10 kDa chaperoninCH10_ECO57Protein Cpn10groES proteinP0A6G1CH10_ECO5762288020Escherichia coli O157:H7MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEAType I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts. GroES consists of seven identical 10 kDa subunits and is involved in assisting protein folding as the partner of another oligomeric protein, the GroEL chaperonin. Each GroES subunit uses a mobile loop with a conserved hydrophobic tripeptide for interaction with GroEL. The mobile loops are ∼16 amino acids in length and undergo a transition from disordered loops to beta-hairpins concomitant with binding the apical domains of GroEL. Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.DisorderedMobile loop1731VETKSAGGIVLTGSANativeFunction arises via a disorder to order transitionChaperonesProtein-protein bindingNuclear magnetic resonance (NMR)3036.5Potassium phosphate45Paper8876186Landry SJ, Taher A, Georgopoulos C, van der Vies SM1996Proc Natl Acad Sci U S A932111622-716223749Csizmók V, Szollosi E, Friedrich P, Tompa P2006Mol Cell Proteomics52265-7315238634Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ2004Protein Sci1382139-48Additional UniProt ID: P0A6F9 strain K12 (B178) was also used.