HslUV protease complex

Definition

Target type: cellularcomponent

A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. [GOC:bhm, PMID:12670962, UniProt:P0A6H5]

The HslUV protease complex is a multi-subunit ATP-dependent protease that plays a crucial role in protein quality control in bacteria. It is composed of two distinct subunits: HslU and HslV.

HslU is a hexameric ring-shaped ATPase that functions as a "chaperone" component. It binds to unfolded or misfolded proteins and uses the energy from ATP hydrolysis to unfold them. The HslU hexamer has a central channel that allows the unfolded protein to pass through.

HslV is a tetradecamer (14 subunits) that forms a cylindrical chamber containing the active sites of the protease. This chamber is the catalytic core of the complex where the degradation of unfolded proteins occurs. The HslV cylinder has two distinct domains: an N-terminal domain that forms the proteolytic chamber and a C-terminal domain that interacts with the HslU ring.

The HslU and HslV subunits form a complex through their C-terminal domains. HslU serves as a "gatekeeper" for the HslV chamber, controlling the entry of unfolded proteins. Once inside the HslV chamber, the unfolded protein is degraded by the active sites of the protease. The HslU and HslV subunits work together to ensure that only unfolded or misfolded proteins are degraded, while preventing the degradation of functional proteins.

The cellular component of the HslUV protease complex is primarily located in the cytoplasm of bacteria. It is an integral part of the protein quality control machinery, ensuring that only properly folded proteins are present within the cell. The complex is also involved in various cellular processes, such as stress response, regulation of gene expression, and bacterial pathogenesis.

In summary, the HslUV protease complex is a multi-subunit protein complex located in the cytoplasm of bacteria. It is composed of HslU and HslV subunits, which function as a chaperone and a proteolytic chamber, respectively. The complex plays a crucial role in protein quality control by degrading unfolded or misfolded proteins, thus ensuring the proper functioning of the cell.'
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Proteins (1)

Compounds (2)