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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B17 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

EC Number Protein Variants Comment Organism
3.4.24.B17 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
3.4.24.B17 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
3.4.24.B17 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
3.4.24.B17 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
3.4.24.B17 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 cytoplasmic membrane
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Zn2+ metalloprotease Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.24.B17 protein + H2O Escherichia coli
-
 peptides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B17 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B17 coiled-coil C-terminus, residues 541-585, as His-tagged peptide Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 CII protein of phage lambda + H2O
-
 Escherichia coli ?
-
 ?
3.4.24.B17 protein + H2O
-
 Escherichia coli peptides
-
 ?
3.4.24.B17 sigma32 + H2O
-
 Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 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

EC Number Synonyms Comment Organism
3.4.24.B17 FtsH
-
 Escherichia coli
3.4.24.B17 HflB
-
 Escherichia coli
3.4.24.B17 M41.001 Merops-ID Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.B17 22
-
 assay at, ambient temperature Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B17 7.4
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 ATP dependent on Escherichia coli