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Information on EC 3.4.24.B20 - FtsH protease and Organism(s) Escherichia coli and UniProt Accession P0AAI3
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3.4.24.B20 FtsH proteaseSpecify your search results
Word Map
- 3.4.24.B20
- chloroplast
-
photosystem
- thylakoids
-
variegation
-
photodamaged
-
photoinhibition
- sigma32
-
ftsh-mediated
- rpoh
-
grana
- lpxc
-
photoinhibitory
-
ftsh-dependent
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ftsh protease, ftsh2, ftsh1, ftsh11, ftsh5, ftsh3, ftsh6, ftsh12, atp-dependent zinc metalloprotease, atftsh2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
253850-13-4
-
SUBSTRATE
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
RNase colicin D + H2O
?
-
the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
-
-
?
subunit SecY of the SecAEG translocase + H2O
?
-
membrane substrate of FtsH
-
-
?
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
-
-
?
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin from Anabaena PCC 7119 is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form
-
-
?
lambdaCII + H2O
?
-
the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
-
-
?
RpoH + H2O
?
-
RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
-
-
?
RpoH + H2O
?
-
several RpoH residues critical for degradation are located in the highly conserved region 2.1. The double mutation A131E/K134V significantly stabilizes RpoH against degradation by the FtsH protease, while the single-point mutations at these positions only show a slight effect on RpoH stability. A minimal RpoH variant composed of residues L37-G147, including region 2.1 and C, is a sufficient FtsH substrate. Region 2.1 and region C might serve as interaction surfaces for FtsH-mediated degradation
-
-
?
additional information
?
-
-
fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
-
-
?
additional information
?
-
-
the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
-
-
?
additional information
?
-
-
complex substrate recognition mechanisms, detailed overview. The ATPase domain forms the entrance to the central pore of FtsH with a diameter of about 15 A, a conserved Phe at position 228 of the pore is crucial for substrate binding. Substrates are pulled through the narrow gate and into the following protease domain using the energy of ATP hydrolysis for unfolding and translocation of the proteins. FtsH has only weak unfolding activity and is not able to degrade tightly folded model substrate proteins like GFP or DHFR
-
-
?
additional information
?
-
-
mutational substrate analysis, structure-function anaylsis, modelling, overview
-
-
?
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
Anabaena apoflavodoxin + H2O
?
-
FtsH degradation of 31 point mutants of Anabaena apoflavodoxin is inversely proportional to their conformational stabilities. FtsH degrades the apo form of Anabaena flavodoxin, but it is unable to hydrolyze the holo form, activities with fully and partly unfolded substrate protein, overview
-
-
?
lambdaCII + H2O
?
-
the key protein that influences the lysis/lysogeny decision of lambda by activating several phage promoters
-
-
?
RNase colicin D + H2O
?
-
the interaction of colicin D with LepB may ensure a stable association with the inner membrane that in turn allows the colicin recognition by FtsH
-
-
?
RpoH + H2O
?
-
RpoH is rapidly degraded by chaperone-mediated FtsH-dependent proteolysis
-
-
?
additional information
?
-
-
fully unfolded states of proteins are the general substrates of FtsH, FtsH substrates can be either tagged proteins or proteins of low stability, substrate recognition and substrate specificity, overview
-
-
?
additional information
?
