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 keyword mapping
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
Combined Automated Annotation using Multiple IEA Methods
Deep research on SecA function in Bacillus subtilis
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Comprehensive review of SecA structure and mechanism
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SecA cycles between cytoplasm and membrane during translocation
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ATP hydrolysis drives conformational changes pushing polypeptides through SecYEG
Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli secA mutants in vivo.
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Mutagenesis demonstrates K106 is essential for SecA ATPase activity
"Replacement of a lysine residue at position 106, which corresponds to an invariable amino acid residue, in the consensus motif by asparagine (K106N) resulted in the loss of the ability of the B. subtilis SecA protein to complement the growth and secretion defects of E. coli secA mutants"
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Experimental evidence for catalytic activity EC 7.4.2.8
"We conclude that lysine 106 is part of the catalytic ATP-binding site of the B. subtilis SecA protein, which is required for protein translocation in vivo"
Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA.
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Crystal structure of SecA with and without ADP
"We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively"
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Reveals conformational changes upon nucleotide binding
"Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding"
Super Resolution Fluorescence Microscopy and Tracking of Bacterial Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein Microdomains within the Bacterial Membrane but Absence of Clusters Containing Detergent-Resistant Proteins.
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SecA shows some colocalization with FloA/FloT membrane assemblies
"B. subtilis flotillins can be co-isolated with NfeD proteins of unknown function, with the signaling receptor KinC [26], cell wall synthesis enzyme Pbp5, secretory protein SecY, membrane transporters like FhuD"
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Experimental evidence for membrane raft localization
"flotillins have been suggested to set up microdomains within the membrane, by recruiting other proteins and possibly specific lipids into the special structures"