EC Number   |
General Information |
Reference |
|---|
   3.6.4.B6 | evolution |
the closest structural homologues of FlaH are KaiC-like proteins, which are archaeal homologues of the circadian clock protein KaiC from cyanobacteria |
-, 758289 |
| 3.6.4.B6 | more |
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 |
-, 758289 |
| 3.6.4.B6 | more |
interaction analysis of fluorescent-labeled proteins FlaI, FlaX and FlaH , overview |
-, 733831 |
| 3.6.4.B6 | 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 |
734633 |
| 3.6.4.B6 | physiological function |
it is proposed that the enzyme is bi-functional in driving flagella assembly and movement |
-, 724227 |
| 3.6.4.B6 | 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 |
-, 733831 |
| 3.6.4.B6 | 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 |
-, 734205 |
| 3.6.4.B6 | 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 |
-, 758289 |
