Literature summary for 3.4.24.B17 extracted from

Shotland, Y.; Teff, D.; Koby, S.; Kobiler, O.; Oppenheim, A.B.
Characterization of a conserved alpha-helical, coiled-coil motif at the C-terminal domain of the ATP-dependent FtsH (HflB) protease of Escherichia coli (2000), J. Mol. Biol., 299, 953-964.

Search for more literature for 3.4.24.B17

Cloned(Commentary)

Cloned (Comment)	Organism
expression of GST-wild-type enzyme fusion protein, expression of coiled-coil structure mutant enzymes, expression of coiled-coil C-terminus, residues 541-585, as His-tagged peptide	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
L567R	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	Escherichia coli
L574A	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	Escherichia coli
L574R	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	Escherichia coli
L581R	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	Escherichia coli
additional information	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	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytoplasmic membrane	-	Escherichia coli	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	metalloprotease	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
protein + H2O	Escherichia coli	-	peptides	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
coiled-coil C-terminus, residues 541-585, as His-tagged peptide	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CII protein of phage lambda + H2O	-	Escherichia coli	?	-	?
protein + H2O	-	Escherichia coli	peptides	-	?
sigma32 + H2O	-	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
More	C-terminal region of the enzyme, residues 541-585, forms a coiled-coil, leucine-zipper structure, three of the leucine residues are essential	Escherichia coli

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at, ambient temperature	Escherichia coli

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
ATP	dependent on	Escherichia coli

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Release 2023.1 (January 2023)