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
-
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
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General Information
General Information on EC 3.4.24.B20 - FtsH protease
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evolution
malfunction
metabolism
physiological function
additional information
FtsH gene multiplication is of adaptive value during the course of evolution of oxygenic photosynthesis
evolution
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the mode of action of FtsH proteases seems to be different between cyanobacteria and higher plants
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mutants lacking isoforms FtsH2 and FtsH5 are characterized by a typical leaf-variegated phenotype
malfunction
a mutant conditionally depleted in FtsH3 is unable to induce normal expression of the IsiA chlorophyll-protein and FutA1 iron transporter upon iron deficiency due to a block in transcription, which is regulated by the Fur transcriptional repressor
malfunction
a mutant depleted in isoform FtsH3 displays impaired protein D1 degradation
malfunction
A stabilizing effect on Fur is observed in a mutant conditionally depleted in the FtsH1 subunit
malfunction
the ftsh1-1 mutation Increases photosystem II sensitivity to photoinhibition, prevents photosystem II repair, and leads to the accumulation of D1 protein fragments
malfunction
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the loss of isoform FtsH4 regulates Arabidopsis development and architecture by mediating the peroxidase-dependent interplay between hydrogen peroxide and auxin homeostasis
metabolism
enzyme regulation, overview
metabolism
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FtsH cellular functions and regulation involving several factors, overview
metabolism
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FtsH5/VAR1, FtsH2/VAR2, VAR3 and THF1 control leaf variegation in Arabidopsis thaliana
metabolism
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the thylakoid located FtsH complex in Arabidopsis is responsible for degradation of photodamaged D1 protein in concert with lumenal Deg proteases
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Chloroplast development promoted by the ectopic expression of cGPA1 is dependent on FtsH complexes. FtsH complexes, which are composed of type-A (FtsH1/FtsH5) and type-B (FtsH2/FtsH8) subunits, are required for cGPA1-promoted chloroplast development in the leaf-variegated mutant thylakoid formation 1, thf1, overview
physiological function
filamentation temperature-sensitive H, FtsH, is a membrane-anchored ATP-dependent metalloprotease
physiological function
FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber
physiological function
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FtsH has both chaperone and protease activities, and it is a crucial element in protein quality control, involving a number of substrates and processes, including the degradation of unneeded and damaged membrane proteins as well as soluble signaling factors
physiological function
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FtsH has to degrade or to regulate the steady-state level of one or more proteins that interfere with successful sporulation. In the absence of the ATP-dependent metalloprotease FtsH, the sporulation frequency of Bacillus subtilis cells is reduced by several orders of magnitude
physiological function
FtsH is a membrane-bound protein essential for the cell viability in Escherichia coli
physiological function
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FtsH is a peculiar prokaryotic protease with low unfoldase activity. FtsH takes care of degrading unstable or inappropriately assembled proteins
physiological function
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FtsH is an essential membrane-bound protease that degrades integral membrane proteins as well as cytoplasmic proteins. FtsH is a stress-response protein that promotes the pathogen's ability to deal with reactive oxygen intermediates stress and is possibly involved in the regulation of FtsZ levels. Optimal intracellular levels of the essential cell-division protein FtsZ are critical for cell division and viability, overview
physiological function
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FtsH is the only known membrane-anchored AAA protease in bacteria that fulfills a variety of regulatory functions. FtsH-mediated regulation of LpxC levels by proteolysis crucial for cell viability. FtsH is involved in the quality control of misfolded or incorrectly inserted membrane proteins and acts either as a chaperone to help them refold or degrades them. Another important function of FtsH in Escherichia coli is control of heat shock gene expression, overview
physiological function
in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins
physiological function
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in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins. slr0228 is involved in the early steps of D1 degradation and also plays a role in the removal of other damaged or unassembled thylakoid proteins
physiological function
in chloroplasts, the most clearly defined function of FtsH is in photosystem II, PSII, repair, where it degrades photooxidatively damaged D1 proteins. The AtFtsH6 isoform degrades the light-harvesting complex of PSII, LHCII, under conditions of high light and senescence
physiological function
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the ATP-dependent metalloprotease FtsH is involved in the degradation of the photo- or heat-damaged D1 protein. Damage occurs in the reaction center-binding D1 protein understrong visible light and heat stress, overview
