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ATP + H2O
ADP + phosphate
CTP + H2O
CDP + phosphate
GTP + H2O
GDP + phosphate
UTP + H2O
UDP + phosphate
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
essential role in archaellum assembly
-
-
?
ATP + H2O
ADP + phosphate
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement
-
-
?
ATP + H2O
ADP + phosphate
hydrolyses ATP in a co-operative manner. Hydrolyses ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP. No conversion of ADP into AMP is detected
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement
-
-
?
ATP + H2O
ADP + phosphate
hydrolyses ATP in a co-operative manner. Hydrolyses ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP. No conversion of ADP into AMP is detected
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
essential role in archaellum assembly
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
CTP + H2O
CDP + phosphate
about 30% of the activity with ATP
-
-
?
CTP + H2O
CDP + phosphate
about 30% of the activity with ATP
-
-
?
CTP + H2O
CDP + phosphate
hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP
-
-
?
CTP + H2O
CDP + phosphate
hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP
-
-
?
GTP + H2O
GDP + phosphate
about 20% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
about 20% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP
-
-
?
GTP + H2O
GDP + phosphate
hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP
-
-
?
UTP + H2O
UDP + phosphate
about 50% of the activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
about 50% of the activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP
-
-
?
UTP + H2O
UDP + phosphate
hydrolysed ATP with the highest rate, but it is also able to hydrolyse GTP, CTP and UTP
-
-
?
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaH binds to immobilized ATP but lacks ATPase activity. FlaH may need additional factor(s) to enable ATPase activity, or that perhaps it lacks ATPase activity but ATP acts as a cofactor, affecting FlaH function
-
-
-
additional information
?
-
FlaI is the bifunctional ATPase that is involved in assembly and rotation of the archaellum
-
-
?
additional information
?
-
FlaI is the bifunctional ATPase that is involved in assembly and rotation of the archaellum
-
-
?
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ATP + H2O
ADP + phosphate
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
essential role in archaellum assembly
-
-
?
ATP + H2O
ADP + phosphate
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement
-
-
?
ATP + H2O
ADP + phosphate
essential role in archaellum assembly
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
enzyme FlaH interacts with the ATPase FlaI, another archaeal motility system protein. FlaI is an ATP-binding protein. In the presence of ATP, the interaction between FlaH and FlaI becomes weaker
-
-
-
additional information
?
-
FlaI is the bifunctional ATPase that is involved in assembly and rotation of the archaellum
-
-
?
additional information
?
-
FlaI is the bifunctional ATPase that is involved in assembly and rotation of the archaellum
-
-
?
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evolution
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria
evolution
-
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria
-
evolution
-
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria
-
evolution
-
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria
-
evolution
-
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria
-
evolution
-
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria
-
physiological function
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement
physiological function
-
FlaI, the only ATPase in the archaellum operon, is bifunctional, essential not only for the assembly of the archaellum filament but also for the completed organelle to rotate. While the major function of the archaellum is motility, it can also help archaeal cells attach to various surfaces or to interact with other cells
physiological function
-
FlaI, the only ATPase in the archaellum operon, is bifunctional, essential not only for the assembly of the archaellum filament but also for the completed organelle to rotate. While the major function of the archaellum is motility, it can also help archaeal cells attach to various surfaces or to interact with other cells
physiological function
-
FlaI, the only ATPase in the archaellum operon, is bifunctional, essential not only for the assembly of the archaellum filament but also for the completed organelle to rotate. While the major function of the archaellum is motility, it can also help archaeal cells attach to various surfaces or to interact with other cells
physiological function
-
FlaI, the only ATPase in the archaellum operon, is bifunctional, essential not only for the assembly of the archaellum filament but also for the completed organelle to rotate. While the major function of the archaellum is motility, it can also help archaeal cells attach to various surfaces or to interact with other cells
physiological function
the enzyme shows a dual function in the assembly and the rotation of the archaellum, the archaeal motility structure that is the functional pendant of the bacterial flagellum but is assembled by a mechanism similar to that for type IV pili. FlaX, a crenarchaeal archaellum subunit from Sulfolobus acidocaldarius, forms a ring-like oligomer, and it was proposed that this ring may act as a static platform for torque generation in archaellum rotation. FlaX acts as a cytoplasmic scaffold in archaellum assembly, as it interacts with FlaI as well as with the recA family protein FlaH, the only cytoplasmic components of the archaellum. FlaI N- and C-termini interact with FlaX. FlaI, FlaX and FlaH interact with high affinities in the nanomolar range forming the cytoplasmic motor complex of the archaellum. The FlaX ring may assemble around FlaJ, and that FlaI confers conformational change of FlaJ transfers to the membrane domain of FlaX ring, which leads to correct incorporation of archaellin (FlaB) into the newly growing archaellum filament
