U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

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.