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hdeA [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948025, updated on 11-Sep-2024

Summary

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Official Symbol
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. Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH. Widjaja MA, et al. Biochim Biophys Acta Proteins Proteom, 2021 Feb. PMID 33253897, Free PMC Article
  2. 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
  3. 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. Garrison MA, et al. Protein Sci, 2014 Feb. PMID 24375557, Free PMC Article
  4. Chaperone activation by unfolding. Foit L, et al. Proc Natl Acad Sci U S A, 2013 Apr 2. PMID 23487787, Free PMC Article
  5. Protein refolding by pH-triggered chaperone binding and release. Tapley TL, et al. Proc Natl Acad Sci U S A, 2010 Jan 19. PMID 20080625, 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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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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