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

Gene ID: 948430, updated on 26-Mar-2025
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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

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 nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
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 
Preferred Names
ATPase component of the HslVU protease

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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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