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
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Substrates Products
Substrates Products on EC 3.4.24.B17 - FtsH endopeptidase
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REACTION DIAGRAM
3-deoxy-D-manno-octulosonate transferase + H2O
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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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apo-flavodoxin + H2O
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degradation of apo-flavodoxin from Escherichia coli, no degradation of holo-flavodoxin containing non-covalently bound flavin mononucleotide. A mutant flavodoxin carrying a substitution of Tyr94 to Asp (FldYD) with a lower affinity for FMN is efficiently degraded. FtsH is able to initiate degradation of the FldYD moiety even when it is sandwiched by glutathione S-transferase, green fluorescent protein, or both green fluorescent protein and glutathione S-transferase
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barnase tagged with SsrA tail + H2O
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tail specific degradation
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beta-casein + H2O
small peptides of 13-20 amino acid residues
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product analysis
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biotin carboxylase/biotin carboxyl carrier protein + H2O
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chimeric protein PhoA-TM8-C30 + H2O
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recombinant substrate protein consists of one transmembrane segment of protein SecY, i.e. TM8, plus the following 30 residues of a cytoplasmic part, and the C-terminal end of alkaline phosphatase PhoA
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?
dihydrofolate reductase tagged with SsrA tail + H2O
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tail specific degradation
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FGH-(NO2)FFAF-methyl ester + H2O
FGH-(NO2)F + Phe-Ala-Phe-methyl ester
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exclusively cleaved at the (NO2)Phe-Phe bond
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fusion protein SecY-(P5)-PhoA + H2O
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recombinant substrate protein consists of one protein SecY without its C-terminus, and the alkaline phosphatase PhoA
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heat shock sigma factor RpoH (sigma32) + H2O
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in addition to the turnover element in region 2.1, a second region important for proteolysis of RpoH by FtsH lies in region C of the sigma factor
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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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?
largely unfolded alpha-lactalbumin + H2O
peptides
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
?
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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?
phage lambda CII protein + H2O
small peptides of 13-20 amino acid residues
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recombinant protein substrate with -terminal or C-terminal His-tag, respectively, or no His-tag
product analysis
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protein GlpG + H2O
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helical bundle membrane protein, model membrane substrate
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protein P22 Arc repressor tagged with 108 motif tail + H2O
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tail specific degradation
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protein P22 Arc repressor tagged with SsrA tail + H2O
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tail specific degradation
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?
protein sigma32 + H2O
peptides
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regulatory protein
approximately 10 peptides with MW below 3 kDa
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RpoH protein + H2O
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enzyme recognizes the internal RpoH protein region, N- and C-terminus have no or only marginal effect on substrate binding
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?
ssrA-tagged ProW1-182 + H2O
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substrate is a truncated variant of multiple-pass inner-membrane protein ProW
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unstable derivatives of the N-terminal domain of the lambdacI repressor + H2O
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3 derivatives with a nonpolar pentapeptide tail, i.e. cI104, cI105, cI108, and 1 with the SsrAtag, i.e. cI-SsrA
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casein + H2O
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caseinolytic activity is not stimulated by ATP
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FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form
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flavodoxin + H2O
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degrades flavin mononucleotide-free flavodoxin but not holo-flavodoxin
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flavodoxin + H2O
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degrades flavin mononucleotide-free flavodoxin but not holo-flavodoxin
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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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substrate is a virulence protein located at the inner mitochondrial membrane. A single substitution W226A promotes the FtsH-mediated proteolysis. The Trp residue is located at the very C-terminus of the cytoplasmic domain of the MgtC protein
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MgtC mutant W226A
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substrate is a virulence protein located at the inner mitochondrial membrane. A single substitution W226A promotes the FtsH-mediated proteolysis. The Trp residue is located at the very C-terminus of the cytoplasmic domain of the MgtC protein
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phage shock protein C is the only core component of the phage shock protein system affected by FtsH. Phage shock protein B prevents FtsH-dependent degradation of phage shock protein C
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phage shock protein C + H2O
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phage shock protein C is the only core component of the phage shock protein system affected by FtsH. Phage shock protein B prevents FtsH-dependent degradation of phage shock protein C
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phage shock protein C + H2O
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phage shock protein C is the only core component of the phage shock protein system affected by FtsH. Phage shock protein B prevents FtsH-dependent degradation of phage shock protein C
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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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ATP hydrolysis cause conformational changes, regulate the accessibility of the proteolytic sites and trigger unfolding of substrate polypeptides, C-terminally located second region of homology, i.e. SRH region, is conserved throughout the AAA proteases and plays an intermolecular catalytic role
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protein + H2O
peptides
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degradation of membrane and cytoplasmic proteins
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protein + H2O
peptides
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degradation probably involves dislocation of the substrate membrane protein to the cytosol
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protein + H2O
peptides
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enzyme recognizes nonpolar tails, overview, degrades integral and cytoplasmic proteins
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protein + H2O
peptides
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enzyme shows limited substrate specificity which is not primarily determined by the structure of the protein
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protein + H2O
peptides
