V6M3Y3 · V6M3Y3_9BACL

Function

function

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
Type
IDPosition(s)Description
Active site7
Binding site164Na+ (UniProtKB | ChEBI)
Binding site167Na+ (UniProtKB | ChEBI)
Binding site170Na+ (UniProtKB | ChEBI)

GO annotations

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
      T458_16475

Organism names

Accessions

  • Primary accession
    V6M3Y3

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

Sequence similarities

Belongs to the peptidase T1B family. HslV subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    180
  • Mass (Da)
    19,597
  • Last updated
    2014-02-19 v1
  • Checksum
    F0DF2521C85B868A
MEQFHATTIFAVHHNGSVAMAGDGQVTFGQSTVMKHGAKKVRRLYRGEVLAGFAGSVADAITLFEKFEGKLEEYHGNLQRAAVELTKEWRMDKVLRRLEAMMIVVNKEHILLLSGNGEIIEPDDGILAIGSGGSFALAAGRALKKYAPHLSAREIAEASLHTAADICVFTNHNLVVDELN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AYJU01000017
EMBL· GenBank· DDBJ
EST52570.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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