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Literature summary for 7.4.2.5 extracted from

  • Yu, D.; Wowor, A.J.; Cole, J.L.; Kendall, D.A.
    Defining the Escherichia coli SecA dimer interface residues through in vivo site-specific photo-cross-linking (2013), J. Bacteriol., 195, 2817-2825.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.4.2.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
Ile3A mutation completely blocks dimerization of SecA in 300 mM KCl buffer Escherichia coli
L2A/I3A mutation does not substantially affect SecA dimerization Escherichia coli
Leu2A mutation completely blocks dimerization of SecA in 300 mM KCl buffer Escherichia coli
Leu5A mutation completely blocks dimerization of SecA in 300 mM KCl buffer Escherichia coli
Leu6A mutation completely blocks dimerization of SecA in 300 mM KCl buffer Escherichia coli
Phe10A mutation completely blocks dimerization of SecA in 300 mM KCl buffer Escherichia coli
V9A/F10A mutation enhances dissociation by 8fold with respect to that of wild-type SecA Escherichia coli
Val9A mutation completely blocks dimerization of SecA in 300 mM KCl buffer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P10408
-
-

Subunits

Subunits Comment Organism
More residues Leu6, the amino terminus (residues 2 to 11) in the nucleotide binding domain, Phe263 in the preprotein binding domain, and Tyr794 and Arg805 in the intramolecular regulator of the ATPase 1 domain are involved in ecSecA dimerization Escherichia coli

Synonyms

Synonyms Comment Organism
SecA
-
 Escherichia coli