EC Number   |
General Information |
Reference |
|---|
   3.4.25.2 | evolution |
Escherichia coli HslUV protease is a member of a major family of ATP-dependent AAA+ degradation machines |
720248 |
| 3.4.25.2 | malfunction |
depletion of HslUV leads to an increase in the number of kinetoplasts which undergo abnormal segregation, causing the appearance of giant kinetoplasts as a result of the overreplication of minicircle DNA |
734572 |
| 3.4.25.2 | more |
ClpYQ or HslUV is a two-component ATP-dependent protease composed of ClpY or HslU, an ATPase with unfolding activity, and ClpQ or HslV, a peptidase. In the ClpYQ proteolytic complex, the hexameric rings of ClpY (HslU) are responsible for protein recognition, unfolding, and translocation into the proteolytic inner chamber of the dodecameric ClpQ (HslV). The highly conserved sequence GYVG, residues 90 to 93, pore I site, along with the GESSG pore II site, residues 265 to 269, contribute to the central pore of ClpY in domain N. These two central loops of ClpY are in the center of its hexameric ring in which the energy of ATP hydrolysis allows substrate translocation and then degradation by ClpQ. The pore I site of ClpY has an effect on the adjoining structural region in protein substrates, and the pore I site is essential for the translocation of substrates. The pore II site also interfaces with nearby regions in the substrates but is not necessary for their translocation. An ATP-binding site in domain N, separate from its role in polypeptide, ClpY, oligomerization, is required for complex formation with ClpQ. Tyr408 in ClpY, like residue 385 in ClpX, is necessary for self-oligomerization, and this activity is likely important for in vivo protein-subunit stability |
719731 |
| 3.4.25.2 | more |
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV |
-, 719424 |
| 3.4.25.2 | more |
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, does not influence the co-expression level of HslV and proteasome 20 in strain Be-78 |
-, 719424 |
| 3.4.25.2 | more |
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Be-62 |
-, 719424 |
| 3.4.25.2 | more |
the enzyme is part of the HslVU enzyme complex, HslVU is an ATP-dependent protease consisting of two multimeric components: the HslU ATPase and the HslV peptidase, interaction between HslU and HslV. PSI, a classical proteasome inhibitor, influences the co-expression level of HslV and proteasome 20 in strain Y |
-, 719424 |
| 3.4.25.2 | physiological function |
constrction of subunit HslU pseudohexamers containing mixtures of ATPase active and inactive subunits at defined positions in the hexameric ring. Genetic tethering impairs subunit HslV binding and degradation, even for pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defects. Pseudohexamers containing different patterns of hydrolytically active and inactive subunits retain the ability to unfold protein substrates and/or collaborate with HslV in their degradation |
754155 |
| 3.4.25.2 | physiological function |
HslUV is involved in DNA replication and transcription |
734572 |
| 3.4.25.2 | physiological function |
HslV is essential for Leishmania donovani viability |
-, 734007 |
