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:
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[Homology]
Score
clpBChaperone 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. (871 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.986
clpP
Endopeptidase Clp; 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.
 
 
 0.961
Dshi_2892
SWISSPROT P0C054: Small heat shock protein ibpA; PFAM: PF00011; PROSITE: PS01031; SUPERFAMILY: SSF49764; COG: COG0071 - Molecular chaperone (small heat shock protein); Belongs to the small heat shock protein (HSP20) family.
  
 
 0.863
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 [...]
  
 
 0.833
ibpAB
PFAM: heat shock protein Hsp20; NCBI conserved domains: ibpA; low swissprot hit to Small heat shock protein ibpA from Salmonella choleraesuis; good Ref YP hit to heat shock protein Hsp20 [Jannaschia sp. CCS1].
  
 
 0.831
hslV
ATP-dependent HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.812
dnaJ
Chaperone protein 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, D [...]
  
 
 0.796
Dshi_2796
PFAM: heat shock protein Hsp20 SSF49764: HSP20-like chaperones superfamily; Hsp20; Belongs to the small heat shock protein (HSP20) family.
 
 
 0.791
groS
Chaperonin 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.780
lon
ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 
 0.746
Your Current Organism:
Dinoroseobacter shibae
NCBI taxonomy Id: 398580
Other names: D. shibae DFL 12 = DSM 16493, Dinoroseobacter shibae DFL 12, Dinoroseobacter shibae DFL 12 = DSM 16493, Dinoroseobacter shibae DSM 16493, Dinoroseobacter shibae DSM 16493 = DFL 12, Jannaschia sp. DFL-12
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.