Literature summary for 3.4.24.B17 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.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of maltose-binding fusion proteins in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
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

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

Metals/Ions

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

Purification (Commentary)

Purification (Comment)	Organism
recombinant soluble fusion proteins, more than 80% homogeneity	Escherichia coli

Reaction

Reaction	Comment	Organism	Reaction ID
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]

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

Substrates and Products (Substrate)

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

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
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
8	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	dependent on, ATPase activity in the C-terminus	Escherichia coli

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Release 2023.1 (January 2023)