Cloned (Comment) | Organism |
---|---|
recombinant expression of Strep II-tagged FlaI protein in Escherichia coli strain BL21-CodonPlus-RIL, co-expression with Strep II-tagged FlaXc and His6-tagged FlaH | Sulfolobus acidocaldarius |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of various truncated versions of FlaI and interaction analysis with the archaellum subunit FlaX | Sulfolobus acidocaldarius |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
archaeal-type flagellum | archaellum | Sulfolobus acidocaldarius | 97589 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Sulfolobus acidocaldarius |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Sulfolobus acidocaldarius | - |
ADP + phosphate | - |
? | |
ATP + H2O | Sulfolobus acidocaldarius ATCC 33909 | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus acidocaldarius | Q4J9L0 | - |
- |
Sulfolobus acidocaldarius ATCC 33909 | Q4J9L0 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant Strep II-tagged FlaI, Strep II-tagged FlaXc, and His6-tagged FlaH from in Escherichia coli strain BL21-CodonPlus-RIL as ternary complex by nickel affinity chromatography, or single FlaI by avidin affinity chromatography | Sulfolobus acidocaldarius |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Sulfolobus acidocaldarius | ADP + phosphate | - |
? | |
ATP + H2O | - |
Sulfolobus acidocaldarius ATCC 33909 | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | crystal structure analysis, FlaI forms hexameric species in an ATP-dependent manner | Sulfolobus acidocaldarius |
Synonyms | Comment | Organism |
---|---|---|
FlaI | - |
Sulfolobus acidocaldarius |
General Information | Comment | Organism |
---|---|---|
additional information | interaction analysis of fluorescent-labeled proteins FlaI, FlaX and FlaH , overview | Sulfolobus acidocaldarius |
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 | Sulfolobus acidocaldarius |