STRINGSTRING
clpB-1 clpB-1 groL groL dnaJ-1 dnaJ-1 APB32934.1 APB32934.1 dnaK-1 dnaK-1 grpE grpE dnaK-2 dnaK-2 APB34178.1 APB34178.1 APB34231.1 APB34231.1 hrcA hrcA dnaJ-2 dnaJ-2 cbpA-1 cbpA-1 groL-2 groL-2 groS groS APB35093.1 APB35093.1 cbpA-2 cbpA-2 dnaK-3 dnaK-3
Nodes:
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
clpB-1ATP-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; Belongs to the ClpA/ClpB family. (866 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (559 aa)
dnaJ-1Heat shock protein; 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, DnaK [...] (374 aa)
APB32934.1DnaJ-class molecular chaperone with C-terminal Zn finger domain. (373 aa)
dnaK-1Molecular chaperone dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. (626 aa)
grpEGrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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 i [...] (267 aa)
dnaK-2Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (624 aa)
APB34178.1Hypothetical protein. (352 aa)
APB34231.1DnaK-type molecular chaperone; Belongs to the heat shock protein 70 family. (514 aa)
hrcANegative regulator of class I heat shock protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (354 aa)
dnaJ-2DnaJ-class molecular chaperone. (207 aa)
cbpA-1Heat shock protein DnaJ domain-containing protein. (304 aa)
groL-2Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)
groSCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (103 aa)
APB35093.1Heat shock protein DnaJ domain-containing protein. (139 aa)
cbpA-2Chaperone DnaJ domain-containing protein. (314 aa)
dnaK-3Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (637 aa)
Your Current Organism:
Gloeomargarita lithophora
NCBI taxonomy Id: 1188229
Other names: Candidatus Gloeomargarita lithophora D10, G. lithophora Alchichica-D10, Gloeomargarita lithophora Alchichica-D10, Gloeomargarita lithophora PMC 919.15
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