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groS protein (Sideroxydans lithotrophicus) - STRING interaction network
"groS" - Chaperonin Cpn10 in Sideroxydans lithotrophicus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (96 aa)    
Predicted Functional Partners:
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (548 aa)
 
  0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone (641 aa)
 
 
  0.984
grpE
GrpE 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 [...] (175 aa)
     
 
  0.975
htpG
ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity (633 aa)
     
 
  0.931
rpsJ
Ribosomal protein S10; Involved in the binding of tRNA to the ribosomes (103 aa)
   
   
  0.871
Slit_2312
Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (194 aa)
   
 
  0.846
rplL
Ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation (126 aa)
   
   
  0.841
hscA
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)
 
 
  0.821
tuf
Translation elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (396 aa)
     
 
  0.790
Slit_0753
Translation elongation factor Tu (396 aa)
     
 
  0.790
Your Current Organism:
Sideroxydans lithotrophicus
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
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