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
ibpBHsp20/alpha crystallin family protein; COG: COG0071; Pfam: PF00011; InterPro: IPR002068; Belongs to the small heat shock protein (HSP20) family. (120 aa)    
Predicted Functional Partners:
clpB
ATP-dependent chaperone protein 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.
  
 
 0.629
clpV
Type VI secretion ATPase, ClpV1 family; COG: COG0542; Pfam: PF02861,PF00004,PF07724; InterPro: IPR003593; Belongs to the ClpA/ClpB family.
  
 
 0.629
clpA
ATP-dependent Clp protease ATP-binding subunit ClpA; COG: COG0542; Pfam: PF02861,PF00004,PF07724; InterPro: IPR013461; Belongs to the ClpA/ClpB family.
  
 
 0.629
htpG
Hsp90 protein; Molecular chaperone. Has ATPase activity.
  
 
 0.594
ibpA
Hsp20/alpha crystallin family protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent.
 
    
0.515
grpE
Co-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 of ATP-depend [...]
  
  
 0.473
EFE97004.1
TrkA C-terminal domain protein; COG: COG2985; Pfam: PF06826,PF02080; InterPro: IPR006512.
       0.456
hslV
ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.445
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.441
hslO
Chaperonin HslO; 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.
  
  
 0.441
Your Current Organism:
Serratia odorifera
NCBI taxonomy Id: 667129
Other names: S. odorifera DSM 4582, Serratia odorifera DSM 4582, Serratia odorifera str. DSM 4582, Serratia odorifera strain DSM 4582
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