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

Summary

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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: REVIEWED
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadati; 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].
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Genomic context

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Sequence:: NC_000913.3 (200482..200967)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.
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

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

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 protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in 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 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 more info	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