The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.
The L8 protein complex consisting of ribosomal proteins L7/L12 and L10 in E. coli is assembled on the conserved region of 23 S rRNA termed the GTPase-associated domain. L7/L12 occur in four copies organised as two dimers. The L7/L12 dimer probably interacts with EF-Tu. L7 and L12 have identical sequences except an N-terminal serine in L7 which is post-translationally modified (addition of an acetyl group). The eukaryotic counterpart of the prokaryotic L8 is the P 'complex' consisting of homodimers of P1 and P2 and monomeric P0.
In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. The N-end rule targets specific proteins for destruction in prokaryotes and eukaryotes. ClpS is an N-end rule adaptor, which recognises N-end rule substrates, tethers them to the ClpAP protease, and then actively transfers the substrate to ClpAP for degradation. 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.
|Domain clusters (>95% seq id):||7|
|Domain clusters (>35% seq id):||3|
|Structural Clusters (5A):||1|
|Structural Clusters (9A):||1|