STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
clpB_1Chaperone protein 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. (861 aa)    
Predicted Functional Partners:
dnaK_1
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.963
dnaK_2
Chaperone protein DnaK; Belongs to the heat shock protein 70 family.
  
 
 0.949
clpP
ATP-dependent Clp protease proteolytic subunit; 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.
 
 
 0.927
tepA
Translocation-enhancing protein TepA.
  
 
 0.897
dnaJ
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 [...]
  
 
 0.880
grpE
Protein 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-dependent i [...]
  
 
 0.852
mecA1
Adapter protein MecA 1; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
    
 
 0.845
mecA2
Adapter protein MecA 2; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
    
 
 0.790
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.788
mcsB
Putative ATP:guanido phosphotransferase; Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.
  
 
 0.759
Your Current Organism:
Geobacillus thermodenitrificans
NCBI taxonomy Id: 33940
Other names: ATCC 29492, BGSC 94A1, Bacillus sp. BGSC W9A21, Bacillus sp. BGSC W9A45, Bacillus sp. BGSC W9A5, Bacillus sp. BGSC W9A54, Bacillus sp. BGSC W9A65, Bacillus sp. BGSC W9A66, Bacillus sp. BGSC W9A67, Bacillus sp. BGSC W9A69, Bacillus sp. BGSC W9A71, Bacillus sp. BGSC W9A73, Bacillus sp. BGSC W9A74, Bacillus sp. BGSC W9A86, Bacillus sp. BGSC W9A87, Bacillus sp. BGSC W9A91, Bacillus thermodenitrificans, DSM 465, G. thermodenitrificans, Geobacillus sp. A333, Geobacillus sp. F84a, Geobacillus sp. G11MC16, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Cihan et al. 2011, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Coorevits et al. 2012, LMG 17532, LMG:17532, strain R-35647
Server load: low (24%) [HD]