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    htpG chaperone protein HtpG [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945099, updated on 2-May-2024

    Summary

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    Gene symbol
    htpG
    Gene description
    chaperone protein HtpG
    Primary source
    ASAP:ABE-0001642
    Locus tag
    b0473
    See related
    ECOCYC:EG10461
    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
    ECK0467
    Summary
    HtpG undergoes substantial nucleotide-dependent conformational rearrangements (Huai, 2005; Shiau, 2006). [More information is available at EcoGene: EG10461]. The HtpG protein is the Escherichia coli homolog of the ubiquitous HSP90 family of proteins . [More information is available at EcoCyc: EG10461].
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    Genomic context

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    Sequence:
    NC_000913.3 (495120..496994)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA polymerase III subunit gamma;DNA polymerase III subunit tau Neighboring gene putative nucleoid-associated protein YbaB Neighboring gene recombination mediator protein RecR Neighboring gene adenylate kinase Neighboring gene ferrochelatase Neighboring gene acetylesterase

    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. Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity. Jin Y, et al. Protein Sci, 2017 Jun. PMID 28383119, Free PMC Article
    2. The Bacterial Stress-Responsive Hsp90 Chaperone (HtpG) Is Required for the Production of the Genotoxin Colibactin and the Siderophore Yersiniabactin in Escherichia coli. Garcie C, et al. J Infect Dis, 2016 Sep 15. PMID 27412582
    3. Interactions of Escherichia coli molecular chaperone HtpG with DnaA replication initiator DNA. Grudniak AM, et al. Cell Stress Chaperones, 2015 Nov. PMID 26246199, Free PMC Article
    4. Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity. Motojima-Miyazaki Y, et al. Biochem Biophys Res Commun, 2010 Sep 17. PMID 20727857
    5. Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. Graf C, et al. EMBO J, 2009 Mar 4. PMID 19165152, Free PMC Article

    See all (62) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Folding and domain interactions of three orthologs of Hsp90 have been reported.
      Title: Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy.
    2. bacterial Hsp90 (HtpG) has a pH-dependent ATPase activity that is unique among other Hsp90 homologs. The underlying mechanism is a conformation-specific electrostatic interaction between a single histidine, H255, and bound ATP.
      Title: Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity.
    3. Taken together, these results suggest that a specific region in the nucleotide-binding domain of DnaK is involved in the interaction with Escherichia coli Hsp90, and this interaction is functionally important.
      Title: Interaction of E. coli Hsp90 with DnaK Involves the DnaJ Binding Region of DnaK.
    4. This is the first report highlighting the role of heat shock protein Hps90Ec in the production of two secondary metabolites, colibactin and yersiniabactin, involved in Escherichia coli virulence.
      Title: The Bacterial Stress-Responsive Hsp90 Chaperone (HtpG) Is Required for the Production of the Genotoxin Colibactin and the Siderophore Yersiniabactin in Escherichia coli.
    5. N-terminus verified by Edman degradation on complete protein
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    6. ADP binding drives dramatic conformational changes, suggesting a mechanism by which nucleotides could control client protein binding and release.
      Title: Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.
    Submit: New GeneRIF Correction

    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 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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP-dependent protein folding chaperone IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein-folding chaperone binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables unfolded protein binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in DNA damage response IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within DNA damage response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    acts_upstream_of_or_within FtsZ-dependent cytokinesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein folding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to heat IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within response to heat IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    chaperone protein HtpG
    NP_415006.1

    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
      495120..496994
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415006.1 chaperone protein HtpG [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415006.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A895NW17, A0A8T6Q506
      Conserved Domains (1) summary
      PRK05218
      Location:4 → 623
      PRK05218; heat shock protein 90; Provisional
    Nucleotide Protein
    Heading Accession and Version

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