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    hdeA periplasmic acid stress chaperone HdeA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948025, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hdeA
    Official Full Name
    periplasmic acid stress chaperone HdeA
    Primary source
    ECOCYC:EG11398
    Locus tag
    b3510
    See related
    ASAP:ABE-0011464
    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
    ECK3494; yhhC; yhiB
    Summary
    Overexpression causes abnormal biofilm architecture. [More information is available at EcoGene: EG11398]. HdeA is a periplasmic protein that plays a role in resistance to low pH, which is involved in pathogenesis . [More information is available at EcoCyc: EG11398].
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    Genomic context

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    Sequence:
    NC_000913.3 (3656408..3656740, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene inner membrane protein YhiD Neighboring gene periplasmic acid stress chaperone HdeB Neighboring gene acid-resistance membrane protein Neighboring gene ncRNA

    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. Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. Yu XC, et al. J Biol Chem, 2019 Mar 1. PMID 30573682, Free PMC Article
    2. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. Hong W, et al. J Biol Chem, 2005 Jul 22. PMID 15911614
    3. Identification of bacterial proteins observed in MALDI TOF mass spectra from whole cells. Holland RD, et al. Anal Chem, 1999 Aug 1. PMID 10450164
    4. Conserved amphiphilic feature is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria. Wu YE, et al. Biochem J, 2008 Jun 1. PMID 18271752
    5. Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Tapley TL, et al. Proc Natl Acad Sci U S A, 2009 Apr 7. PMID 19321422, Free PMC Article

    See all (48) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH.
      Title: Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH.
    2. HdeA binds its substrates heterogeneously, and the "amphiphilic" model for HdeA-substrate interaction is discussed.
      Title: Characterizations of the Interactions between Escherichia coli Periplasmic Chaperone HdeA and Its Native Substrates during Acid Stress.
    3. 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.
    4. these results provide insight into the process by which HdeA is primed to unfold and carry out its chaperone duties below pH 3.0
      Title: NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation.
    5. During anaerobic growth at pH 5.5, strains deleted for fnr showed enhanced transcription of acid-survival genes gadB, cfa, and hdeA, as well as catalase (katE).
      Title: Escherichia coli K-12 survives anaerobic exposure at pH 2 without RpoS, Gad, or hydrogenases, but shows sensitivity to autoclaved broth products.
    6. The small periplasmic chaperone HdeA is directly activated by partial unfolding in a low ph environment.
      Title: Chaperone activation by unfolding.
    7. 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.
    8. the partially unfolded character of active HdeA allows the chaperone to adopt different conformations as required for the recognition and high-affinity binding of different substrate proteins.
      Title: Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding.
    9. 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.
    10. 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.
    Submit: New GeneRIF Correction See all GeneRIFs (12)

    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 protein folding chaperone EXP
    Inferred from Experiment
    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular response to acidic pH IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cellular stress response to acidic pH IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within cellular stress response to acidic pH IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in outer membrane-bounded periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in outer membrane-bounded periplasmic space RCA
    inferred from Reviewed Computational Analysis
    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 HdeA

    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
      3656408..3656740 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417967.1 periplasmic acid stress chaperone HdeA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417967.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376FVA3, A0A8S7SZ47
      Conserved Domains (1) summary
      PRK10208
      Location:19 → 107
      PRK10208; acid-activated periplasmic chaperone HdeA
    Nucleotide Protein
    Heading Accession and Version

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