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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
groL-460 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)    
Predicted Functional Partners:
groS-2
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.994
groS
10 kDa chaperonin 1; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.984
groS1_2
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.984
grpE
Heat shock 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- [...]
 
 0.967
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.930
dnaJ
Molecular chaperone 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, [...]
 
 0.842
AMS39010.1
Pfam:pfam00012 Hsp70 protein.
  
 0.834
AMS43770.1
Molecular chaperone DnaJ; Pfam:pfam00226 DnaJ domain.
 
 0.789
AMS40304.1
Hypothetical protein; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
  
 
 0.766
rpoH
RNA polymerase sigma 70; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes.
  
 
 0.766
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.