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
Cabys_384Co-chaperonin GroES (HSP10). (131 aa)    
Predicted Functional Partners:
groL
groL chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.966
dnaK
dnaK molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.864
grpE
grpE molecular chaperone 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 o [...]
  
 
 0.854
htpG
htpG molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
   
 
 0.814
hslU
hslU ATP-dependent HslUV protease ATP-binding subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.797
hslV
hslV ATP dependent peptidase CodWX, CodW component, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.781
rplL
Large subunit ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
   
  
 0.638
clpB
clpB ATP-dependent Clp protease ATP-binding subunit 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.
  
 
 0.637
Cabys_863
ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family.
  
 
 0.637
clpP
clpP ATP-dependent Clp protease, protease subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
  
 
 0.520
Your Current Organism:
Caldithrix abyssi
NCBI taxonomy Id: 880073
Other names: C. abyssi DSM 13497, Caldithrix abyssi DSM 13497, Caldithrix abyssi LF13, Caldithrix abyssi str. DSM 13497, Caldithrix abyssi strain DSM 13497
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.