3.4.24.B17: FtsH endopeptidase
This is an abbreviated version!
For detailed information about FtsH endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.B17
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3.4.24.B17
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cushing
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cortisol-producing
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matriptase
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ttsps
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pro-hgf
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prkar1a
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ctnnb1
- 3.4.24.B17
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cushing
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cortisol-producing
- matriptase
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ttsps
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pro-hgf
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prkar1a
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ctnnb1
Reaction
proteolytic degradation of proteins =
Synonyms
cell division protein ftsH, FtsH, FtsH protease, FTSH_ECOLI, HflB, HlB, M41.001, MtFtsH, T.ftsH
ECTree
3.4.24.B17 FtsH endopeptidaseAdvanced search results
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Natural Substrates Products on EC 3.4.24.B17 - FtsH endopeptidase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-deoxy-D-manno-octulosonate transferase + H2O
?
3-deoxy-D-manno-octulosonate transferase carries out the attachment of two KDO residues to the lipid A precursor (lipid IVA) to form the minimal essential structure of the lipopolysaccharide (KDO2-lipid A). Thus, FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of lipopolysaccharide
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?
lambda Xis + H2O
?
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protein substrate is required for site-specific excision of phage lambda from the bacterial chromosome
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?
LpxC + H2O
?
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ATP-dependent. Essentiality of FtsH lies in its function to keep the proper LPS/phospholipid ratio by degrading LpxC
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-
?
phage lambda CII protein + H2O
small peptides
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enzyme participates in the phage lambda lysis-lysogeny decision by degrading the CII transcriptional activator and by its response to inhibition by the lambda CIII gene product
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?
protein F0 subunit a + H2O
?
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degradation of membrane protein, essentially required as a membrane-integrated quality control
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?
protein LpxC + H2O
?
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essential for cell viability, enzyme controls the steady-state level of the LpxC protein, which has a key regulatory role in the biosynthesis of lipopolysaccharides
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?
protein YccA + H2O
?
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degradation of membrane protein, essentially required as a membrane-integrated quality control
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?
sigma32 + H2O
?
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hydrolyzes about 140 ATP molecules during the degradation of a single molecule of cy2-sigma32. Degradation of sigma32 proceeds from the N-terminus to the C-terminus
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?
Protein + H2O
?
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FtsH degrades misassembled membrane proteins and a subset of cytoplasmic regulatory proteins
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?
Protein + H2O
?
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the enzyme can unfold proteins with lower Tms such as glutathione S-transferase (Tm: 52°C)
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?
protein + H2O
peptides
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degradation of regulatory proteins to control gene activity and metabolism
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?
protein + H2O
peptides
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degrades misassembled membrane protein complexes and plays a vital role in membrane quality control, degrades cytoplasmic regulatory proteins
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?
protein + H2O
peptides
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enzyme affects several processes including cell division, the synthesis of phospholipids and lipopolysaccharides, the anchoring of integral membrane proteins, mRNA stability, and colchicin tolerance, degradation of membrane proteins, essentially required as a membrane-integrated quality control
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?
protein + H2O
peptides
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housekeeping function, because the enzyme lacks a robust unfoldase activity, it is able to use the substrate protein folding state as a criterion for degradation
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?
protein + H2O
peptides
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involved in membrane protein assembly as well as degradation of unstable proteins
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?
protein + H2O
peptides
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involved in the degradation of regulatory proteins and uncomplexed subunits of membrane protein complexes
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?
protein + H2O
peptides
tail specific pathway for removing abnormal cytoplasmic proteins via the enzyme, disposition by degradation of polypeptides synthesized from truncated mRNA molecules and are C-terminally tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10Sa stable RNA
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?
protein + H2O
peptides
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FtsH degrades a set of short-lived proteins, enabling cellular regulation at the level of protein stability. FtsH also degrades some misassembles membrane proteins, contributing to their quality maintenance. One biological role of FtsH might be to affect the development and life cycle of infecting or episomal genetic systems, by degrading their key regulatory molecules. The enzyme has a special ability to dislocate membrane protein substrates out of the membrane for which its own membrane-embedded nature is essential
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?
protein SecY + H2O
?
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uncomplexed subunit of the protein translocase
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?
protein SecY + H2O
?
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degradation of membrane protein, essentially required as a membrane-integrated quality control
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?
protein SecY + H2O
?
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quality control, the enzyme regulates the amount of SecY assembled in the mitochondrial membrane, elimination of uncomplexed SecY is important for optimum protein translocation and for the integrity of the membrane
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?
protein SecY + H2O
?
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SecY protein is a subunit of protein translocase
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?
additional information
?
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dislocation of membrane proteins mediated by the enzyme, periplasmic segments can also be degraded by the enzyme
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?
additional information
?
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FtsH functions as a membrane chaperone and protease. FtsH and YidC have a linked role in the quality control of inner membrane proteins
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?
