{PDOC50885} {PS50885; HAMP} {BEGIN} *********************** * HAMP domain profile * *********************** The HAMP linker domain (domain present in Histidine kinases, Adenyl cyclases, Methyl-accepting proteins and Phosphatases) is an approximately 50-amino acid alpha-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 ), the bacterial chemotaxis sensory transducer domain (see ), the PAS repeat (see ), the EAL domain (see ), the GGDEF domain (see ), the protein phosphatase 2C- like domain, the guanylate cyclase domain (see ), or the response regulatory domain (see ). 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: - Anabaena cylindrica adenylate cyclase. It may function as a membrane- localized receptor protein. - Escherichia coli osmolarity sensor protein envZ. It functions as a membrane-associated protein kinase that phosphorylates ompR in response to environmental signals. - Escherichia coli sensor protein barA. It could activate ompR by phosphorylation. - Escherichia coli nitrate/nitrite sensor protein narX. It probably activates narL and narP by phosphorylation in the presence of nitrate. - Escherichia coli sensor protein cpxA. - Escherichia coli methyl-accepting chemotaxis protein I. - Escherichia coli hypothetical protein yfiN. - Escherichia coli protein yhjK. - Rhizobium sp. strain NGR234 probable chemoreceptor Y4FA. - Salmonella typhimurium methyl-accepting chemotaxis protein II. - Chlamydia trachomatis sigma regulatory family protein-PP2C phosphatase. - Treponema pallidum hypothetical protein TP0854. - Synechocystis sp. strain PCC 6803 pleD. - Synechocystis sp. strain PCC 6803 hypothetical protein sll1365. - Archaeoglobus fulgidus putative signal-transducing histidine kinase. - Archaeoglobus fulgidus hypothetical protein AF1503. - Halobacterium salinarium halobacterial transducer protein IV. - Yeast osmolarity two-component system protein SLN1. - Candida albicans protein NIK1. The profile we developed covers the entire HAMP domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2002 / First entry. [ 1] Aravind L., Ponting C.P. "The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins." FEMS Microbiol. Lett. 176:111-116(1999). PubMed=10418137 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}