U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

skp periplasmic chaperone Skp [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944861, updated on 19-Feb-2025

Summary

Go to the top of the page Help
Official Symbol
skp
Official Full Name
periplasmic chaperone Skp
Primary source
ECOCYC:EG10455
Locus tag
b0178
See related
ASAP:ABE-0000608
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0177; firA; hlpA; ompH
Summary
The reported binding to DNA was an artifact due to the cationic nature of Skp. [More information is available at EcoGene: EG10455]. Skp is a periplasmic protein chaperone that binds to unfolded outer membrane proteins. [More information is available at EcoCyc: EG10455].
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
Sequence:
NC_000913.3 (200482..200967)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene intramembrane zinc metalloprotease RseP Neighboring gene outer membrane protein assembly factor BamA Neighboring gene UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase Neighboring gene 3-hydroxy-acyl-[acyl-carrier-protein] dehydratase

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Isolation and characterization of nucleoid proteins from Escherichia coli. Yamazaki K, et al. Mol Gen Genet, 1984. PMID 6387397
  2. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones. Levy R, et al. Protein Expr Purif, 2001 Nov. PMID 11676610
  3. The periplasmic E. coli chaperone Skp is a trimer in solution: biophysical and preliminary crystallographic characterization. Schlapschy M, et al. Biol Chem, 2004 Feb. PMID 15101556
  4. Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin. Mavrangelos C, et al. Protein Expr Purif, 2001 Nov. PMID 11676604
  5. Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Korndörfer IP, et al. Nat Struct Mol Biol, 2004 Oct. PMID 15361861

See all (57) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Skp can dissolve aggregated OmpC while SurA cannot convert aggregated OmpC into the monodisperse form and the conformations of OmpC recognized by the two chaperones as well as their stoichiometries of binding are different.
    Title: Single-Molecule Detection Reveals Different Roles of Skp and SurA as Chaperones.
  2. CpxQ combats toxicity at the inner membrane by downregulating the synthesis of the periplasmic chaperone Skp.
    Title: The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane.
  3. Bioinformatic analysis of amino acid conservation, structural analysis of LPS-binding proteins, and MD simulations confirm the absence of a specific lipopolysaccharide binding site on Skp, and reveal a highly conserved salt-bridge network
    Title: Revisiting the interaction between the chaperone Skp and lipopolysaccharide.
  4. The global lifetime of the OmpX-Skp and tOmpA-Skp chaperone-substrate complex is seven orders of magnitude longer, emerging from the short local lifetimes by avidity.
    Title: Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp.
  5. Seventeen kDa protein (Skp) interactions of Skp-OmpA complexes with lipopolysaccharide change the conformation of outer mebrane protein A (OmpA) in the Skp complex for facilitated insertion and folding into membranes.
    Title: Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study.
  6. Evidence presented suggests that DegP/Skp function to rescue OMPs that fall off the SurA pathway.
    Title: Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli.
  7. N-terminus verified by Edman degradation on mature peptide
    Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
Submit: New GeneRIF Correction

Interactions

Go to the top of the page Help
Products Interactant Other Gene Complex Source Pubs Description

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables lipopolysaccharide binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables lipopolysaccharide binding RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables unfolded protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
enables unfolded protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly EXP
Inferred from Experiment
more info
 PubMed 
acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly IGI
Inferred from Genetic Interaction
more info
 PubMed 
acts_upstream_of_or_within Gram-negative-bacterium-type cell outer membrane assembly IPI
Inferred from Physical Interaction
more info
 PubMed 
involved_in chaperone-mediated protein folding IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in chaperone-mediated protein folding IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within protein folding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein insertion into membrane from inner side IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein maturation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein maturation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein stabilization EXP
Inferred from Experiment
more info
 PubMed 
involved_in protein stabilization IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein stabilization IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
located_in cytosol HDA PubMed 
located_in outer membrane-bounded periplasmic space IDA
Inferred from Direct Assay
more info
 PubMed 
located_in periplasmic space IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
periplasmic chaperone Skp

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    200482..200967
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414720.1 periplasmic chaperone Skp [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414720.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S0G0F7
    Conserved Domains (1) summary
    PRK10780
    Location:1 → 161
    PRK10780; molecular chaperone Skp
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.