Protein Family Models

This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterised in E coli chemoreceptors. This domain recognises citrate and TCA cycle intermediates, cis-aconitate, boric acid, Phenanthrene, pyrene and benzopyrene (Matilla et el., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). [1]. 16306392. Four-helix bundle: a ubiquitous sensory module in prokaryotic signal transduction. Ulrich LE, Zhulin IB;. Bioinformatics. 2005;21:iii45-iii48. (from Pfam)

Date:

2024-10-16

This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs. [1]. 1601874. Sequence and characterization of Bacillus subtilis CheW. Hanlon DW, Marquez-Magana LM, Carpenter PB, Chamberlin MJ, Ordal GW;. J Biol Chem 1992;267:12055-12060. (from Pfam)

Date:

2024-10-16

methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

Date:

2024-04-06