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
AMN10636.1Heat-shock protein Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology. (831 aa)    
Predicted Functional Partners:
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, [...]
 0.989
grpE
Heat -hock 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- [...]
 
 0.976
htpG
Heat-shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.975
AMN10637.1
AAA family ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.958
groEL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.917
AMN10226.1
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.916
clpA
Clp protease ClpA; ATPase and specificity subunit of the ClpA-ClpP ATP dependent serine protease; directs protease to specific substrates; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family.
  
 
 0.881
clpB
Clp protease 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.
  
 
 0.881
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 
 0.802
groES
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.800
Your Current Organism:
Alteromonas macleodii
NCBI taxonomy Id: 28108
Other names: A. macleodii, ATCC 27126, Alteromonas sp. F12, CCUG 16128, CIP 103198, DSM 6062, JCM 20772, LMG 2843, LMG:2843, NBRC 102226, Pseudoalteromonas macleodii
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.