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hchA protein/nucleic acid deglycase 1 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946481, updated on 1-May-2025
Official Symbol
hchA
Official Full Name
protein/nucleic acid deglycase 1
Primary source
ECOCYC:G7055
Locus tag
b1967
See related
ASAP:ABE-0006529
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
ECK1963; yedU; yzzC
Summary
Important for the processing of 8-12mer peptides in vivo. [More information is available at EcoGene: EG11755]. Hsp31 (YedU) is a chaperone that is active as a homodimer . [More information is available at EcoCyc: G7055].
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Sequence:
NC_000913.3 (2035835..2036686)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene pseudo Neighboring gene sensor histidine kinase HprS Neighboring gene DNA-binding transcriptional dual regulator HprR Neighboring gene hydroxyisourate hydrolase/transthyretin-related protein

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures. Sastry MS, et al. J Biol Chem, 2002 Nov 29. PMID 12235139
  2. Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions. Mujacic M, et al. Mol Microbiol, 2004 Feb. PMID 14731284
  3. The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures. Sastry MS, et al. Proc Natl Acad Sci U S A, 2004 Jun 8. PMID 15173574, Free PMC Article
  4. A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function. Quigley PM, et al. Protein Sci, 2004 Jan. PMID 14691241, Free PMC Article
  5. The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites. Zhao Y, et al. Protein Sci, 2003 Oct. PMID 14500888, Free PMC Article

See all (39) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The Parkinsonism-associated protein DJ-1 and its bacterial homologs deglycase 1/Hsp31, deglycase 2/YhbO, and deglycase 3/YajL function as deglycases that repair proteins and nucleotides from endogeneous glycation by glyoxal and methylglyoxal. DJ-1, deglycase 1 and deglycase 2 repair glyoxal- and methylglyoxal-glycated substrates, whereas deglycase 3 principally repairs glyoxal-glycated substrates.
    Title: Further characterization of the Maillard deglycase DJ-1 and its prokaryotic homologs, deglycase 1/Hsp31, deglycase 2/YhbO, and deglycase 3/YajL.
  2. The authors found that Hsp31 displays glyoxalase activity that catalyses the conversion of methylglyoxal (MG) to d-lactate without an additional cofactor.
    Title: Hsp31 of Escherichia coli K-12 is glyoxalase III.
  3. N-terminus verified by Edman degradation on mature peptide
    Title: Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant.
  4. Study presents evidence for an additional, novel, temperature-dependent control of Hsp31 expression by increased transcript stability.
    Title: Thermoregulation of Escherichia coli hchA transcript stability.
  5. Hsp31, the hchA gene product, plays an important role in the acid resistance of starved Escherichia coli but that it has little influence on oxidative-stress survival
    Title: Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables glyoxalase III activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables glyoxalase III activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables glyoxalase III activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides IEA
Inferred from Electronic Annotation
more info
  
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein deglycase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein deglycase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables thiolester hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in DNA damage response IEA
Inferred from Electronic Annotation
more info
  
involved_in DNA repair IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within DNA repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within RNA repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within guanine deglycation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in lactate biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within protein repair IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein repair IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within response to acidic pH IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within response to methylglyoxal IMP
Inferred from Mutant Phenotype
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 HDA PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
protein/nucleic acid deglycase 1
NP_416476.1

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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
    2035835..2036686
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416476.1 protein/nucleic acid deglycase 1 [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416476.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7CSP7, A0AAE4NA36
    Conserved Domains (1) summary
    PRK04155
    Location:1 → 283
    PRK04155; protein deglycase HchA
Nucleotide Protein
Heading Accession and Version

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