Ontology highlight
ABSTRACT:
SUBMITTER: Sala A
PROVIDER: S-EPMC4257090 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Sala Ambre A Bordes Patricia P Genevaux Pierre P
Frontiers in microbiology 20141205
Protein export in bacteria is facilitated by the canonical SecB chaperone, which binds to unfolded precursor proteins, maintains them in a translocation competent state and specifically cooperates with the translocase motor SecA to ensure their proper targeting to the Sec translocon at the cytoplasmic membrane. Besides its key contribution to the Sec pathway, SecB chaperone tasking is critical for the secretion of the Sec-independent heme-binding protein HasA and actively contributes to the cell ...[more]