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3.6.4.B6: archaeal flagellar ATPase

This is an abbreviated version!
For detailed information about archaeal flagellar ATPase, go to the full flat file.

Word Map on EC 3.6.4.B6

Reaction

ATP
+
H2O
=
ADP
 +
phosphate

Synonyms

ATPase FlaI, FkaI, flagellar accessory protein, FlaH, FlaI, motor ATPase, Saci_1173, SSO2316

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement
                3.6.4.B6 archaeal flagellar ATPase

Engineering

Engineering on EC 3.6.4.B6 - archaeal flagellar ATPase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 FlaIDELTA1–29 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 FlaIDELTA1–29 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