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Information on EC 3.4.24.B17 - FtsH endopeptidase and Organism(s) Thermus thermophilus and UniProt Accession Q5SI82

for references in articles please use BRENDA:EC3.4.24.B17
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.B17 FtsH endopeptidase
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SI82
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
proteolytic degradation of proteins
Synonyms
t.ftsh, mtftsh, cell division protein ftsh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M41.001
Merops-ID
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
show the reaction diagram
soluble C-terminal domain harbors the ATPase and protease activity, the N-terminal domain permits the indispensible membrane integration of the enzyme, cleavage of small peptides from the C-terminal side of hydrophobic residues, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
CAS REGISTRY NUMBER
COMMENTARY hide
171904-23-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
largely unfolded alpha-lactalbumin + H2O
peptides
show the reaction diagram
no activity with the native protein, cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates
between 10 and 30 kDa, no large intermediates
?
protein + H2O
peptides
show the reaction diagram
unfolded alpha-casein + H2O
peptides
show the reaction diagram
-
between 10 and 30 kDa, no large intermediates
?
unfolded pepsin + H2O
peptides
show the reaction diagram
cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates
between 10 and 30 kDa, no large intermediates
?
protein D1 + H2O
?
show the reaction diagram
-
-
-
-
?
protein D2 + H2O
?
show the reaction diagram
-
-
-
-
?
protein F0a + H2O
?
show the reaction diagram
-
-
-
-
?
protein GgpS + H2O
?
show the reaction diagram
-
-
-
-
?
protein GlnK + H2O
?
show the reaction diagram
-
-
-
-
?
protein KdtA + H2O
?
show the reaction diagram
-
-
-
-
?
protein LpxC + H2O
?
show the reaction diagram
-
-
-
-
?
protein MgtC + H2O
?
show the reaction diagram
-
-
-
-
?
protein RpoH + H2O
?
show the reaction diagram
-
-
-
-
?
protein SecY + H2O
?
show the reaction diagram
-
-
-
-
?
protein YccA + H2O
?
show the reaction diagram
-
-
-
-
?
superoxide response protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protein + H2O
peptides
show the reaction diagram
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CTP
can substitute for ATP by 74%
GTP
can substitute for ATP by 19%
additional information
no activity with TTP, UTP, AMP, and ADP
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
dependent on
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
strong, complete inhibition at equimolar amounts to ATP
o-phenanthroline
chelator for divalent metal ions
additional information
no inhibition by AMP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-casein
temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess
-
Pepsin
temperature-independent, native protein is slightly, the unfolded protein stimulatory to a higher extent, maximal at 50fold excess
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
ATP
recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
ATPase activity, recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36 - 70
5% of maximal activity at 36°C, 17% of maximal activity at 50°C, 63% of maximal activity at 60°C, and 67% of maximal activity at 70°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
inner membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
FtsH plays a role in phage lambda infection, serves a dual function in regulation of lipopolysaccharide biosynthesis and is involved in survival upon stress conditions like heat shock or osmotic stress
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
-
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
T.ftsH gene, DNA determination and analysis, expression as His-tagged protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Asahara, Y.; Atsuta, K.; Motohashi, K.; Taguchi, H.; Yohda, M.; Yoshida, M.
FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues
J. Biochem.
127
931-937
2000
Thermus thermophilus (Q5SI82), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SI82)
Manually annotated by BRENDA team
Langklotz, S.; Baumann, U.; Narberhaus, F.
Structure and function of the bacterial AAA protease FtsH
Biochim. Biophys. Acta
1823
40-48
2012
Aquifex aeolicus, Helicobacter pylori, Thermotoga maritima (Q9WZ49), Thermus thermophilus
Manually annotated by BRENDA team