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
grpEMolecular chaperone GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology. (189 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
dnaJ
Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.993
hrcA
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
  
 0.984
groEL
Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...]
 
 0.981
AMB94242.1
Molecular chaperone GroES; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.959
clpB
ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.784
AMB94144.1
ATP-dependent Clp protease ATP-binding subunit ClpC; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.784
AMB94583.1
ATP-dependent Clp protease ATP-binding subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.784
clpP
ATP-dependent Clp protease proteolytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.700
trxA
Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.653
Your Current Organism:
Aerococcus sanguinicola
NCBI taxonomy Id: 119206
Other names: A. sanguinicola, Aerococcus sanguicola, Aerococcus sanguinicola corrig. Lawson et al. 2001 emend. Tohno et al. 2014, Aerococcus sp. CCUG 43001, CCUG 43001, CIP 106533, DSM 15633, JCM 11549
Server load: low (28%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.