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preference for positively charged and hydrophobic amino acid residues, degradation of uncomplexed integral membrane proteins and short-life cytoplasmic proteins
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protein + H2O
peptides
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substrate binding by the cytoplasmic domain
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protein + H2O
peptides
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substrate specificity, soluble and integral membrane proteins, initiation of degradation by recognition and binding of more than 20 amino acids of the C-terminal cytosolic tail of the substrate, subsequently the substrate can be dislocated into the cytosol or degraded simultaneously bidirectionally
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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 + H2O
peptides
cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates, overview
between 10 and 30 kDa, no large intermediates
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protein + H2O
peptides
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates, overview
between 10 and 30 kDa, no large intermediates
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protein F0 subunit a + H2O
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subunit a of the F0 part of the H+-ATPase, unstable in the absence of other F0 subunits leading to degradation by the enzyme
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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 LpxC + H2O
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protein LpxC is UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
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protein LpxC + H2O
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turnover of LpxC requires a length- and sequence-specific C-terminal degradation signal. LpxC proteins from Salmonella enterica, Yersinia pseudotuberculosis, and Vibrio cholerae are degraded with half-lives comparable to the half-life of Escherichia coli LpxC (8 to 12 min). LpxC from Pseudomonas aeruginosa is degraded slowly with a half-life of 78 min. LpxC proteins from Agrobacterium tumefaciens and Rhodobacter capsulatus are degraded with half-lives of about 68 min and 20 min, respectively
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protein LpxC + H2O
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Escherichia coli W3110 / ATCC 27325
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turnover of LpxC requires a length- and sequence-specific C-terminal degradation signal. LpxC proteins from Salmonella enterica, Yersinia pseudotuberculosis, and Vibrio cholerae are degraded with half-lives comparable to the half-life of Escherichia coli LpxC (8 to 12 min). LpxC from Pseudomonas aeruginosa is degraded slowly with a half-life of 78 min. LpxC proteins from Agrobacterium tumefaciens and Rhodobacter capsulatus are degraded with half-lives of about 68 min and 20 min, respectively
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protein LpxC + H2O
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Escherichia coli W3110 / ATCC 27325
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protein LpxC is UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
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protein SecY + H2O
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substrate protein is a subunit of protein translocase, failed to assemble with its partner SecE
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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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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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protein sigma32 + H2O
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no activity with the isolated 21 amino acid peptide from the C-terminus, heat shock promotor-specific subunit of RNA polymerase, wild-type and C-terminally truncated, up to 21 amino acid residues, protein, the substrates C-terminus is not required for activity or recognition and binding
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protein sigma32 + H2O
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wild-type enzyme and fusion mutants MF1-4, not MF5, substrate protein is a heat-shock transcription factor, sigma32-C-his
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protein sigma32 + H2O
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Escherichia coli W3110 / ATCC 27325
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protein sigma32 is also called RhoP
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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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UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase + H2O
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Escherichia coli W3110 / ATCC 27325
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uncomplexed form of the subunit alpha of the proton ATPase F0 + H2O
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Escherichia coli W3110 / ATCC 27325
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peptides
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between 10 and 30 kDa, no large intermediates
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unfolded alpha-casein + H2O
peptides
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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between 10 and 30 kDa, no large intermediates
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peptides
cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates
between 10 and 30 kDa, no large intermediates
?
unfolded pepsin + H2O
peptides
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
cleavage of small peptides from the C-terminal side of hydrophobic residues, no large intermediates
between 10 and 30 kDa, no large intermediates
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?
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no activity with bovine serum albumin
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additional information
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construction of an in vitro reaction system in which the enzyme is membrane embedded and not solubilized by detergent, two inverted membrane vesicles or proteoliposomes, one bearing the enzyme, the other bearing the substrate protein, are fused
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additional information
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enzyme shows overlapping substrate specificity with the proteases C1pXP and C1pAP, the enzymes can compensate for each other in degrading the c1-SsrA tagged substrate protein
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additional information
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large complexes exhibit either ATPase and protease activity, while smaller ones do not
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additional information
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no activity with GFP-tagged proteins
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additional information
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the enzyme acts in cooperation with the homologous proteins HflK and HflC, the 3 proteins assemble at the periplasmic site of the plasma membrane, resulting in prohibitin-like modulation of the enzymes substrate specificity and activity
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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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additional information
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protein LpxC from A aeolicus is not degraded by FtsH from Escherichia coli
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additional information
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Escherichia coli W3110 / ATCC 27325
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protein LpxC from A aeolicus is not degraded by FtsH from Escherichia coli
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additional information
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no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
no activity with native proteins as isopropylmalate dehydrogenase, glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus, and bovine pancreas RNaseA
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?