| Primary Identifier | IPR014792 | Type | Domain |
| Short Name | RsbRA_N |
| description | The general stress response in Bacillus subtilis is governed by sigma(B), whose activity is controlled by a partner switching mechanism in which key protein interactions are governed by serine phosphorylation. In the environmental stress pathway, the RsbS antagonist binds and inactivates the RsbT switch protein/kinase. Following stress, RsbT phosphorylates RsbS, releasing RsbT to bind and activate the RsbU phosphatase.RsbRA (also known as RsbR) was previously reported to be a positive regulator that enhances RsbT kinase activity []. It has since been reported instead to function as a co-antagonist of RsbS [].For RsbS to function, it requires one of a family of four co-antagonist proteins, named RsbRA (RsbR), RsbRB (YkoB), RsbRC (YojH) and RsbRD (YqhA). These RsbRA paralogs each have a a C-terminal domain closely resembling the entire RsbS protein []. The N-terminal domain of RsbRA has been reported to show a classic globin fold. However, structural analysis has not revealed the presence of any bound cofactor, such as heme []. |
