A0A2S1GZ37 · A0A2S1GZ37_9BACI

  • Protein
    ATP-dependent protease subunit HslV
  • Gene
    hslV
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.

Catalytic activity

  • ATP-dependent cleavage of peptide bonds with broad specificity.
    EC:3.4.25.2 (UniProtKB | ENZYME | Rhea)

Activity regulation

Allosterically activated by HslU binding.

Features

Showing features for active site, binding site.

118020406080100120140160180
TypeIDPosition(s)Description
Active site7
Binding site165Na+ (UniProtKB | ChEBI)
Binding site168Na+ (UniProtKB | ChEBI)
Binding site171Na+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentHslUV protease complex
Cellular Componentproteasome core complex
Molecular Functionmetal ion binding
Molecular Functionthreonine-type endopeptidase activity
Biological Processproteolysis involved in protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent protease subunit HslV
  • EC number

Gene names

    • Name
      hslV
    • ORF names
      DCE79_04335

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 2017
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Lysinibacillus

Accessions

  • Primary accession
    A0A2S1GZ37

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.

Family & Domains

Sequence similarities

Belongs to the peptidase T1B family. HslV subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    180
  • Mass (Da)
    19,246
  • Last updated
    2018-07-18 v1
  • Checksum
    B2BEADB7BA4AB940
MGQIHATTIFAIHHKGECAMAGDGQVTLGNAVVMKHTARKVRRLFNGKVLAGFAGSVADAFTLFEMFEVKLNEYNGNLQRAAVEVAKQWRGDKMLRQLEAMLLVMDQSTLLLVSGTGEVIEPDDGILAIGSGGNYALSAGRALKKHAGDHLTAKEIAEAALTTAADICVFTNHNIILEAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP029002
EMBL· GenBank· DDBJ
AWE06666.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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