Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli.

The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure.

Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA.

Structure of the E. coli protein-conducting channel bound to a translating ribosome.

Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.

Assembly of the translocase motor onto the preprotein-conducting channel.

Signal peptides are allosteric activators of the protein translocase.

The action of cardiolipin on the bacterial translocon.

The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.

The binary protein-protein interaction landscape of Escherichia coli.

A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion.

SecYEG and SecA are the stoichiometric components of preprotein translocase.

A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.

The Escherichia coli SRP and SecB targeting pathways converge at the translocon.

Manual curation notes for Escherichia coli SecG