3.4.24.B17: FtsH endopeptidase
This is an abbreviated version!
For detailed information about FtsH endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.B17
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3.4.24.B17
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cushing
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cortisol-producing
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matriptase
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ttsps
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pro-hgf
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prkar1a
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ctnnb1
- 3.4.24.B17
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cushing
-
cortisol-producing
- matriptase
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ttsps
-
pro-hgf
-
prkar1a
-
ctnnb1
Reaction
proteolytic degradation of proteins =
Synonyms
cell division protein ftsH, FtsH, FtsH protease, FTSH_ECOLI, HflB, HlB, M41.001, MtFtsH, T.ftsH
ECTree
3.4.24.B17 FtsH endopeptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.24.B17 - FtsH endopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C229F
ATPase activity is 114% of wild-type activity, protease activity with BODIPY-casein is 47% of wild-type activity, protease activity with Cy3-sigma32 is 22% of wild-type activity
D223K
ATPase activity is 20% of wild-type activity, protease activity with BODIPY-casein is 10% of wild-type activity, protease activity with Cy3-sigma32 is 5% of wild-type activity
D272N
ATPase activity is 97% of wild-type activity, protease activity with BODIPY-casein is 81% of wild-type activity
E226A
ATPase activity is 10% of wild-type activity, protease activity with BODIPY-casein is 11% of wild-type activity
E226K
ATPase activity is less than 5% of wild-type activity, protease activity with BODIPY-casein is 6% of wild-type activity
E226Q
ATPase activity is 20% of wild-type activity, protease activity with BODIPY-casein is 18% of wild-type activity, protease activity with Cy3-sigma32 is 17% of wild-type activity
E273A
ATPase activity is 20% of wild-type activity, protease activity with BODIPY-casein is 8% of wild-type activity, protease activity with Cy3-sigma32 is less than 5% of wild-type activity
E273D
ATPase activity is 143% of wild-type activity, protease activity with BODIPY-casein is 82% of wild-type activity
E273K
ATPase activity is less 5% of wild-type activity, protease activity with BODIPY-casein is 7% of wild-type activity
E273Q
ATPase activity is 68% of wild-type activity, protease activity with BODIPY-casein is 50% of wild-type activity, protease activity with Cy3-sigma32 is 11% of wild-type activity
E415K
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site-directed mutagenesis, mutation of the zinc binding sequence motif, reduced proteolytic activity
F228A
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site-directed point mutation, proteolytically inactive with protein sigma32, but degrades casein, decreased ATPase activity
F228E
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site-directed point mutation, proteolytically inactive mutant, increased ATPase activity
F228K
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site-directed point mutation, proteolytically inactive mutant, highly decreased ATPase activity
G230A
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site-directed point mutation, proteolytically inactive mutant, highly decreased ATPase activity
H271D
ATPase activity is 78% of wild-type activity, protease activity with BODIPY-casein is 39% of wild-type activity, protease activity with Cy3-sigma32 is 20% of wild-type activity
H417A/E418Q/H421A
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the mutant shows 106% ATPase activity compared to the wild type enzyme
K136N
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site-directed mutagenesis, mutation is located in a second ATP binding site, activity is slightly reduced, can complement a deficient mutant strain
K198N
L189W
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mutation ftsH102, partial complementation of temperature sensitivity of the ftsH1 mutant at 42°C but not other cols-sensitive mutants, overview
L567R
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
L574A
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
L574R
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
L581R
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site-directed mutagenesis, mutation in the C-terminal coiled-coil structure, mutant is defective in binding and degradation of sigma32 protein and phage lambda CII protein, no growth of phage lambda
M227K
ATPase activity is 55% of wild-type activity, protease activity with BODIPY-casein is 69% of wild-type activity, protease activity with Cy3-sigma32 is 8% of wild-type activity
S137N
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site-directed mutagenesis, mutation is located in a second ATP binding site, activity is slightly reduced, can complement a deficient mutant strain
T199A
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site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, inactive, no complementation of a deficient mutant strain
T199N
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site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, highly reduced activity, weak complementation of a deficient mutant strain
H417A/E418Q/H421A
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the mutant shows 106% ATPase activity compared to the wild type enzyme
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K198N
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the mutant shows 12% ATPase activity compared to the wild type enzyme
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additional information
K198N
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site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, inactive, no complementation of a deficient mutant strain
K198N
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the mutant shows 12% ATPase activity compared to the wild type enzyme
additional information
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construction of mutants by deletion of N-terminal membrane region, replacement by a leucine-zipper, or replacement by a lactose permease transmembrane segment, the matated proteins show very low remaining activity, but are stimulated by dimethylsulfoxide, the deletion mutant does not show ATPase and proteolytic activity
additional information
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defects in the ftsH gene stabilize the SecY protein, overexpression increase the degradation of SecY, enzyme deficient mutantion ftsH101 suppresses the temperature-sensitive export defect of a secY24 mutant G240D in the cytoplasmic domain of SecY by stabilizing the mutant protein
additional information
enzyme mutant still shows activity with substrates derivative of the N-terminal domain of the lambdacI repressor tagged with cI105 and SsrA
additional information
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enzyme mutation stabilizes the cII and cIII proteins resulting in greater levels of the cI repressor and thus shifting the lytic-lysogeny decision in favor of the lysogeny, lon ftsH double mutant shows 6fold reduced activity with lambda Xis protein, which accumulates and interferes with the integration of lambda
additional information
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mutational amino acid exchange of the self-processing site M640-S641 reveal the preference for positively charged and hydrophobic amino acid residues at this site for proteolytic cleavage
additional information
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mutations cause an abnormal orientation of some model proteins in the plasma membrane, the effect can be supressed by overexpression of molecular-chaperone proteins, deletion of FtsH is lethal
additional information
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several mutant strains harboring mutations in the C-terminal coiled-coil leucine-zipper structure, are defective in binding and degradation of sigma32 protein and the phage lambda CII proteins, the mutations do not interfere with the ATPase activity, the mutants are more sensitive against trypsin digestion than the wild-type and show reduced growth
additional information
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soluble form of the enzyme having only the cytoplasmic C-terminal region is inactive, construction of maltose-binding protein fusion proteins with fusion at 5 different N-termini of the enzyme, i.e. MF1-5, shorter constructs lacking the second transmembrane segment are proteolytically inactive and do not form oligomers, while the longer constructs are similar to the wild-type
