Gene Symbol: skp
Description: periplasmic chaperone
Alias: ECK0177, JW0173, hlpA, ompH
Species: Escherichia coli str. K-12 substr. MG1655
Products:     skp

Top Publications

  1. Kleinschmidt J. Membrane protein folding on the example of outer membrane protein A of Escherichia coli. Cell Mol Life Sci. 2003;60:1547-58 pubmed publisher
    ..In the periplasm, unfolded OmpA is kept in solution in complex with the molecular chaperone Skp. After binding of periplasmic lipopolysaccharide, OmpA insertion and folding occur spontaneously upon interaction ..
  2. Rizzitello A, Harper J, Silhavy T. Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J Bacteriol. 2001;183:6794-800 pubmed publisher
    ..Using depletion analysis, we directly demonstrated that null mutations in skp and surA, as well as in degP and surA, result in synthetic phenotypes, suggesting that Skp, SurA, and DegP are ..
  3. Patel G, Behrens Kneip S, Holst O, Kleinschmidt J. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry. 2009;48:10235-45 pubmed publisher
    ..A (OmpA) of Escherichia coli from its urea-unfolded form and from the complex with its periplasmic chaperone Skp into lipid bilayers...
  4. Walton T, Sandoval C, Fowler C, Pardi A, Sousa M. The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc Natl Acad Sci U S A. 2009;106:1772-7 pubmed publisher
    ..The 17-kDa protein (Skp) is a periplasmic chaperone that assists the folding and insertion of many OMPs, including OmpA, a model OMP with a ..
  5. Sklar J, Wu T, Kahne D, Silhavy T. Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 2007;21:2473-84 pubmed unknown mechanism that requires the outer membrane YaeT complex and the periplasmic chaperones SurA, DegP, and Skp. Here, we have established the relationship between these three chaperones providing insight into the mechanism of ..
  6. Korndörfer I, Dommel M, Skerra A. Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat Struct Mol Biol. 2004;11:1015-20 pubmed
    The 17-kDa protein (Skp) of Escherichia coli is a homotrimeric periplasmic chaperone for newly synthesized outer-membrane proteins. Here we present its X-ray structure at a resolution of 2.35 A...
  7. Qu J, Behrens Kneip S, Holst O, Kleinschmidt J. Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study. Biochemistry. 2009;48:4926-36 pubmed publisher
    Periplasmic Skp facilitates folding and membrane insertion of many outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria...
  8. Qu J, Mayer C, Behrens S, Holst O, Kleinschmidt J. The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions. J Mol Biol. 2007;374:91-105 pubmed
    The interactions of outer membrane proteins (OMPs) with the periplasmic chaperone Skp from Escherichia coli are not well understood. We have examined the binding of Skp to various OMPs of different origin, size, and function...
  9. Walton T, Sousa M. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol Cell. 2004;15:367-74 pubmed
    The Seventeen Kilodalton Protein (Skp) is a trimeric periplasmic chaperone that assists outer membrane proteins in their folding and insertion into membranes. Here we report the crystal structure of Skp from E. coli...

More Information


  1. Ernst F, Hoffschulte H, Thome Kromer B, Swidersky U, Werner P, Muller M. Precursor-specific requirements for SecA, SecB, and delta muH+ during protein export of Escherichia coli. J Biol Chem. 1994;269:12840-5 pubmed
    ..vesicles (INV) of the in vitro synthesized outer membrane proteins LamB and OmpA and the periplasmic protein Skp of Escherichia coli and demonstrate a precursor-specific dependence on the export factors SecA, SecB, and the ..
  2. Bulieris P, Behrens S, Holst O, Kleinschmidt J. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem. 2003;278:9092-9 pubmed publisher
    ..The deletion of the gene of periplasmic Skp impairs the assembly of outer membrane proteins of bacteria...
  3. Levy R, Weiss R, Chen G, Iverson B, Georgiou G. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones. Protein Expr Purif. 2001;23:338-47 pubmed publisher
    ..GroEL/ES, trigger factor, DnaK/J), as well as signal sequenceless versions of periplasmic chaperones (DsbC and Skp), was examined...
  4. Chen R, Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol. 1996;19:1287-94 pubmed
    ..The corresponding gene was found in a gene bank; it encodes the periplasmic protein Skp. The protein was isolated and it could be demonstrated that it bound outer membrane proteins, following SDS-PAGE, ..
  5. McMorran L, Bartlett A, Huysmans G, Radford S, Brockwell D. Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP. J Mol Biol. 2013;425:3178-91 pubmed publisher
    ..Here, we have investigated the effect of two chaperones, Skp and SurA, on the folding kinetics of the OMP, PagP...
  6. Matsuyama S, Tokuda H. [Transport of outer membrane proteins]. Tanpakushitsu Kakusan Koso. 2004;49:965-6 pubmed
  7. Bothmann H, Pluckthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat Biotechnol. 1998;16:376-80 pubmed
    ..We thus identified the periplasmic protein Skp/OmpH/HlpA as improving phage display of a wide range of scFv fragments...
