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Literature summary for 3.4.24.B17 extracted from

  • Akiyama, Y.; Kihara, A.; Tokuda, H.; Ito, K.
    FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins (1996), J. Biol. Chem., 271, 31196-31201.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutants as His-Myc-tagged proteins Escherichia coli

Protein Variants

Protein Variants Comment Organism
E415K site-directed mutagenesis, mutation of the zinc binding sequence motif, reduced proteolytic activity Escherichia coli
K136N site-directed mutagenesis, mutation is located in a second ATP binding site, activity is slightly reduced, can complement a deficient mutant strain Escherichia coli
K198N site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, inactive, no complementation of a deficient mutant strain Escherichia coli
S137N site-directed mutagenesis, mutation is located in a second ATP binding site, activity is slightly reduced, can complement a deficient mutant strain Escherichia coli
T199A site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, inactive, no complementation of a deficient mutant strain Escherichia coli
T199N site-directed mutagenesis, mutation is located in the C-terminal ATP binding site, highly reduced activity, weak complementation of a deficient mutant strain Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc metalloprotease, essential zinc binding sequence motif HEXXH at the cytoplasmic domain Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protein + H2O Escherichia coli involved in membrane protein assembly as well as degradation of unstable proteins peptides
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-Myc-tagged wild-type and mutants Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein + H2O
-
Escherichia coli peptides
-
?
protein + H2O involved in membrane protein assembly as well as degradation of unstable proteins Escherichia coli peptides
-
?
protein SecY + H2O substrate protein is a subunit of protein translocase, failed to assemble with its partner SecE Escherichia coli ?
-
?
subunit a of F0 + H2O F0 part of the proton ATPase Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
FtsH
-
Escherichia coli
HlB
-
Escherichia coli
M41.001 Merops-ID Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
42
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, 2 ATP binding consensus sequences, 1 is located at the C-terminus and is essential for proteolytic activity Escherichia coli
CTP ineffective substitute for ATP, low activity Escherichia coli
UTP ineffective substitute for ATP, low activity Escherichia coli