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

    Gene ID: 944861, updated on 3-Dec-2024

    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
    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].
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    Genomic context

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    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

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    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

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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

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    Preferred Names
    periplasmic chaperone Skp

    NCBI Reference Sequences (RefSeq)

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    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

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