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    hslU ATPase component of the HslVU protease [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948430, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hslU
    Official Full Name
    ATPase component of the HslVU protease
    Primary source
    ECOCYC:EG11881
    Locus tag
    b3931
    See related
    ASAP:ABE-0012843
    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
    clpY; ECK3923; htpI
    Summary
    An hslU deletion suppresses dnaA46(Ts). [More information is available at EcoGene: EG11881]. HslU is the ATPase component of the HslVU protease, which is composed of HslU and HslV . [More information is available at EcoCyc: EG11881].
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    Genomic context

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    Sequence:
    NC_000913.3 (4120416..4121747, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ribonuclease E inhibitor protein A Neighboring gene 1,4-dihydroxy-2-naphthoate octaprenyltransferase Neighboring gene peptidase component of the HslVU protease Neighboring gene cell division protein FtsN

    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. Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. Baytshtok V, et al. J Biol Chem, 2017 Apr 7. PMID 28223361, Free PMC Article
    2. The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation. Sundar S, et al. Protein Sci, 2012 Feb. PMID 22102327, Free PMC Article
    3. Elimination of basic gaps at high pH values in 2-DE. Kask L, et al. Proteomics, 2009 Dec. PMID 19834893
    4. Expression of heat shock protein D 48.5 of Escherichia coli is subject to modulation by catabolite repression. Peruski LF Jr. Microbiol Res, 1996 Aug. PMID 8817918
    5. Asymmetric nucleotide transactions of the HslUV protease. Yakamavich JA, et al. J Mol Biol, 2008 Jul 25. PMID 18582897, Free PMC Article

    See all (87) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Roles of double-loop (130~159 aa and 175~209 aa) in ClpY(HslU)-I domain for SulA substrate degradation by ClpYQ(HslUV) protease in Escherichia coli.
      Title: Roles of double-loop (130~159 aa and 175~209 aa) in ClpY(HslU)-I domain for SulA substrate degradation by ClpYQ(HslUV) protease in Escherichia coli.
    2. a model in which ATP hydrolysis and linked mechanical function in the HslU ring operate by a probabilistic mechanism.
      Title: Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.
    3. The authors conclude that RcsA is indeed proteolized by ClpYQ protease.
      Title: The degradation of RcsA by ClpYQ(HslUV) protease in Escherichia coli.
    4. Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases
      Title: Transfer-messenger RNA-SmpB protein regulates ribonuclease R turnover by promoting binding of HslUV and Lon proteases.
    5. The I domain plays an active role in coordinating substrate binding, ATP hydrolysis, and protein degradation by the HslUV proteolytic machine.
      Title: The I domain of the AAA+ HslUV protease coordinates substrate binding, ATP hydrolysis, and protein degradation.
    6. Data revealed that an ATP-binding site in domain N, separate from its role in polypeptide (ClpY) oligomerization, is required for complex formation with ClpQ.
      Title: Stepwise activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates.
    7. Results suggest that each ATP-bound HslU subunit activates one HslV subunit and that substrate bound to the HslV active site stimulates the HslU ATPase activity by stabilizing the HslV-HslU interaction.
      Title: HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis.
    8. Study showed that domain I of ClpY contains the residues responsible for recognition of its natural substrates, while domain C is necessary to engage ClpQ.
      Title: Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system.
    9. HslUV is a powerful protein unfoldase and initial substrate engagement by the HslU ATPase occurs after ATP binding.
      Title: Nucleotide-dependent substrate recognition by the AAA+ HslUV protease.
    10. the GYVG pore motif of HslU ATPase has a role in protein unfolding and translocation for degradation by HslV peptidase
      Title: Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase.
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    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 ATP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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
    		  
    contributes_to ATP-dependent peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proteasome-activating activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein domain specific binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular response to heat NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in positive regulation of proteasomal protein catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein denaturation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein unfolding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein unfolding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteolysis involved in protein catabolic process 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
    part_of HslUV protease complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of HslUV protease complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of HslUV protease complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of HslUV protease complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane HDA PubMed 

    General protein information

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    Preferred Names
    ATPase component of the HslVU protease

    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
      4120416..4121747 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418366.1 ATPase component of the HslVU protease [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418366.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A377KEP5, A0A828PF17
      Conserved Domains (1) summary
      PRK05201
      Location:1 → 443
      hslU; ATP-dependent protease ATPase subunit HslU
    Nucleotide Protein
    Heading Accession and Version

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