STRINGSTRING
PBAL39_21640 protein (Pedobacter sp. BAL39) - STRING interaction network
"PBAL39_21640" - Heat shock protein 70 in Pedobacter sp. BAL39
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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PBAL39_21640Heat shock protein 70 (617 aa)    
Predicted Functional Partners:
grpE
HSP-70 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. Several rounds of ATP- depend [...] (193 aa)
 
  0.992
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, [...] (388 aa)
 
  0.989
groL
Protein Cpn60 ; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (546 aa)
 
  0.971
PBAL39_18439
Chaperone protein, dnaJ family (296 aa)
 
  0.958
PBAL39_24920
Iron-sulfur cluster assembly scaffold protein IscU ; A scaffold on which IscS assembles Fe-S clusters. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters (137 aa)
 
 
  0.891
PBAL39_24645
Putative heat-shock protein (594 aa)
     
  0.874
PBAL39_11337
Heat shock protein 90 (629 aa)
     
  0.874
PBAL39_21345
Co-chaperone Hsc20 (178 aa)
   
  0.858
PBAL39_14094
Putative ATP-dependent protease (828 aa)
   
 
  0.842
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 (865 aa)
   
 
  0.842
Your Current Organism:
Pedobacter sp. BAL39
NCBI taxonomy Id: 391596
Other names: P. sp. BAL39, Pedobacter BAL39, Pedobacter sp. BAL39
Server load: low (6%) [HD]