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hslO molecular chaperone Hsp33 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947178, updated on 17-Dec-2024

Summary

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Official Symbol
hslO
Official Full Name
molecular chaperone Hsp33
Primary source
ECOCYC:G7744
Locus tag
b3401
See related
ASAP:ABE-0011096
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
ECK3388; yrfI
Summary
Hsp33 is functionaly down regulated by zinc binding, zinc masks the hydrophobic surfaces under reduced conditions, release of zinc during oxidative induced disulfide bond formation results in the unmasking of the hydrophobic surfaces and partial activation of chaperone function. [More information is available at EcoGene: EG12930]. The Hsp33 protein is expressed under heat shock conditions and activated by oxidative stress. [More information is available at EcoCyc: G7744].
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Genomic context

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Sequence:
NC_000913.3 (3529774..3530652)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene purine nucleotidase Neighboring gene heat shock protein Hsp15 Neighboring gene putative transport protein YhgE Neighboring gene phosphoenolpyruvate carboxykinase (ATP)

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. Order out of disorder: working cycle of an intrinsically unfolded chaperone. Reichmann D, et al. Cell, 2012 Mar 2. PMID 22385960, Free PMC Article
  2. Redox switch of hsp33 has a novel zinc-binding motif. Jakob U, et al. J Biol Chem, 2000 Dec 8. PMID 10976105
  3. Redox-regulated chaperone function and conformational changes of Escherichia coli Hsp33. Raman B, et al. FEBS Lett, 2001 Jan 26. PMID 11231006
  4. Activation of the redox-regulated molecular chaperone Hsp33--a two-step mechanism. Graumann J, et al. Structure, 2001 May 9. PMID 11377198
  5. Redox-regulated molecular chaperones. Graf PC, et al. Cell Mol Life Sci, 2002 Oct. PMID 12475172, Free PMC Article

See all (29) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Disruption of the TF/DnaK chaperone pathway is rescued by overexpression of the redox-regulated chaperone Hsp33.
    Title: Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones.
  2. fluorescence quenching of the active dimer contradicted the results expected from the domain-swapped fold observed in the truncated dimer crystal
    Title: Verification of the interdomain contact site in the inactive monomer, and the domain-swapped fold in the active dimer of Hsp33 in solution.
  3. crystal structure; Q151E mutant HSP33 retains molecular chaperone activity similar to that of wild-type Hsp33(1-235), suggesting that a Hsp33 monomer is sufficient to interact with slowly unfolded substrate
    Title: Crystal structure of constitutively monomeric E. coli Hsp33 mutant with chaperone activity.
  4. the tight functional regulation of Hsp33 chaperone activity plays a vital role in bacterial survival
    Title: Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.
  5. Hsp33 undergoes conformational and quaternary structural changes leading to the formation of oligomeric species in response to oxidative stress
    Title: Oligomeric Hsp33 with enhanced chaperone activity: gel filtration, cross-linking, and small angle x-ray scattering (SAXS) analysis.
  6. Upon odixative stress, proteins are no longer protected by the DnaK system. Instead, they bind to the redox-regulated chaperone Hsp33.
    Title: Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33.
Submit: New GeneRIF Correction

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 binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein folding chaperone IBA
Inferred from Biological aspect of Ancestor
more info
  
enables protein folding chaperone IDA
Inferred from Direct Assay
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within maintenance of unfolded protein IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
involved_in protein refolding IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within protein refolding IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within response to heat IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within response to oxidative stress IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
molecular chaperone Hsp33

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
    3529774..3530652
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417860.2 molecular chaperone Hsp33 [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417860.2

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A776LMP1, A0A8S7TAE9
    Conserved Domains (1) summary
    PRK00114
    Location:3 → 285
    hslO; Hsp33 family molecular chaperone HslO
Nucleotide Protein
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