2019-08-28 09:45:402025-08-08 16:01:02

function

control of chemotaxisthreonine, glycine, serine, lysine, valine and arginine

control of chemotaxis to proline, threonine, glycine, serine, lysine, valine and arginine

The protein

[SW|Domains]

[SW|Cache domain] (aa 148-225) (according to UniProt)

[SW|HAMP domain] (aa 298-350) (according to UniProt)

[SW|Methyl-accepting transducer domain (aa 369-619)] (according to UniProt)

[SW|Cache domain] (aa 148-225) (according to UniProt)

[SW|HAMP domain] (aa 298-350) (according to UniProt)

[SW|Methyl-accepting transducer domain] (aa 369-619) (according to UniProt)

References

12864845, 15317802, 8251536, 9353924, 15544802, 6137212, 9721285, 2505839, 2105313, 12603740, 23038252, 18763711, 9721285, 21515776, 22931217, 27899502

12864845, 15317802, 8251536, 9353924, 15544802, 6137212, 9721285, 2505839, 2105313, 12603740, 23038252, 18763711, 9721285, 21515776, 22931217, 27899502, 31925330

The protein

Structure

[PDB|6S1K] (from E. coli, corresponds to aa 279 ... 593, 26% identity) [pubmed|31925330]