3.4.24.B17: FtsH endopeptidase

This is an abbreviated version!
For detailed information about FtsH endopeptidase, go to the full flat file.

Reaction

proteolytic degradation of proteins =

Synonyms

cell division protein ftsH, FtsH, FtsH protease, FTSH_ECOLI, HflB, HlB, M41.001, MtFtsH, T.ftsH

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.B17 FtsH endopeptidase

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Results	in table
7	Activating Compound
5	AA Sequence
1	CAS Registry Number
19	Cloned(Commentary)
57	Cofactor
5	Crystallization (Commentary)
2	Expression
18	General Information
18	Inhibitors
6	KM Value [mM]
49	Localization
26	Metals/Ions
3	Molecular Weight [Da]
63	Natural Substrates/ Products (Substrates)
308	Organism
7	pH Optimum
3	Posttranslational Modification
39	Protein Variants
13	Purification (Commentary)
13	Reaction
24	Reaction Type
77	Reference
2	Renatured (Commentary)
12	Specific Activity [micromol/min/mg]
263	Substrates and Products (Substrate)
22	Subunits
100	Synonyms
12	Temperature Optimum [°C]
2	Temperature Range [°C]
8	Turnover Number [1/s]

Reaction

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Reaction on EC 3.4.24.B17 - FtsH endopeptidase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

proteolytic degradation of proteins

12 entries

proteolytic degradation of proteins

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proteolytic degradation of proteins

mechanism

Escherichia coli

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650184, 651704

proteolytic degradation of proteins

degenerate cleavage specificity, degradation of hydrophobic membrane-spanning segments of misfolded mitochodrial membrane proteins

Escherichia coli

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649814

proteolytic degradation of proteins

degradation of membrane proteins

Escherichia coli

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652391

proteolytic degradation of proteins

degradation of soluble and integral membrane proteins

Escherichia coli

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650082

proteolytic degradation of proteins

enzyme is a AAA protease, highly conserved residues Phe228 and Gly230 lie in the central pore region of the hexamer and are important in proteolysis and coupling to ATP

Escherichia coli

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652491

proteolytic degradation of proteins

essential for activity are residues Asn301, Asp307, Arg312, and Arg315, mechanism, ligand binding site at residues 144-398

Escherichia coli

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653896

proteolytic degradation of proteins

mechanism, reaction only occurs with protein substrates of low intrinsic thermodynamic stability, sequential degradation from the tail

Escherichia coli

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653191

proteolytic degradation of proteins

preference for positively charged and hydrophobic amino acid residues, large cytoplasmic domain contains ATPase and protease activities

Escherichia coli

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649856

proteolytic degradation of proteins

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

Thermus thermophilus

Q5SI82

651768

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

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651260

proteolytic degradation of proteins

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

Thermus thermophilus HB8 / ATCC 27634 / DSM 579

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