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    spy ATP-independent periplasmic chaperone [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946253, updated on 3-Dec-2024

    Summary

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    Official Symbol
    spy
    Official Full Name
    ATP-independent periplasmic chaperone
    Primary source
    ECOCYC:G6939
    Locus tag
    b1743
    See related
    ASAP:ABE-0005812
    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
    ECK1741
    Summary
    Spy is induced by envelope stress, dependent on both CpxR and BaeSR. [More information is available at EcoGene: EG13490]. Expression of spy is regulated by the Cpx envelope stress response as well as by the BaeSR two-component response regulator . [More information is available at EcoCyc: G6939].
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    Genomic context

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    Sequence:
    NC_000913.3 (1825140..1825625, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene NH3-dependent NAD(+) synthetase Neighboring gene excinuclease Cho Neighboring gene HutD family protein Ves Neighboring gene succinylglutamate desuccinylase Neighboring gene N-succinylarginine dihydrolase Neighboring gene aldehyde dehydrogenase Neighboring gene arginine N-succinyltransferase

    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. Electrostatic interactions are important for chaperone-client interaction in vivo. Lee C, et al. Microbiology (Reading), 2018 Jul. PMID 29870331, Free PMC Article
    2. Forces Driving Chaperone Action. Koldewey P, et al. Cell, 2016 Jul 14. PMID 27293188, Free PMC Article
    3. Visualizing chaperone-assisted protein folding. Horowitz S, et al. Nat Struct Mol Biol, 2016 Jul. PMID 27239796, Free PMC Article
    4. Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Stull F, et al. Nat Struct Mol Biol, 2016 Jan. PMID 26619265, Free PMC Article
    5. Super Spy variants implicate flexibility in chaperone action. Quan S, et al. Elife, 2014. PMID 24497545, Free PMC Article

    See all (28) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Insights into the client protein release mechanism of the ATP-independent chaperone Spy.
      Title: Insights into the client protein release mechanism of the ATP-independent chaperone Spy.
    2. Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.
      Title: Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.
    3. We revealed an important protein-folding defect in the DeltaelyC mutant and showed that overproduction of the periplasmic chaperone DsbG or Spy was sufficient to correct the protein-folding defect and restore peptidoglycan biosynthesis.
      Title: The Chaperone Activities of DsbG and Spy Restore Peptidoglycan Biosynthesis in the elyC Mutant by Preventing Envelope Protein Aggregation.
    4. Increasing the ionic strength inhibits ATP-independent periplasmic chaperone, Spy activity in vivo, strongly suggesting that electrostatic forces are important for chaperone function in vivo. The function of the super Spy variant Q100L is also salt-sensitive, despite its increased hydrophobicity, further emphasizing the importance of electrostatic interactions in Spy function.
      Title: Electrostatic interactions are important for chaperone-client interaction in vivo.
    5. Visualizing of Spy chaperone-assisted Im7 protein folding has been reported.
      Title: Visualizing chaperone-assisted protein folding.
    6. Experimental results on Spy-Im7 interactions were used to construct a model for how this chaperone interacts with its clients. It appears that Spy binds to and releases client proteins in a regulated fashion that uses client protein folding as its own cue for release.
      Title: Forces Driving Chaperone Action.
    7. Spy rapidly associates with its substrate, immunity protein 7 (Im7), thereby eliminating Im7's potential for aggregation.
      Title: Substrate protein folds while it is bound to the ATP-independent chaperone Spy.
    8. Establish a good relationship between the degree of instability and the improvement chaperone activity of spy variants.
      Title: Super Spy variants implicate flexibility in chaperone action.
    9. Report of the crystal structure of Escherichia coli spheroplast protein y (EcSpy).
      Title: The crystal structure Escherichia coli Spy.
    10. The induction of spy gene transcription by external zinc may include multiple steps such as through sensing the zinc-induced envelope disorder by BaeSR.
      Title: Involvement of multiple transcription factors for metal-induced spy gene expression in Escherichia coli.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein folding chaperone IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within response to organic cyclic compound IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in outer membrane-bounded periplasmic space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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
    ATP-independent periplasmic chaperone

    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
      1825140..1825625 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416257.1 ATP-independent periplasmic chaperone [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416257.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AJF6
      Conserved Domains (1) summary
      PRK10455
      Location:1 → 161
      PRK10455; periplasmic protein; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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