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Literature summary for 7.4.2.5 extracted from

  • Das, S.; Stivison, E.; Folta-Stogniew, E.; Oliver, D.
    Reexamination of the role of the amino terminus of SecA in promoting its dimerization and functional state (2008), J. Bacteriol., 190, 7302-7307.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.4.2.5

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli using special plasmids Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
 molecular weight depends on dimerization rate which depends on concentration of SecA and KCl: at 100 nM KCl molecular weight is 200000 Da, at 300 nM KCl molecular weight is around 140000 Da (both at 1microM SecA), monomer-dimer equilibrium is altered in SecA mutants: mutants lacking 2 to 11 residues of the amino terminus of SecA failed to form dimers at 1microM SecA and 300 nM KCl, determination by gel filtration controlling eluate by photodiode array UV/Vis detector, a differential refractometer and a static, multiangle laser light scattering detector Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 translocation ATPase activity: 0.9 nmol phosphate/microgramm SecA/min, mutants lacking 2 to 11 residues of the amino terminus of SecA shows defect translocation ATPase activities (below 0.1 nmol phosphate/microgramm/min) Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Escherichia coli ADP + phosphate
-
 ?

Subunits

Subunits Comment Organism
dimer chemical cross-linking experiments, dimerization is necessary for the translocation ATPase activity of SecA, monomer-dimer equilibrium is altered in SecA mutants: mutants lacking 2 to 11 residues of the amino terminus of SecA failed to form dimers at 1microM SecA and 300 nM KCl, determination by gel filtration controlling eluate by photodiode array UV/Vis detector, a differential refractometer and a static, multiangle laser light scattering detector Escherichia coli

Synonyms

Synonyms Comment Organism
SecA
-
 Escherichia coli