-
-
the six AAA domains bind and translocate proteins that are targeted for destruction in an ATP-dependent manner into the interior of the molecule, where the proteolytic sites are located and where substrate proteins are degraded in a processive manner
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
-
dependent on. FtsH is a metalloprotease and the protease domain contains the zinc-coordinating HEXXH motif
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HflC protein
-
purified recombinant His6-tagged, 74 kDa dimers from Escherichia coli expressed in strain Bl21, inhibits the proteolysis of lambdaCII by FtsH, i.e. HflB, both in vitro and in vivo, mechanism, overview. Each HflC molecules interacts with another HflC molecule attached to the juxtaposed HflB
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HflK protein
-
purified recombinant His6-tagged, 74 kDa dimers from Escherichia coli expressed in strain Bl21, inhibits the proteolysis of lambdaCII by FtsH, i.e. HflB, both in vitro and in vivo, mechanism, overview. Each HflK molecules interacts with another HflK molecule attached to the juxtaposed HflB
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
dependent on, the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the hexameric FtsH protease is anchored to the inner membrane by two transmembrane helices per monomer such that both termini protrude into the cytoplasm
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
FtsH is a membrane-bound protein essential for the cell viability in Escherichia coli
metabolism
-
FtsH cellular functions and regulation involving several factors, overview
physiological function
physiological function
-
FtsH has both chaperone and protease activities, and it is a crucial element in protein quality control, involving a number of substrates and processes, including the degradation of unneeded and damaged membrane proteins as well as soluble signaling factors
physiological function
-
FtsH is a peculiar prokaryotic protease with low unfoldase activity. FtsH takes care of degrading unstable or inappropriately assembled proteins
physiological function
-
FtsH is the only known membrane-anchored AAA protease in bacteria that fulfills a variety of regulatory functions. FtsH-mediated regulation of LpxC levels by proteolysis crucial for cell viability. FtsH is involved in the quality control of misfolded or incorrectly inserted membrane proteins and acts either as a chaperone to help them refold or degrades them. Another important function of FtsH in Escherichia coli is control of heat shock gene expression, overview
physiological function
-
FtsH is necessary for the processing of colicinsDand E3 during their import
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
-
FtsH forms homohexameric ring structures and large heterocomplexes with HflK/C
additional information
-
the C-terminus comprise the cytoplasmic ATPase and protease domain. The ATPase domain contains the Walker A/B motifs and the second region of homology responsible for the binding and hydrolysis of ATP
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
FtsH is subject to selfprocessing and removes its C-terminal 7 amino acid residues
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Obrist, M.; Langklotz, S.; Milek, S.; Fuehrer, F.; Narberhaus, F.
Region C of the Escherichia coli heat shock sigma factor RpoH (sigma 32) contains a turnover element for proteolysis by the FtsH protease
FEMS Microbiol. Lett.
290
199-208
2009
Escherichia coli
Bandyopadhyay, K.; Parua, P.K.; Datta, A.B.; Parrack, P.
Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of lambdaCII in vitro
Arch. Biochem. Biophys.
501
239-243
2010
Escherichia coli
Liu, X.; Yu, F.; Rodermel, S.
Arabidopsis chloroplast FtsH, var2 and suppressors of var2 leaf variegation: a review
J. Integr. Plant Biol.
52
750-761
2010
Arabidopsis thaliana (O80860), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q9SD67), Escherichia coli, Synechocystis sp.
Ayuso-Tejedor, S.; Nishikori, S.; Okuno, T.; Ogura, T.; Sancho, J.
FtsH cleavage of non-native conformations of proteins
J. Struct. Biol.
171
117-124
2010
Escherichia coli
Yamamoto, Y.; Aminaka, R.; Yoshioka, M.; Khatoon, M.; Komayama, K.; Takenaka, D.; Yamashita, A.; Nijo, N.; Inagawa, K.; Morita, N.; Sasaki, T.; Yamamoto, Y.
Quality control of photosystem II: impact of light and heat stresses
Photosynth. Res.
98
589-608
2008
Arabidopsis thaliana (O80860), Arabidopsis thaliana (O80983), Arabidopsis thaliana (Q1PDW5), Arabidopsis thaliana (Q39102), Arabidopsis thaliana (Q84WU8), Arabidopsis thaliana (Q8VZI8), Arabidopsis thaliana (Q8W585), Arabidopsis thaliana (Q9FGM0), Arabidopsis thaliana (Q9FH02), Arabidopsis thaliana (Q9FIM2), Arabidopsis thaliana (Q9SAJ3), Arabidopsis thaliana (Q9SD67), Escherichia coli (P0AAI3), Spinacia oleracea, Synechocystis sp.
-
Narberhaus, F.; Obrist, M.; Fuehrer, F.; Langklotz, S.
Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents
Res. Microbiol.
160
652-659
2009
Escherichia coli
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