Editors||F Bagnoli, R Rappuoli|
|Place of Publication||Cham, Switzerland|
|Publisher||Springer International Publishing|
|Number of pages||23|
|Publication status||Published - 2017|
|Name||Current Topics in Microbiology and Immunology|
- TRANSLOCATION ATPASE SECA, BINDING PROTEIN-GSPB, MYCOBACTERIUM-TUBERCULOSIS SECA1, SIGNAL-SEQUENCE RECOGNITION, LARGE CONFORMATIONAL-CHANGE, RICH REPEAT GLYCOPROTEIN, BACILLUS-SUBTILIS SECA, X-RAY-STRUCTURE, ESCHERICHIA-COLI, STREPTOCOCCUS-GORDONII