skp
Domain
Composed of a compact central beta-barrel domain with long alpha-helical extensions that form a three-pronged structure around an internal cavity. Substrate proteins may be bound in this cavity.
Function
Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.
Sequence Similarities
Belongs to the Skp family.
Cellular localization
- Periplasm
Alternative names
hlpA, ompH, b0178, JW0173, skp, Chaperone protein Skp, DNA-binding 17 kDa protein, Histone-like protein HLP-1, Seventeen kilodalton protein