Protein Family Models

In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins [1]. [1]. 11931773. ClpS, a substrate modulator of the ClpAP machine. Dougan DA, Reid BG, Horwich AL, Bukau B;. Mol Cell 2002;9:673-683. [2]. 12426582. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA;. Nat Struct Biol 2002;9:906-911. (from Pfam)

Date:

2024-10-16

ATP-dependent Clp protease adaptor ClpS modulates the specificity of protein degradation by the ClpAP chaperone-protease complex; binds to the N-terminal substrate-domain of ClpA thereby redirecting degradation by ClpAP towards aggregated proteins

Date:

2015-09-24

Gene:

clpS

Date:

2020-10-26

Gene:

clpS

Date:

2021-08-26