Gene Ontology annotation through association of InterPro records with GO terms

Gene Ontology annotation based on Enzyme Commission mapping

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

Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Zinc stabilizes the SecB binding site of SecA.

Interaction network containing conserved and essential protein complexes in Escherichia coli.

Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.

Protein complexes of the Escherichia coli cell envelope.

A protein network for phospholipid synthesis uncovered by a variant of the tandem affinity purification method in Escherichia coli.

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

Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.

Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.

Delta mu H+ and ATP function at different steps of the catalytic cycle of preprotein translocase.

Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.

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.

Orientation of SecA and SecB in complex, derived from disulfide cross-linking.

SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.

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.

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.

The binary protein-protein interaction landscape of Escherichia coli.

SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.

Lipids Activate SecA for High Affinity Binding to the SecYEG Complex.

SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

SecA mediates cotranslational targeting and translocation of an inner membrane protein.

Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.

Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli.

Identification of a region of interaction between Escherichia coli SecA and SecY proteins.

Manual curation notes for Escherichia coli SecA