Member database | HAMAP |
HAMAP type | family |
Short name | HslV |
Description Imported from IPR022281
ATP-dependent protease complexes are present in all three kingdoms of life, where they rid the cell of misfolded or damaged proteins and control the level of certain regulatory proteins. They include the proteasome in Eukaryotes, Archaea, and Actinomycetales and the HslVU (ClpQY, clpXP) complex in other eubacteria. Genes homologues to eubacterial HslU (ClpY, clpX) have also been demonstrated in to be present in the genome of trypanosomatid protozoa
[3].
The prokaryotic ATP-dependent proteasome is coded for by the heat-shock locus VU (HslVU). It consists of HslV, a peptidase, and HslU (
IPR004491), the ATPase and chaperone belonging to the AAA/Clp/Hsp100 family. The crystal structure of Thermotoga maritima HslV has been determined to 2.1-A resolution. The structure of the dodecameric enzyme is well conserved compared to those from Escherichia coli and Haemophilus influenzae
[2, 1].
This entry represents the HslV peptidase subunit of the ATP-depdendent HSIVU protease complex found in bacteria and some lower eukaryotes.
References Imported from IPR022281
1.Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. Kwon AR, Kessler BM, Overkleeft HS, McKay DB. J. Mol. Biol. 330, 185-95, (2003). View articlePMID: 12823960
2.Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R. Biophys. Chem. 100, 437-52, (2003). View articlePMID: 12646382
3.Eubacterial HslV and HslU subunits homologs in primordial eukaryotes. Couvreur B, Wattiez R, Bollen A, Falmagne P, Le Ray D, Dujardin JC. Mol. Biol. Evol. 19, 2110-7, (2002). View articlePMID: 12446803
Integrated to
External Links
Representative structure
1jjw: Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution