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PROSITE documentation PDOC50885 [for PROSITE entry PS50885] |
The HAMP linker domain (domain present in Histidine kinases, Adenyl cyclases, Methyl-accepting proteins and Phosphatases) is an approximately 50-amino acid α-helical region common to chemoreceptors and histidine kinases that is present in several multidomain sensor proteins that participate in a variety of signal transduction processes. One or several copies of the HAMP domain can be found in association with other domains such as the histidine kinase domain (see <PDOC50109>), the bacterial chemotaxis sensory transducer domain (see <PDOC00465>), the PAS repeat (see <PDOC50112>), the EAL domain (see <PDOC50883>), the GGDEF domain (see <PDOC50887>), the protein phosphatase 2C-like domain, the guanylate cyclase domain (see <PDOC00425>), or the response regulatory domain (see <PDOC50110>). It has been suggested that the HAMP domain possesses a role of regulating the phosphorylation or methylation of homodimeric receptors by transmitting the conformational changes in periplasmic ligand-binding domains to cytoplasmic signalling kinase and methyl-acceptor domains [1].
Some proteins known to contain a HAMP domain are listed below:
The profile we developed covers the entire HAMP domain.
Last update:December 2002 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Aravind L. Ponting C.P. |
Title | The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. | |
Source | FEMS Microbiol. Lett. 176:111-116(1999). | |
PubMed ID | 10418137 |