Emerging themes in SecA2-mediated protein export

Nat Rev Microbiol. 2012 Nov;10(11):779-89. doi: 10.1038/nrmicro2874. Epub 2012 Sep 24.

Abstract

The conserved general secretion (Sec) pathway carries out most protein export in bacteria and is powered by the essential ATPase SecA. Interestingly, mycobacteria and some Gram-positive bacteria possess two SecA proteins: SecA1 and SecA2. In these species, SecA1 is responsible for exporting most proteins, whereas SecA2 exports only a subset of substrates and is implicated in virulence. However, despite the impressive body of knowledge about the canonical SecA1, less is known concerning SecA2 function. Here, we review our current understanding of the different types of SecA2 systems and outline future directions for their study.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / metabolism*
  • Bacteria / genetics
  • Bacteria / metabolism*
  • Bacteria / pathogenicity
  • Bacterial Physiological Phenomena
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Membrane Transport Proteins / chemistry
  • Membrane Transport Proteins / genetics*
  • Membrane Transport Proteins / metabolism*
  • Protein Transport*
  • SEC Translocation Channels
  • SecA Proteins
  • Virulence Factors / metabolism

Substances

  • Bacterial Proteins
  • Membrane Transport Proteins
  • SEC Translocation Channels
  • Virulence Factors
  • Adenosine Triphosphatases
  • SecA Proteins