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
Bccel_0831PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. (518 aa)    
Predicted Functional Partners:
grpE
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-dependent i [...]
  
  
 0.790
Bccel_3709
PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein.
  
  
 0.765
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.703
groL-2
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 0.703
clpX
ATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
  
 
 0.686
ftsH
Peptidase M41 FtsH domain protein; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family.
  
 
 0.680
eno
Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
   
 
 0.672
Bccel_0011
KEGG: hypothetical protein.
  
  
 0.636
Bccel_2868
KEGG: hypothetical protein; PFAM: Ankyrin repeat-containing domain-containing protein; SMART: Ankyrin.
  
  
 0.636
hslO
33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
  
  
 0.616
Your Current Organism:
Pseudobacteroides cellulosolvens
NCBI taxonomy Id: 398512
Other names: Bacteroides cellulosolvens ATCC 35603, Bacteroides cellulosolvens DSM 2933, P. cellulosolvens ATCC 35603 = DSM 2933, Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933, Pseudobacteroides cellulosolvens DSM 2933 = ATCC 35603
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