Gene Ontology annotation through association of InterPro records with GO terms
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
Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export.
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Skp is synthesized as a precursor with a signal peptide and exported to the periplasm via the Sec pathway
"Skp is synthesized as a larger precursor that is processed upon translocation across the plasma membrane. Translocation is dependent on the H(+)-gradient, ATP, SecA, and SecY"
A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins.
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Skp selectively binds OMPs (OmpA, OmpC, OmpF, LamB) and skp deletion reduces OMP levels
"it could be demonstrated that it bound outer membrane proteins, following SDS-PAGE, with high selectivity. Among these were OmpA, OmpC, OmpF and the maltoporin LamB"
Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein.
Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins.
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Skp is required for release of newly translocated OMPs from the inner membrane and maintenance of their solubility in the periplasm
"Skp is a molecular chaperone involved in generating and maintaining the solubility of early folding intermediates of outer membrane proteins in the periplasmic space of Gram-negative bacteria"
The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.
Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.
Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.
Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.
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Skp forms a jellyfish-like trimer with a central cavity for substrate binding and has an LPS binding site
"The structure of the Skp trimer resembles a jellyfish with alpha-helical tentacles protruding from a beta barrel body defining a central cavity"
A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.
Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
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SurA is the primary OMP chaperone; Skp/DegP rescue OMPs that fall off the SurA pathway
"SurA is the primary chaperone responsible for the periplasmic transit of the bulk mass of OMPs to the YaeT complex. The role of Skp and DegP is amplified in the absence of SurA"
The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions.
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Skp trimer forms stable 1:1 complexes with multiple bacterial OMPs with nanomolar affinity
"The Skp trimer formed 1:1 complexes, OMP.Skp(3), with bacterial OMPs, independent of their size or origin. The dissociation constants of these OMP.Skp(3) complexes were all in the nanomolar range"
The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains.
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Skp holds OmpA beta-barrel unfolded in its cavity while allowing the periplasmic domain to fold independently
"while bound to Skp, the beta-barrel domain of OmpA is maintained in an unfolded state, whereas the periplasmic domain is folded in its native conformation"
Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP.
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Skp rescues aggregation-prone PagP and delivers it for membrane insertion via electrostatic interactions
"the key role of Skp in holding aggregation-prone OMPs prior to their direct or indirect delivery to the membrane"
Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
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OMP substrates bound to Skp populate a dynamic conformational ensemble enabling energy-independent release
"The dynamic state allows for energy-independent substrate release and provides a general paradigm for the conformation of OMP polypeptides bound to energy-independent chaperones"
Deep research synthesis for Escherichia coli Skp
Unfolded Protein Binding Annotation Review