STRINGSTRING
hslV hslV hslU hslU Rta_16570 Rta_16570 grpE grpE dnaK dnaK dnaJ dnaJ Rta_28350 Rta_28350 htpG htpG groS groS groL groL Rta_36760 Rta_36760
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:
hslVCandidate ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (186 aa)
hslUCandidate ATP-dependent hsl protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. (436 aa)
Rta_16570Hypothetical protein. (168 aa)
grpECandidate heat shock protein, HSP70 cofactor; 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. S [...] (197 aa)
dnaKCandidate heat shock protein, HSP70 family; Acts as a chaperone; Belongs to the heat shock protein 70 family. (652 aa)
dnaJCandidate heat shock protein J; 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 [...] (382 aa)
Rta_28350Chaperone protein-like protein. (422 aa)
htpGCandidate heat shock protein, HSP90 family; Molecular chaperone. Has ATPase activity. (641 aa)
groSgroES protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (117 aa)
groLgroEL protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
Rta_36760Thioredoxin-like protein. (300 aa)
Your Current Organism:
Ramlibacter tataouinensis
NCBI taxonomy Id: 365046
Other names: Acidivorax sp. TTB310, Acidovorax sp. TTB310, R. tataouinensis TTB310, Ramlibacter tataouinensis TTB310, Ramlibacter tataouinensis str. TTB310, Ramlibacter tataouinensis strain TTB310
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