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    hscA iron-sulfur cluster biosynthesis chaperone HscA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944885, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hscA
    Official Full Name
    iron-sulfur cluster biosynthesis chaperone HscA
    Primary source
    ECOCYC:EG12130
    Locus tag
    b2526
    See related
    ASAP:ABE-0008315
    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
    ECK2523; hsc
    Summary
    dnaK, hscA, hscC and yegD are paralogs. [More information is available at EcoGene: EG12130]. Hsc66 together with Hsc20 may comprise a chaperone system similar to DnaK/DnaJ . [More information is available at EcoCyc: EG12130].
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    Genomic context

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    Sequence:
    NC_000913.3 (2657085..2658935, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene accessory iron-sulfur cluster assembly protein IscX Neighboring gene reduced ferredoxin Neighboring gene [Fe-S] cluster biosynthesis co-chaperone HscB Neighboring gene iron-sulfur cluster insertion protein IscA

    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. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli. Hesterkamp T, et al. EMBO J, 1998 Aug 17. PMID 9707441, Free PMC Article
    2. Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. Silberg JJ, et al. J Biol Chem, 2000 Mar 17. PMID 10713091
    3. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Vickery LE, et al. Crit Rev Biochem Mol Biol, 2007 Mar-Apr. PMID 17453917
    4. Structural determinants of HscA peptide-binding specificity. Tapley TL, et al. Biochemistry, 2006 Jul 4. PMID 16800630
    5. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Brehmer D, et al. Nat Struct Biol, 2001 May. PMID 11323718

    See all (41) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 ADP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP hydrolysis activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP hydrolysis activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP-dependent protein folding chaperone IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heat shock protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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 unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within cellular response to cold IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in chaperone cofactor-dependent protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in iron-sulfur cluster assembly IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein maturation by iron-sulfur cluster transfer IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein maturation by iron-sulfur cluster transfer IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein refolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of iron-sulfur cluster transfer complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    iron-sulfur cluster biosynthesis chaperone HscA

    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
      2657085..2658935 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417021.1 iron-sulfur cluster biosynthesis chaperone HscA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417021.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A830SGK2
      Conserved Domains (1) summary
      PRK05183
      Location:1 → 616
      hscA; chaperone protein HscA; Provisional
    Nucleotide Protein
    Heading Accession and Version

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