Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Combined Automated Annotation using Multiple IEA Methods
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.
SecY, SecE, and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase.
Demonstration of a specific Escherichia coli SecY-signal peptide interaction.
FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon.
Global topology analysis of the Escherichia coli inner membrane proteome.
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.
Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS.
Assembly of the translocase motor onto the preprotein-conducting channel.
A role for the two-helix finger of the SecA ATPase in protein translocation.
Signal peptides are allosteric activators of the protein translocase.
The action of cardiolipin on the bacterial translocon.
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes.
The bacterial SRP receptor, SecA and the ribosome use overlapping binding sites on the SecY translocon.
Solubilization and functional reconstitution of the protein-translocation enzymes of Escherichia coli.
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.
Structure, function, and biogenesis of SecY, an integral membrane protein involved in protein export.
Characterization of cold-sensitive secY mutants of Escherichia coli.
Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.
Site-specific antibodies against the PrlA (secY) protein of Escherichia coli inhibit protein export by interfering with plasma membrane binding of preproteins.
A central cavity within the holo-translocon suggests a mechanism for membrane protein insertion.
The SecY membrane component of the bacterial protein export machinery: analysis by new electrophoretic methods for integral membrane proteins.
The secY protein can act post-translationally to promote bacterial protein export.
Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in Escherichia coli.
A previously unidentified gene in the spc operon of Escherichia coli K12 specifies a component of the protein export machinery.
A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.
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.
Identification of a region of interaction between Escherichia coli SecA and SecY proteins.
In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase.
The Escherichia coli SRP and SecB targeting pathways converge at the translocon.
Manual curation notes for Escherichia coli SecY