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    hdeB periplasmic acid stress chaperone HdeB [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948026, updated on 17-Dec-2024

    Summary

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    Official Symbol
    hdeB
    Official Full Name
    periplasmic acid stress chaperone HdeB
    Primary source
    ECOCYC:EG11399
    Locus tag
    b3509
    See related
    ASAP:ABE-0011458
    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
    ECK3493; yhhD; yhiC
    Summary
    RpoS regulon. [More information is available at EcoGene: EG11399]. HdeB is a periplasmic acid stress chaperone. [More information is available at EcoCyc: EG11399].
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    Genomic context

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    Sequence:
    NC_000913.3 (3655966..3656292, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative DNA-binding transcriptional regulator DctR Neighboring gene inner membrane protein YhiD Neighboring gene periplasmic acid stress chaperone HdeA Neighboring gene acid-resistance membrane protein

    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. The Chaperone-Active State of HdeB at pH 4 Arises from Its Conformational Rearrangement and Enhanced Stability Instead of Surface Hydrophobicity. Thapliyal C, et al. Biochemistry, 2024 May 7. PMID 38640496
    2. Salt bridges regulate both dimer formation and monomeric flexibility in HdeB and may have a role in periplasmic chaperone function. Wang W, et al. J Mol Biol, 2012 Jan 20. PMID 22138344, Free PMC Article
    3. Evolutionary silence of the acid chaperone protein HdeB in enterohemorrhagic Escherichia coli O157:H7. Carter MQ, et al. Appl Environ Microbiol, 2012 Feb. PMID 22179243, Free PMC Article
    4. Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB. Malki A, et al. J Biol Chem, 2008 May 16. PMID 18359765
    5. Role of the multidrug resistance regulator MarA in global regulation of the hdeAB acid resistance operon in Escherichia coli. Ruiz C, et al. J Bacteriol, 2008 Feb. PMID 18083817, Free PMC Article

    See all (32) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The Chaperone-Active State of HdeB at pH 4 Arises from Its Conformational Rearrangement and Enhanced Stability Instead of Surface Hydrophobicity.
      Title: The Chaperone-Active State of HdeB at pH 4 Arises from Its Conformational Rearrangement and Enhanced Stability Instead of Surface Hydrophobicity.
    2. HdeB activation is coupled to its intrinsic dynamics instead of structural changes, and therefore its functional mechanism is apparently different from HdeA.
      Title: HdeB chaperone activity is coupled to its intrinsic dynamic properties.
    3. Of these proteins, only HdeB has convincingly been previously shown to function as chaperone in vivo.
      Title: Folding Optimization In Vivo Uncovers New Chaperones.
    4. The authors conclude that E. coli O157:H7 strains have evolved acid survival strategies independent of the HdeA/B chaperones and are more acid resistant than nonpathogenic K-12.
      Title: Evolutionary silence of the acid chaperone protein HdeB in enterohemorrhagic Escherichia coli O157:H7.
    5. This analysis identifies a structural interaction within the HdeB monomer that is disrupted as pH is lowered, leading to enhanced structural flexibility.
      Title: Salt bridges regulate both dimer formation and monomeric flexibility in HdeB and may have a role in periplasmic chaperone function.
    6. Findings show that repression of hdeAB by MarA depends on pH, growth phase, and other regulators of hdeAB and is associated with reduced resistance to acid conditions.
      Title: Role of the multidrug resistance regulator MarA in global regulation of the hdeAB acid resistance operon in Escherichia coli.
    7. HdeA and HdeB not only help to maintain proteins in a soluble state during acid treatment, as previously reported, but also assist, both in vitro and in vivo, in the solubilization at neutral pH of mixed protein-chaperone aggregates formed at acidic pH
      Title: Solubilization of protein aggregates by the acid stress chaperones HdeA and HdeB.
    8. N-terminus verified by Edman degradation on mature peptide
      Title: Small genes/gene-products in Escherichia coli K-12.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cellular stress response to acidic pH IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within response to acidic pH IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within response to acidic pH IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to pH IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    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 acid stress chaperone HdeB

    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
      3655966..3656292 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417966.4 periplasmic acid stress chaperone HdeB [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417966.4

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1M0D3, B1LJ51
      Conserved Domains (1) summary
      PRK11566
      Location:7 → 108
      hdeB; acid-activated periplasmic chaperone HdeB
    Nucleotide Protein
    Heading Accession and Version

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