  8. Yamazaki K, Nagata A, Kano Y, Imamoto F. Isolation and characterization of nucleoid proteins from Escherichia coli. Mol Gen Genet. 1984;196:217-24 pubmed
    ..The biological significance of these nucleoid proteins, which constitute a family of proteins participating in formation of the nucleoid structure, is discussed. ..
  9. Strachan G, Williams S, Moyle S, Harris W, Porter A. Reduced toxicity of expression, in Escherichia coli, of antipollutant antibody fragments and their use as sensitive diagnostic molecules. J Appl Microbiol. 1999;87:410-7 pubmed
    ..Co-expression with the colE1-compatible, arabinose-inducible, skp expression vector pHELP1 prevented bacterial lysis and significantly increased both total and functional expression ..
  10. Missiakas D, Betton J, Raina S. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol. 1996;21:871-84 pubmed
    ..the dsb genes encoding catalysts of the protein disulphide isomerase (PDI) family, as well as to the surA, fkpA and ompH/skp genes...
  11. Schlapschy M, Dommel M, Hadian K, Fogarasi M, Korndörfer I, Skerra A. The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization. Biol Chem. 2004;385:137-43 pubmed
    The 'seventeen kilodalton protein' Skp confers transient solubility on outer membrane proteins during biogenesis in Gram-negative bacteria...
  12. Narayanan N, Chou C. Physiological improvement to enhance Escherichia coli cell-surface display via reducing extracytoplasmic stress. Biotechnol Prog. 2008;24:293-301 pubmed publisher
    ..Coexpression of Skp, a periplasmic chaperone known to interact with several outer membrane proteins for their transport and insertion ..
  13. Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, et al. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J Biol Chem. 2001;276:18804-11 pubmed
    ..Newly translocated PhoE protein could be cross-linked to the periplasmic chaperone Skp at the periplasmic side of the inner membrane...
  14. Thome B, Muller M. Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export. Mol Microbiol. 1991;5:2815-21 pubmed
    Skp of Escherichia coli (OmpH of Salmonella typhimurium) is a protein whose precise function has been obscured by its ubiquity in a wide range of subcellular fractions such as those containing DNA, ribosomes, and outer membranes...
  15. de Cock H, Schafer U, Potgeter M, Demel R, Muller M, Tommassen J. 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. Eur J Biochem. 1999;259:96-103 pubmed
    The Skp protein of Escherichia coli has been proposed to be a periplasmic molecular chaperone involved in the biogenesis of outer membrane proteins...
  16. Coleman J, Raetz C. First committed step of lipid A biosynthesis in Escherichia coli: sequence of the lpxA gene. J Bacteriol. 1988;170:1268-74 pubmed
  17. Dicker I, Seetharam S. Cloning and nucleotide sequence of the firA gene and the firA200(Ts) allele from Escherichia coli. J Bacteriol. 1991;173:334-44 pubmed
    ..code for a small, histonelike DNA-binding protein, has been cloned and found to reside immediately downstream from skp, a gene previously identified as the firA locus. firA encodes a 36-kDa protein...
  18. Schafer U, Beck K, Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem. 1999;274:24567-74 pubmed
    Using a cross-linking approach, we have analyzed the function of Skp, a presumed molecular chaperone of the periplasmic space of Escherichia coli, during the biogenesis of an outer membrane protein (OmpA)...
  19. Hirvas L, Coleman J, Koski P, Vaara M. Bacterial 'histone-like protein I' (HLP-I) is an outer membrane constituent?. FEBS Lett. 1990;262:123-6 pubmed
    ..The nucleotide sequence similarity between the corresponding genes hlpA and ompH is 87%. The ompH gene is located in a gene cluster resembling the hlpA-ORF17 region of E...
  20. Aasland R, Coleman J, Holck A, Smith C, Raetz C, Kleppe K. Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene product. J Bacteriol. 1988;170:5916-8 pubmed
    The 17-kilodalton protein, a DNA-binding protein encoded by the skp gene of Escherichia coli, was found to be identical to histonelike protein I, the product of the firA gene...
  21. Holck A, Kleppe K. Cloning and sequencing of the gene for the DNA-binding 17K protein of Escherichia coli. Gene. 1988;67:117-24 pubmed
    The skp gene encoding the 17K protein, a basic DNA-binding nucleoid-associated protein of Escherichia coli, was cloned as part of a 2.3-kb genomic fragment...
  22. Hirvas L, Koski P, Vaara M. The ompH gene of Yersinia enterocolitica: cloning, sequencing, expression, and comparison with known enterobacterial ompH sequences. J Bacteriol. 1991;173:1223-9 pubmed
    ..protein of Salmonella typhimurium and Escherichia coli and cloned and sequenced the corresponding gene, the ompH gene, of S. typhimurium (P. Koski, M. Rhen, J. Kantele, and M. Vaara, J. Biol. Chem. 264:18973-18980, 1989)...
