Q8F3Q5 · HSLU_LEPIN

Function

function

ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.

Features

Showing features for binding site.

147950100150200250300350400450
TypeIDPosition(s)Description
Binding site32ATP (UniProtKB | ChEBI)
Binding site74-79ATP (UniProtKB | ChEBI)
Binding site290ATP (UniProtKB | ChEBI)
Binding site355ATP (UniProtKB | ChEBI)
Binding site427ATP (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
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionpeptidase activity
Molecular Functionproteasome-activating activity
Biological Processprotein unfolding
Biological Processproteolysis involved in protein catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent protease ATPase subunit HslU
  • Alternative names
    • Unfoldase HslU

Gene names

    • Name
      hslU
    • Ordered locus names
      LA_2345

Organism names

Accessions

  • Primary accession
    Q8F3Q5

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001605191-479ATP-dependent protease ATPase subunit HslU

Proteomic databases

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.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the ClpX chaperone family. HslU subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    479
  • Mass (Da)
    53,988
  • Last updated
    2003-03-01 v1
  • Checksum
    51D0B2DDBE94DA9B
MANHPIDQELTSPAEEELTPREIVAKLDEHIISQKNAKKAVAIALRNRTRRKKLDPEMREEIYPKNIIMIGPTGVGKTEIARRLSKLCGAPFLKVEATKYTEVGYVGRDVESMIRDLAVISMNLVKQEFRTKVEETAKQKAEEALLDILLPFPGENKHGSGQITGFATSSTLADEEDRKTHFLETREFMRKKLKTGKLDDQEVELDLPNPSVSQVPMLQVFGAGNLDDLDNQLQNVLGDILPKKNKKRKLKIPEALKALEESEAEKLLDPDKVQREALRRVEEMGIIFLDEIDKIAGREGKSGADVSREGVQRDLLPIVEGATVNTKIGPVKTDHILFIAAGAFHMTKPSDLIPELQGRFPIRVELEKLSREDFEKILTAPCSSLTRQYEALLSTDGIQLEFSLDGIQEIARIAYDMNEKHENIGARRLNTILERLLEEVSFEGPDLPESQRKVRIDGKYVTDRLQGVIQNKDLSQYIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE010300
EMBL· GenBank· DDBJ
AAN49544.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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