HAMP Domain

In molecular biology, the HAMP domain (present in Histidine kinases, Adenylate cyclases, Methyl-accepting chemotaxis protein, Methyl accepting proteins and Phosphatases) is an approximately 50-amino acid alpha helix, alpha-helical region that forms a dimeric, four-helical coiled coil. It is found in bacterial sensor and chemotaxis proteins and in eukaryotic histidine kinases. The bacterial proteins are usually integral membrane proteins and part of a Two-component regulatory system, two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the PAS domain, PAS repeat, the EAL domain, the GGDEF domain, the protein phosphatase 2C-like domain, the guanylate cyclase domain, or the response gene regulation, regulatory domain. In its most common setting, the HAMP domain transmits conformational changes in periplasmic ligand (biochemistry), ligand-binding protein domain, domains to cytoplasmic cell signalling, signalling kinase and methyl-acceptor domains and thus regulates the phosphorylation or methylation activity of homodimeric receptor (biochemistry), receptors.

References

{{InterPro content, IPR003660

Protein families