physiological function
the enzyme shows a dual function in the assembly and the rotation of the archaellum, the archaeal motility structure that is the functional pendant of the bacterial flagellum but is assembled by a mechanism similar to that for type IV pili. The enzyme is required for stabilization of Flax, FlaX is essential for archaellum assembly and it is destabilized in the absence of FlaI, FlaH, and FlaJ indicating that these proteins might form a complex within the archaellum assembly apparatus. FlaI, the archaella subunit that forms an ATP-dependent hexamer, probably interacts with the sole polytopic membrane protein FlaJ. FlaX interacts with FlaI during the assembly of archaella using the C-terminal region
physiological function
the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system
physiological function
-
the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system
-
physiological function
-
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement
-
physiological function
-
the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system
-
physiological function
-
the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system
-
physiological function
-
the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system
-
physiological function
-
the enzyme shows a dual function in the assembly and the rotation of the archaellum, the archaeal motility structure that is the functional pendant of the bacterial flagellum but is assembled by a mechanism similar to that for type IV pili. FlaX, a crenarchaeal archaellum subunit from Sulfolobus acidocaldarius, forms a ring-like oligomer, and it was proposed that this ring may act as a static platform for torque generation in archaellum rotation. FlaX acts as a cytoplasmic scaffold in archaellum assembly, as it interacts with FlaI as well as with the recA family protein FlaH, the only cytoplasmic components of the archaellum. FlaI N- and C-termini interact with FlaX. FlaI, FlaX and FlaH interact with high affinities in the nanomolar range forming the cytoplasmic motor complex of the archaellum. The FlaX ring may assemble around FlaJ, and that FlaI confers conformational change of FlaJ transfers to the membrane domain of FlaX ring, which leads to correct incorporation of archaellin (FlaB) into the newly growing archaellum filament
-
physiological function
-
the enzyme shows a dual function in the assembly and the rotation of the archaellum, the archaeal motility structure that is the functional pendant of the bacterial flagellum but is assembled by a mechanism similar to that for type IV pili. The enzyme is required for stabilization of Flax, FlaX is essential for archaellum assembly and it is destabilized in the absence of FlaI, FlaH, and FlaJ indicating that these proteins might form a complex within the archaellum assembly apparatus. FlaI, the archaella subunit that forms an ATP-dependent hexamer, probably interacts with the sole polytopic membrane protein FlaJ. FlaX interacts with FlaI during the assembly of archaella using the C-terminal region
-
physiological function
-
the flagellar accessory protein FlaH of Methanocaldococcus jannaschii seems to have a regulatory role in archaeal flagellum motor complex assembly. FlaH is one of the conserved components of the archaeal motility system
-
additional information
interaction analysis of fluorescent-labeled proteins FlaI, FlaX and FlaH , overview
additional information
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
additional information
-
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
additional information
-
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
-
additional information
-
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
-
additional information
-
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
-
additional information
-
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
-
additional information
-
interaction analysis of fluorescent-labeled proteins FlaI, FlaX and FlaH , overview
-
additional information
-
a Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif. In the RecA protein this interaction coordinates position of Mg2+ ion which is important for ATP hydrolysis. The Asp127-Ser128 peptide bond of the Walker B motif is in the cis-conformation that has also been observed in other RecA superfamily members and seems to be a common feature of all RecA-like fold proteins
-
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hexamer
6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration
hexamer
ATP binding locks the FlaI hexamer into a more symmetrical and less dynamic conformation, which may promote hexamer assembly by stabilizing interactions across adjacent subunits FlaI must be able to assemble into its hexameric state to function as the archaellum-assembly ATPase
hexamer
crystal structure analysis, FlaI forms hexameric species in an ATP-dependent manner
hexamer
FlaI forms an ATP-dependent hexamer
hexamer
-
crystal structure analysis, FlaI forms hexameric species in an ATP-dependent manner
-
hexamer
-
FlaI forms an ATP-dependent hexamer
-
hexamer
-
6 * 55000, the enzyme undergoes ATP-dependent hexamerization, gel filtration
-
hexamer
-