  23. Wagner J, Heindl J, Gray A, Jain S, Goldberg M. Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri. J Bacteriol. 2009;191:815-21 pubmed publisher
    ..We investigated the role of the periplasmic chaperone Skp in IcsA maturation...
  24. Lathe R, Buc H, Lecocq J, Bautz E. Prokaryotic histone-like protein interacting with RNA polymerase. Proc Natl Acad Sci U S A. 1980;77:3548-52 pubmed
    ..This protein forms the largest of a unique set of three abundant histone-like proteins (HLP) found in E. coli and is hence referred to as HLPI. We discuss possible routes by which these proteins might affect transcription. ..
  25. Burmann B, Wang C, Hiller S. Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp. Nat Struct Mol Biol. 2013;20:1265-72 pubmed publisher
    ..NMR spectroscopy to examine the conformation and dynamics of the Escherichia coli periplasmic chaperone Skp and two of its complexes with OMPs...
  26. Lin B, Renshaw M, Autote K, Smith L, Calveley P, Bowdish K, et al. A step-wise approach significantly enhances protein yield of a rationally-designed agonist antibody fragment in E. coli. Protein Expr Purif. 2008;59:55-63 pubmed publisher
    ..Co-expression of the bacterial chaperon protein Skp alleviated this toxicity. A two-step purification method was used to isolate monomeric Fab59 from the periplasm...
  27. Gatsos X, Perry A, Anwari K, Dolezal P, Wolynec P, Likic V, et al. Protein secretion and outer membrane assembly in Alphaproteobacteria. FEMS Microbiol Rev. 2008;32:995-1009 pubmed publisher
    ..g. Skp, YfgL and NlpB), other proteins are conserved but are missing characteristic domains (e.g. SurA)...
  28. Buescher E, McIlheran S, Banks S, Vadhan Raj S. Alteration of the functional effects of granulocyte-macrophage colony-stimulating factor on polymorphonuclear leukocytes by membrane-fluidizing agents. Infect Immun. 1990;58:3002-8 pubmed
    ..The data suggest that GM-CSF may affect PMN function via mechanisms involving membrane fluidity or cell deformability or both. ..
  29. Muller M, Koch H, Beck K, Schafer U. Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog Nucleic Acid Res Mol Biol. 2001;66:107-57 pubmed
    ..These folding processes require distinct molecular chaperones of the periplasm, such as Skp, SurA, and PpiD.
  30. Jarchow S, Lück C, Görg A, Skerra A. Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp. Proteomics. 2008;8:4987-94 pubmed publisher
    The "seventeen kilodalton protein" (Skp) is a predominant periplasmic chaperone of Escherichia coli, which is involved in the biogenesis of abundant outer membrane proteins (OMPs) such as OmpA, PhoE, and LamB...
  31. Hayhurst A, Harris W. Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments. Protein Expr Purif. 1999;15:336-43 pubmed
    ..We have increased scAb solubility and prevented cell culture lysis by coexpressing the E. coli Skp chaperone gene...
  32. Burmann B, Holdbrook D, Callon M, Bond P, Hiller S. Revisiting the interaction between the chaperone Skp and lipopolysaccharide. Biophys J. 2015;108:1516-1526 pubmed publisher the Lpt system, whereas outer membrane proteins (Omps) are transported by chaperones, including the periplasmic Skp. In this study, we revisit the specificity of the chaperone-lipid interaction of Skp and LPS...
  33. Grabowicz M, Koren D, Silhavy T. The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of ?-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane. MBio. 2016;7:e00312-16 pubmed publisher
    ..that CpxQ combats toxicity at the inner membrane (IM) by downregulating the synthesis of the periplasmic chaperone Skp. Our data indicate that this regulation prevents Skp from inserting ?-barrel outer membrane proteins (OMPs) into ..
  34. Mavrangelos C, Thiel M, Adamson P, Millard D, Nobbs S, Zola H, et al. Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin. Protein Expr Purif. 2001;23:289-95 pubmed publisher
    ..that combines high-level expression driven by a modified Shine-Dalgarno sequence with the periplasmic chaperonin Skp. Using this vector, we are able to obtain higher yields of soluble antibody fragments from cultures without the ..
  35. Helander I, Lindner B, Seydel U, Vaara M. Defective biosynthesis of the lipid A component of temperature-sensitive firA (omsA) mutant of Escherichia coli. Eur J Biochem. 1993;212:363-9 pubmed
    ..Inspection of dephosphorylated free lipid A preparations by laser-desorption mass spectrometry confirmed that significant amounts of heptaacyl lipid A was elaborated by the firA strain grown at 42 degrees C. ..
  36. Thome B, Hoffschulte H, Schiltz E, Muller M. A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli. FEBS Lett. 1990;269:113-6 pubmed
    ..The NH2-terminal 35 amino acids were found to be identical to those of the skp (firA) gene product, to which several putative functions have previously been attributed.