3.4.24.B20: FtsH protease
This is an abbreviated version!
For detailed information about FtsH protease, go to the full flat file.
Word Map on EC 3.4.24.B20
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3.4.24.B20
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chloroplast
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photosystem
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thylakoids
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variegation
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photodamaged
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photoinhibition
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sigma32
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ftsh-mediated
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rpoh
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grana
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lpxc
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photoinhibitory
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ftsh-dependent
- 3.4.24.B20
- chloroplast
-
photosystem
- thylakoids
-
variegation
-
photodamaged
-
photoinhibition
- sigma32
-
ftsh-mediated
- rpoh
-
grana
- lpxc
-
photoinhibitory
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ftsh-dependent
Reaction
degradative cleavage of proteins =
Synonyms
AAA protease, AtFtsH, AtFtsH2, AtFtsH5, AtFtsH6, ATP-dependent zinc metalloprotease, filamentation temperature sensitive H, filamentation temperature sensitive H protease, FtsH, FtsH (slr0228), FtsH metalloprotease, FtsH protease, FtsH protease slr0228, FtsH1, FtsH10, FtsH11, FtsH12, FtsH2, FtsH2 protease, FtsH3, FtsH4, FtsH5, FtsH6, FtsH7, FtsH8, FtsH9, FTSHA, FtsHB, HflB, M41.005, More, putative cell division protein, RISP-degrading activity, slr0228, VAR1, VAR2, zinc dependent protease, ZmFtsH2A, ZmFtsH2B
ECTree
3.4.24.B20 FtsH proteaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.B20 - FtsH protease
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
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-
?
Fur repressor protein + H2O
?
degraded by the FtsH1/FtsH3 complex
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-
?
lambdaCII + H2O
?
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the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
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-
?
light-harvesting complex II + H2O
?
-
AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
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-
?
Rieske FeS protein + H2O
?
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degradation of membrane protein, essentially required as a membrane-integrated quality control
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?
RpoH + H2O
?
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RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
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-
?
Spo0E + H2O
?
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the Spo0E phosphatase is distinguished from the YisI and YnzD phosphatases by a C-terminal extension of about 25 amino acids, the C-terminal region of Spo0E confers target specificity to FtsH
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-
?
23 kDa fragment of photosystem II D1 protein + H2O
?
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enzyme is required for protection against photoinhibition and induction of repair of photosystem II D1 protein, degradation of irreversible damaged D1 protein in form of the 23 kDa fragment
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?
23 kDa fragment of photosystem II D1 protein + H2O
?
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degradation, irreversibly damaged substrate by reactive oxygen species formed in the light
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?
D1 protein + H2O
?
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FtsH protease is responsible for the primary cleavage of the D1 protein under moderate heat stress conditions
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?
D1 protein + H2O
?
isoform FtsH2 is involved in selective D1 protein degradation during photosystem II repair
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?
D1 protein + H2O
?
substrate for isoform FtsH2
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?
damaged PSII D1 protein + H2O
?
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-
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?
photodamaged D1 protein + H2O
?
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the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
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?
photodamaged D1 protein + H2O
?
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the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
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?
photodamaged D1 protein + H2O
?
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the enzyme produces a 23000 Da N-terminal and a 9000 Da C-terminal fragment
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?
photodamaged D1 protein + H2O
?
degradation, part of photosystem 2 repair
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?
Protein + H2O
?
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FtsH is involved in the degradation of unassembled proteins, the repair of photosystem II from photoinhibition, and the formation of thylakoids
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?
Protein + H2O
?
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FtsH11 protease plays a critical role in Arabidopsis thermotolerance. FtsH11 constitutively protects the photosynthesis apparatus from the damage caused by elevated temperatures
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?
Protein + H2O
?
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thylakoid FtsH protease is involved in the degradation of unassembled proteins, and in the turnover of the D1 protein of the PSII reaction center in the context of its repair from photoinhibition. FtsH proteases are involved in the formation of thylakoids
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?
Protein + H2O
?
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FtsH (slr0228) plays an important role in controlling the removal of unassembled PSII subunits from the thylakoid membrane
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?
Protein + H2O
?
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FtsH mediates repair of the photosystem II complex in response to light stress
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?
protein + H2O
peptides
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degradation of membrane proteins, essentially required as a membrane-integrated quality control
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?
protein + H2O
peptides
degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
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?
protein + H2O
peptides
enzyme is involved in chloroplast biogenesis
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?
protein + H2O
peptides
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degradation of unassembled proteins, apoproteins lacking their prostethic groups or pigments, photo-or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
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?
protein + H2O
peptides
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degradation of unassembled proteins, apoproteins lacking their prosthetic groups or pigments, photo- or otherwise damaged proteins, and of developmentally or environmentally regulated proteins
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?
protein D1 + H2O
?
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FtsH (slr0228) is required for selective D1 turnover during photosystem II repair
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?
protein D1 + H2O
?
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FtsH protease plays an essential role in the turnover of the reaction center D1 protein in Synechocystis PCC 6803 under heat stress as well as light stress conditions
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?
RNase colicin D + H2O
?
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the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
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?
RNase colicin D + H2O
?
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the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
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-
?
additional information
?
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the D1 protein, a core subunit of the PSII reaction enter, is a substrate for FtsH protease
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?
additional information
?
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fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
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?
additional information
?
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the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
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?
additional information
?
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the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
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?
additional information
?
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the D1 processing mutants, D1-S345P and DELTACtpA, are unable to assemble a functional CaMn4 cluster
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?