ATP binding locks the FlaI hexamer into a more symmetrical and less dynamic conformation, which may promote hexamer assembly by stabilizing interactions across adjacent subunits FlaI must be able to assemble into its hexameric state to function as the archaellum-assembly ATPase
-
additional information
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
additional information
-
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
additional information
-
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
-
additional information
-
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
-
additional information
-
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
-
additional information
-
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
-
additional information
-
enzyme FlaH has a characteristic RecA-like fold. FlaH consists of a central, mostly parallel, twisted beta-sheet surrounded by several alpha-helices. A Walker A motif, or phosphate binding loop (P-loop), is located between beta3 and alpha2, and a Walker B motif lies on beta6. The highly conserved Asp127 of Walker B motif forms hydrogen bond with Ser41 of Walker A motif
-
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D290A
mutation has no effect on ATP hydrolysis
DELTA1-224
in strains expressing the mutant enzyme no archaellum is assembled and swimming motility is abolished. Mutant enzyme still exhibits 75% of ATPase activity compared to the full-length FlaI
DELTA1-29
strains overexpressing FlaIDELTA129 show that 10%20% of the cell population can assemble archaella, whereas complementation with wild-type FlaI leads to 40%50% of cells having archaella
E336A
mutation results in a reduction of approximately 90% of ATP hydrolysis compared with wild-type enzyme, mutant forms a stable oligomer after ATP binding
K268A
mutation results in a reduction of approximately 50% of ATP hydrolysis compared with wild-type enzyme, 20-fold lower binding affinity of ATP, no oligomerization
M69E/I72E/F76E
localization to the membrane is significantly reduced compared to that of wild-type
D290A
-
mutation has no effect on ATP hydrolysis
-
DELTA1-224
-
in strains expressing the mutant enzyme no archaellum is assembled and swimming motility is abolished. Mutant enzyme still exhibits 75% of ATPase activity compared to the full-length FlaI
-
DELTA1-29
-
strains overexpressing FlaIDELTA129 show that 10%20% of the cell population can assemble archaella, whereas complementation with wild-type FlaI leads to 40%50% of cells having archaella
-
E336A
-
mutation results in a reduction of approximately 90% of ATP hydrolysis compared with wild-type enzyme, mutant forms a stable oligomer after ATP binding
-
K268A
-
mutation results in a reduction of approximately 50% of ATP hydrolysis compared with wild-type enzyme, 20-fold lower binding affinity of ATP, no oligomerization
-
M69E/I72E/F76E
-
localization to the membrane is significantly reduced compared to that of wild-type
-
additional information
construction of various truncated versions of FlaI and interaction analysis with the archaellum subunit FlaX
additional information
-
construction of various truncated versions of FlaI and interaction analysis with the archaellum subunit FlaX
-
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Ghosh, A.; Hartung, S.; van der Does, C.; Tainer, J.A.; Albers, S.V.
Archaeal flagellar ATPase motor shows ATP-dependent hexameric assembly and activity stimulation by specific lipid binding
Biochem. J.
437
43-52
2011
Sulfolobus acidocaldarius (Q4J9L0), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q4J9L0)
brenda
Albers, S.V.; Driessen, A.J.
Analysis of ATPases of putative secretion operons in the thermoacidophilic archaeon Sulfolobus solfataricus
Microbiology
151
763-773
2005
Saccharolobus solfataricus (Q97WB7), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97WB7)
brenda
Reindl, S.; Ghosh, A.; Williams, G.J.; Lassak, K.; Neiner, T.; Henche, A.L.; Albers, S.V.; Tainer, J.A.
Insights into FlaI functions in archaeal motor assembly and motility from structures, conformations, and genetics
Mol. Cell.
49
1069-1082
2013
Sulfolobus acidocaldarius (Q4J9L0), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (Q4J9L0)
brenda
Banerjee, A.; Neiner, T.; Tripp, P.; Albers, S.V.
Insights into subunit interactions in the Sulfolobus acidocaldarius archaellum cytoplasmic complex
FEBS J.
280
6141-6149
2013
Sulfolobus acidocaldarius (Q4J9L0), Sulfolobus acidocaldarius ATCC 33909 (Q4J9L0)
brenda
Banerjee, A.; Ghosh, A.; Mills, D.J.; Kahnt, J.; Vonck, J.; Albers, S.V.
FlaX, a unique component of the crenarchaeal archaellum, forms oligomeric ring-shaped structures and interacts with the motor ATPase FlaI
J. Biol. Chem.
287
43322-43330
2012
Sulfolobus acidocaldarius (Q4J9L0), Sulfolobus acidocaldarius ATCC 33909 (Q4J9L0)
brenda
Albers, S.; Jarrell, K.
Archaellum moves archaea with distinction: the archaellum is a rotating motility appendage found only in the archaea; it assembles with a type IV pili-like mechanism
Microbe
10
283-288
2015
Halobacterium salinarum, Methanocaldococcus jannaschii, Methanococcus vannielii, Sulfolobus sp.
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brenda
Meshcheryakov, V.A.; Wolf, M.
Crystal structure of the flagellar accessory protein FlaH of Methanocaldococcus jannaschii suggests a regulatory role in archaeal flagellum assembly
Protein Sci.
25
1147-1155
2016
Methanocaldococcus jannaschii (Q58309), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii NBRC 100440 (Q58309), Methanocaldococcus jannaschii DSM 2661 (Q58309), Methanocaldococcus jannaschii ATCC 43067 (Q58309), Methanocaldococcus jannaschii JAL-1 (Q58309), Methanocaldococcus jannaschii JCM 10045 (Q58309)
brenda