A0A1S6WS70 · A0A1S6WS70_9HYPH

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

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site.

143650100150200250300350400
TypeIDPosition(s)Description
Binding site19ATP (UniProtKB | ChEBI)
Binding site249ATP (UniProtKB | ChEBI)
Binding site314ATP (UniProtKB | ChEBI)
Binding site386ATP (UniProtKB | ChEBI)

GO annotations

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
    • ORF names
      BWD162_000200

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • WD16.2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Bartonellaceae > Bartonella

Accessions

  • Primary accession
    A0A1S6WS70

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain50-325AAA+ ATPase
Domain328-422Clp ATPase C-terminal

Sequence similarities

Belongs to the ClpX chaperone family. HslU subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    436
  • Mass (Da)
    48,303
  • Last updated
    2017-05-10 v1
  • Checksum
    A4A915935B3E79F5
MCVVFSPRETVSELDRFIIGQKDAKRSVAIALRNRWRRQQLEGQMREEVMPKNILMIGPTGVGKTGIARRLAKLAGAPFVKVEATKFTEVGYVGRDVEQIIRDLVEIAISLVREKKRDEVKAKAHMNAEERVLNALVGKTASPATRDSFRKKLREGELDDKEIEIEVADNSSNGTPTFDIPGMPGAQMGIMNLSDIFGKMGTRTKIRKTTVKDAFKPLIDDESEKLLDQDQIIQEALRVTENDGIVFIDEIDKIATRDGGAGATVSREGVQRDLLPLVEGTTVSTKYGQIKTDHILFIASGAFHVSKPSDLLPELQGRLPIRVELNALTREDLRRILTEPEASLIKQYIALMATEEVHLEITDDAIDALADIAVDLNARIENIGARRLQTVMERVLDEISFTAPDKAGTSFKVDAAYVKQSIGDLAADVDLSRFIL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP019781
EMBL· GenBank· DDBJ
AQX19161.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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