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Literature summary extracted from

  • Makino, S.; Makino, T.; Abe, K.; Hashimoto, J.; Tatsuta, T.; Kitagawa, M.; Mori, H.; Ogura, T.; Fujii, T.; Fushinobu, S.; Wakagi, T.; Matsuzawa, H.; Makinoa, T.
    Second transmembrane segment of FtsH plays a role in its proteolytic activity and homo-oligomerization (1999), FEBS Lett., 460, 554-558.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.B17 expression of maltose-binding fusion proteins in Escherichia coli Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.4.24.B17 additional information 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 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 membrane integral, with the active site in the cytoplasm Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.B17 Zn2+ zinc-dependent protease, binding and active site at the C-terminus 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
-
 K12, strain JM109
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.B17 recombinant soluble fusion proteins, more than 80% homogeneity Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.B17 proteolytic degradation of proteins the second transmembrane segment participates in not only its membrane-anchoring, but also its protease activity and homolgomerization, it is located next to the C-terminal cytoplasmic region of the enzyme Escherichia coli
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.B17 0.014
-
 purified recombinant fusion protein MF5, ATPase activity Escherichia coli
3.4.24.B17 0.055
-
 purified recombinant fusion protein MF4, ATPase activity Escherichia coli
3.4.24.B17 0.056
-
 purified recombinant fusion protein MF3, ATPase activity Escherichia coli
3.4.24.B17 0.07
-
 purified recombinant fusion protein MF2, ATPase activity Escherichia coli
3.4.24.B17 0.122
-
 purified recombinant fusion protein MF1, ATPase activity Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 protein + H2O
-
 Escherichia coli peptides
-
 ?
3.4.24.B17 protein sigma32 + H2O wild-type enzyme and fusion mutants MF1-4, not MF5, substrate protein is a heat-shock transcription factor, sigma32-C-his Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.B17 More enzyme consists of a membrane-anchoring region of amino acids 1-123 in the N-terminus, and a cytoplasmic region of amino acids 124-647 in the C-terminus, enzyme forms homooligomers Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
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 42
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.B17 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.24.B17 ATP dependent on, ATPase activity in the C-terminus Escherichia coli