STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
from curated databases
ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity (633 aa)
Predicted Functional Partners:
Chaperone protein DnaK; Acts as a chaperone (641 aa)
Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB (622 aa)
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (374 aa)
Peptidylprolyl isomerase (228 aa)
Peptidylprolyl isomerase (151 aa)
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)
Histone deacetylase (307 aa)
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (548 aa)
ATP synthase F1, subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit (513 aa)
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE (861 aa)
Your Current Organism:
NCBI taxonomy Id: 580332 Other names: S. lithotrophicus, S. lithotrophicus ES-1, Siderooxidans, Siderooxidans lithoautotrophicus, Sideroxydans, Sideroxydans lithotrophicus, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1