physiological function
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the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
the ATP-dependent zinc metallopeptidase is a cell division protein
physiological function
the ATP-dependent zinc metallopeptidase is a cell division protein. FtsH2 and FtsH5 are responsible for leaf variegation and proteolysis of photodamaged D1 protein in Arabidopsis
physiological function
the ATP-dependent zinc metallopeptidase is involved in the degradation of both Lhcb3 and Lhcb1 during senescence and high-light acclimation
physiological function
the ATP-dependent zinc metallopeptidase is involved in the repair of PSII following damage incurred during photoinhibition. FtsH2 and FtsH5 are responsible for leaf variegation and proteolysis of photodamaged D1 protein in Arabidopsis
physiological function
the FtsH2 protease plays a key role in the degradation of both precursor and mature forms of D1 following donor-side photoinhibition, and in the selective degradation of photodamaged D1 protein and incompletely processed forms of the D1 protein during the repair of photosystem II in the cyanobacterium, overview. The FtsH2 protease participates in fast D1 replacement in the psbO deletion strain
physiological function
VAR2, a subunit of the chloroplast FtsH complex, is involved in turnover of the photosystem II reaction center D1 protein, as well as in other processes required for the development and maintenance of the photosynthetic apparatus
physiological function
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FtsH is necessary for the processing of colicinsDand E3 during their import
physiological function
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interplay between N-terminal methionine excision and FtsH protease is essential for normal chloroplast development and function. The N-terminally processed D1 and D2 polypeptide chains are primarily degraded by the FtsH complex, which ensures their quality control
physiological function
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part of the FtsH hexamers are juxtapositioned to PSII complexes in the grana in darkness, carrying out immediate degradation of the photodamaged D1 protein under light stress
physiological function
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the heteromeric FtsH complex is important for maintaining thylakoid membranes
physiological function
FtsH is involved in quality control and the regulation of accumulation of cytochrome b6f complexes and complex C subunit B proteins. The enzyme regulates the degradation of photosystem II upon photoinhibition and phosphorus and sulfur starvation
physiological function
FtsH metalloproteases are key components of the photosystem II repair cycle which operates to maintain photosynthetic activity in the light. isoforms FtsH1 and FtsH3 are required for cell viability, whereas FtsH2 and FtsH4 are dispensable. isoform FtsH3 is more important than FtsH2 for cell viability
physiological function
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FtsH1 is a regulatory protein for organelle biogenesis in Plasmodium falciparum
physiological function
isoform FtsH2 is involved in the repair of photosystem II within the thylakoid membranes
physiological function
the FtsH1 protease is involved in the acclimation of cells to iron deficiency
physiological function
the FtsH2/FtsH3 complex is involved in photoprotection
physiological function
the FtsH2/FtsH3 complex is involved in photoprotection. The FtsH3 protease is involved in the acclimation of cells to iron deficiency
physiological function
Q7V1V9; Q7V362
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA
physiological function
comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA. MIT 9313 has less of the FtsH protease
physiological function
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deletion mutants of isoform FtsH1 display a severe growth retardation both in LB and M63 medium. The lag phase is extended from 6 to 8 h and retardation of growth at the second phase of the biphasic growth curve leads to a 1.5 h longer doubling time in the FtsH1 FtsH2 double mutant compared to the FtsH1 mutant. The FtsH2 mutant does not show a pronounced growth retardation phenotype. Deletion of FtsH1, but not FtsH2 moderately enhances sensitivity to a lethal heat shock. Deletion of FtsH1 causes a 13% reduction in swimming motility, which is 38% reduction the FtsH1 FtsH2 double deletion background. The FtsH1 mutant forms an undifferentiated flat biofilm. The FtsH1 FtsH2 double mutant forms dense irregular biofilm structures anchored to the substratum at a few contact points
physiological function
FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction
physiological function
initiation of singlet oxygen signaling in grana margins depends on EX1 and the ATP-dependent zinc metalloprotease FtsH. FtsH cleaves also the D1 protein during the disassembly of damaged PSII, EX1-and singlet oxygen-mediated may be spatially but also functionally associated with the repair of PSII
physiological function
mutation of FtsH11 gene causes significant decreases in photosynthetic efficiency of photosystems when environmental temperature raises above optimal. Under moderately high temperatures, the FtsH11 mutant shows significant decreases in electron transfer rates of photosystem II (PSII) and photosystem I (PSI), decreases in photosynthetic capabilities of PSII and PSI, increases in non-photochemical quenching, and a host of other chlorophyll fluorescence parameter changes. For plants grown under normal temperature and subjected to the high light treatment, no significant difference in chlorophyll fluorescence parameters is found between the FtsH11 mutant and Col-0 WT plants
