STRINGSTRING
sodA sodA grpE grpE clpX clpX groL groL clpP clpP clpB clpB dnaK dnaK
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:
sodASuperoxide dismutase, Mn, putative; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a role in maintaining cell viability throughout all stages of growth, but may be the major SOD activity in the exponential growth- phase. Has a role in resisting external superoxide stress. Involved in acid tolerance and the acid-adaptive response. Mediates the derepression of perR regulon in the response to HOCl stress when the level of SOD activity is low. (199 aa)
grpECo-chaperone GrpE; 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-depend [...] (208 aa)
clpXATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (420 aa)
groLChaperonin, 60 kDa, GrpEL, putative; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (538 aa)
clpPATP-dependent Clp protease, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (195 aa)
clpBATP-dependent Clp protease, ATP-binding subunit 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. (869 aa)
dnaKDNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. (610 aa)
Your Current Organism:
Staphylococcus aureus
NCBI taxonomy Id: 93061
Other names: S. aureus subsp. aureus NCTC 8325, Staphylococcus aureus NCTC 8325, Staphylococcus aureus subsp. aureus NCTC 8325, Staphylococcus aureus subsp. aureus str. NCTC 8325, Staphylococcus aureus subsp. aureus strain NCTC 8325
Server load: low (18%) [HD]