The protein FkpA from the periplasm of Escherichia coli exhibits both cis/trans peptidyl-prolyl isomerase (PPIase) and chaperone activities.

Here, we show that FkpA, a heat shock periplasmic peptidyl-prolyl cis/trans isomerase (PPIase), suppresses the formation of inclusion bodies from a defective- ...

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Catalytic activity.

1 jun 2023 · FkpA is part of a periplasmic chaperone network that maintains outer membrane proteins (OMPs) in an unfolded state prior to membrane insertion [ ...

9 jan 2014 · We identified FkpA as the multicopy suppressor for the lethal phenotype of the ΔsurA Δskp strain. ... These results strongly suggest a functional ...

The protein FkpA from the periplasm of Escherichia coli exhibits both cis/trans peptidyl-prolyl isomerase (PPIase) and chaperone activities.

13 apr 2010 · As Skp and FkpA are both molecular chaperones with general ability to refold misfolded proteins and prevent their aggregation into insoluble ...

12 feb 2023 · The results indicate that FkpA behaves as a chaperone and not as a folding catalyst to influence the OMP folding trajectory. Consistent with the ...

Recombinant Escherichia coli FKBP-type peptidyl-prolyl cis-trans isomerase fkpA (fkpA) ; Mol. Weight. 33.2 kDa ; Protein Length. Full Length of Mature Protein.

E. coli fkpA protein · E. coli fkpA protein [orb358164]. Purity: Greater than 90% as determined by SDS-PAGE. MW: 42.3 kDa. Source: E.coli · E. coli fkpA protein ...