physiological function
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phylogenetic analysis of over 6000 FtsH protease sequences. The FtsH proteases involved in PSII repair form a distinct clade branching out before the divergence of FtsH proteases found in all groups of anoxygenic phototrophic bacteria. The phylogenetic tree of FtsH proteases in phototrophic bacteria is similar to that for Type I and Type II reaction centre proteins
physiological function
protein Psb29a minor component of His-tagged photosystem II preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero-oligomeric complex involved in photosystem II repair. In a Psb29 null mutant, levels of FtsH2 and FtsH3 are substantially decreased
physiological function
the proteolytic activity, and not only the ATPase one, is essential for conferring thermotolerance to the plants. FTSH11 interacts with different components of the CPN60 chaperonin. CPN60s as well as a number of envelope, stroma and thylakoid proteins are found associated with proteolytically inactive FTSH11. In a knockout strain, protein TIC40 is highly stabilized. The nucleotide antiporter PAPST2, the fatty acid binding protein FAP1 and the chaperone HSP70 are trapped in an affinity enrichment assay
physiological function
A8IL08; A8J6C7
upon high light exposure, the FtsH1 and FtsH2 and subunits display a shorter half-life, which is counterbalanced by an increase in FTSH1/2 mRNA levels, resulting in modest upregulation of FtsH1/2 proteins. High light increases the protease activity through a redox-controlled reduction of intermolecular disulfide bridges. In a FTSH1 promoter-deficient mutant, the abundance of FtsH1 and FtsH2 proteins are loosely coupled (decreased by 70% and 30%, respectively) with no formation of large and stable homo-oligomers. High light tolerance is tightly correlated with the abundance of the FtsH protease
physiological function
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filamentation temperature-sensitive H, FtsH, is a membrane-anchored ATP-dependent metalloprotease
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physiological function
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comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA. MIT 9313 has less of the FtsH protease
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physiological function
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comparison of the low light, high nutrient strain Prochlorococcus marinus MIT 9313, the high light, low nutrient Prochlorococcus marinus MED 4, and the high light, high nutrient marine Synechococcus strain WH 8102, under low and high growth light levels. The strains differ significantly in their rates of photosystem II repair under high light and in their capacity to remove the PsbA protein as the first step in the photosystem II repair process. All strains remove the PsbD subunit at the same rate that they remove PsbA. When grown under low light, MIT 9313 loses active photosystem II quickly when shifted to high light, but has no measurable capacity to remove PsbA. MED 4 and WH 8102 show less rapid loss of photosystem II and considerable capacity to remove PsbA
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physiological function
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FtsH is a highly dynamic protease undergoing sequential transitions between five conformational states on the second timescale. Addition of ATP does not influence the number of states or change the timescale of domain motions but affects the state occupancy distribution leading to an interdomain compaction
-
physiological function
-
FtsH is an essential membrane-bound protease that degrades integral membrane proteins as well as cytoplasmic proteins. FtsH is a stress-response protein that promotes the pathogen's ability to deal with reactive oxygen intermediates stress and is possibly involved in the regulation of FtsZ levels. Optimal intracellular levels of the essential cell-division protein FtsZ are critical for cell division and viability, overview
-
physiological function
-
FtsH is necessary for the processing of colicinsDand E3 during their import
-
physiological function
-
deletion mutants of isoform FtsH1 display a severe growth retardation both in LB and M63 medium. The lag phase is extended from 6 to 8 h and retardation of growth at the second phase of the biphasic growth curve leads to a 1.5 h longer doubling time in the FtsH1 FtsH2 double mutant compared to the FtsH1 mutant. The FtsH2 mutant does not show a pronounced growth retardation phenotype. Deletion of FtsH1, but not FtsH2 moderately enhances sensitivity to a lethal heat shock. Deletion of FtsH1 causes a 13% reduction in swimming motility, which is 38% reduction the FtsH1 FtsH2 double deletion background. The FtsH1 mutant forms an undifferentiated flat biofilm. The FtsH1 FtsH2 double mutant forms dense irregular biofilm structures anchored to the substratum at a few contact points
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ftsH interferes with the expression or activity of phosphatases RapA, RapB, RapE and Spo0E, and interferes with the phosphorylation status of Spo0A through Spo0E
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation
additional information
mechanisms of variegation suppression, including an unexpected link between var2 variegation and chloroplast translation