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yegD protein (Xanthomonas campestris campestris) - STRING interaction network
"yegD" - Heat shock protein in Xanthomonas campestris campestris
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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
yegDHeat shock protein; Molecular chaperone (460 aa)    
Predicted Functional Partners:
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 [...] (197 aa)
   
 
  0.941
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (546 aa)
   
 
  0.885
hrcA
Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE- dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons (369 aa)
   
   
  0.874
dnaJ2
Curved DNA binding protein; DnaJ-class molecular chaperone with C-terminal Zn finger domain (302 aa)
   
 
  0.803
XCC1168
Hsp90xo protein; Molecular chaperone HSP90 family (624 aa)
   
 
  0.764
clpB
Chaperone 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family (861 aa)
   
 
  0.749
nfuA
Fe/S biogenesis protein NfuA; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe- 4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins (199 aa)
   
 
  0.743
clpA
ATP-dependent Clp protease subunit; ATPases with chaperone activity ATP-binding subunit; Belongs to the ClpA/ClpB family (760 aa)
   
 
  0.743
XCC3368
Glutaredoxin-like protein; Rhodanese-related sulfurtransferase (308 aa)
   
 
  0.734
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (634 aa)
     
 
  0.731
Your Current Organism:
Xanthomonas campestris campestris
NCBI taxonomy Id: 340
Other names: X. campestris pv. campestris, Xanthomonas campestris, Xanthomonas campestris (pv. campestris), Xanthomonas campestris campestris, Xanthomonas campestris pv. campestris
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