U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

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

    Gene ID: 948429, updated on 17-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    hslV
    Official Full Name
    peptidase component of the HslVU protease
    Primary source
    ECOCYC:EG11676
    Locus tag
    b3932
    See related
    ASAP:ABE-0012845
    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
    clpQ; ECK3924; htpO; yiiC
    Summary
    HslV is the peptidase component of the HslVU protease, which is composed of HslU and HslV . [More information is available at EcoCyc: EG11676].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (4121757..4122287, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 1,4-dihydroxy-2-naphthoate octaprenyltransferase Neighboring gene ATPase component of the HslVU protease Neighboring gene cell division protein FtsN Neighboring gene DNA-binding transcriptional repressor CytR

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. A comprehensive view on proteasomal sequences: implications for the evolution of the proteasome. Gille C, et al. J Mol Biol, 2003 Mar 7. PMID 12595256
    2. Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation. Park E, et al. J Mol Biol, 2013 Aug 23. PMID 23707406
    3. Effect of ELF magnetic fields on protein synthesis in Escherichia coli K12. Nakasono S, et al. Radiat Res, 2000 Aug. PMID 10931694
    4. Crystal structure of heat shock locus V (HslV) from Escherichia coli. Bochtler M, et al. Proc Natl Acad Sci U S A, 1997 Jun 10. PMID 9177170, Free PMC Article
    5. Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. Wang J, et al. J Struct Biol, 1998 Dec 15. PMID 10049803

    See all (81) 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. The authors conclude that RcsA is indeed proteolized by ClpYQ protease.
      Title: The degradation of RcsA by ClpYQ(HslUV) protease in Escherichia coli.
    3. Collectively, these results suggest that substrate degradation by HslV is controlled by gating of its pores.
      Title: Structural alteration in the pore motif of the bacterial 20S proteasome homolog HslV leads to uncontrolled protein degradation.
    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. 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.
    6. 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.
    7. Study show that ClpQ engage domain I of ClpY.
      Title: Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system.
    8. N-terminus verified by Edman degradation on mature peptide
      Title: HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome.
    9. 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.
    Submit: New GeneRIF Correction

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptidase 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 
    enables threonine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables threonine-type endopeptidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular response to heat NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in protein catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein denaturation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteolysis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in proteolysis involved in protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proteolysis involved in protein catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within proteolysis involved in protein catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    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 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 
    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 
    part_of proteasome complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of proteasome core complex IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    peptidase component of the HslVU protease

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      4121757..4122287 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418367.1 peptidase component of the HslVU protease [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418367.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A135PLB9, A0A828U1K2, A0A829KZG5, A0AAN3M7X8, A0AAN4NRC6
      Conserved Domains (1) summary
      PRK05456
      Location:1 → 172
      PRK05456; ATP-dependent protease subunit HslV
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.