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The heat shock proteins HslV and HslU (HslVU complex; also known as ClpQ and ClpY respectively, or ClpQY) are expressed in many bacteria such as E. coli in response to cell stress. The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, consisting of an hslV dodecamer bound to an hslU hexamer, with a central pore in which the protease and ATPase active sites reside. The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. HslV is thought to resemble the hypothetical ancestor of the proteasome, a large protein complex specialized for regulated degradation of unneeded proteins in eukaryotes, many archaea, and a few bacteria. HslV bears high similarity to core su

AttributesValues
rdf:type
rdfs:label
  • HslVU (en)
  • HslVU (ru)
rdfs:comment
  • HslVU (HslUV, ClpYQ) — протеаза из группы АТФ-зависимых протеаз, присутствующая у многих бактерий, включая Escherichii coli и Bacillus subtilis. Состоит из двух компонентов, HslU (ClpY) — АТФ-зависимый шаперон и активатор протеолитической активности у HslV (ClpQ) — собственно протеазы. Активный комплекс состоит из двух колец из шести белковых субъединиц HslV, соединённых вместе, и по кольцу из шести белковых субъединиц HslU с каждой стороны. Кольца соединены вместе, образуя полый цилиндр, при этом кольца HslU находятся со внешней стороны. Как и у всех других АТФ-зависимых протеаз, активный сайт находится внутри цилиндра, и полипептидный субстрат должен быть развёрнут и активно перемещён внутрь для того, чтобы произошел протеолиз,,,. (ru)
  • The heat shock proteins HslV and HslU (HslVU complex; also known as ClpQ and ClpY respectively, or ClpQY) are expressed in many bacteria such as E. coli in response to cell stress. The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, consisting of an hslV dodecamer bound to an hslU hexamer, with a central pore in which the protease and ATPase active sites reside. The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. HslV is thought to resemble the hypothetical ancestor of the proteasome, a large protein complex specialized for regulated degradation of unneeded proteins in eukaryotes, many archaea, and a few bacteria. HslV bears high similarity to core su (en)
foaf:name
  • HslU—HslV peptidase (en)
name
  • ATP-dependent protease, HslV subunit (en)
  • Heat shock protein HslU (en)
  • HslU—HslV peptidase (en)
foaf:depiction
  • http://commons.wikimedia.org/wiki/Special:FilePath/Hslvu_ecoli.png
dcterms:subject
Wikipage page ID
Wikipage revision ID
Link from a Wikipage to another Wikipage
sameAs
dbp:wikiPageUsesTemplate
thumbnail
caption
  • Top view of the hslV/hslU complex isolated from E. coli . (en)
EC number
InterPro
  • IPR004491 (en)
  • IPR022281 (en)
IUBMB EC number
symbol
  • HslU (en)
  • HslV (en)
has abstract
  • The heat shock proteins HslV and HslU (HslVU complex; also known as ClpQ and ClpY respectively, or ClpQY) are expressed in many bacteria such as E. coli in response to cell stress. The hslV protein is a protease and the hslU protein is an ATPase; the two form a symmetric assembly of four stacked rings, consisting of an hslV dodecamer bound to an hslU hexamer, with a central pore in which the protease and ATPase active sites reside. The hslV protein degrades unneeded or damaged proteins only when in complex with the hslU protein in the ATP-bound state. HslV is thought to resemble the hypothetical ancestor of the proteasome, a large protein complex specialized for regulated degradation of unneeded proteins in eukaryotes, many archaea, and a few bacteria. HslV bears high similarity to core subunits of proteasomes. (en)
  • HslVU (HslUV, ClpYQ) — протеаза из группы АТФ-зависимых протеаз, присутствующая у многих бактерий, включая Escherichii coli и Bacillus subtilis. Состоит из двух компонентов, HslU (ClpY) — АТФ-зависимый шаперон и активатор протеолитической активности у HslV (ClpQ) — собственно протеазы. Активный комплекс состоит из двух колец из шести белковых субъединиц HslV, соединённых вместе, и по кольцу из шести белковых субъединиц HslU с каждой стороны. Кольца соединены вместе, образуя полый цилиндр, при этом кольца HslU находятся со внешней стороны. Как и у всех других АТФ-зависимых протеаз, активный сайт находится внутри цилиндра, и полипептидный субстрат должен быть развёрнут и активно перемещён внутрь для того, чтобы произошел протеолиз,,,. (ru)
PIRSF
  • PIRSF039093 (en)
prov:wasDerivedFrom
page length (characters) of wiki page
EC number
  • 3.4.25.2
foaf:isPrimaryTopicOf
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