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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
STM1251Putative molecular chaperone (small heat shock protein); Similar to E. coli heat shock protein (AAC76710.1); Blastp hit to AAC76710.1 (137 aa), 33% identity in aa 1 - 136; Belongs to the small heat shock protein (HSP20) family. (155 aa)    
Predicted Functional Partners:
ibpB
Small heat shock protein; Associates with aggregated proteins, together with IbpA, 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.
  
 
0.827
clpB
ATP-dependent protease; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...]
  
 
 0.734
ybbK
Putative inner membrane protein; Similar to E. coli putative protease (AAC73591.1); Blastp hit to AAC73591.1 (305 aa), 95% identity in aa 1 - 302.
 
 
  
 0.727
clpA
Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family.
 
 
 0.669
STM0272
Putative ATPase with chaperone activity; Homolog of Yersinia clpB; similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 42% identity in aa 150 - 449, 40% identity in aa 421 - 685, 32% identity in aa 30 - 74; Belongs to the ClpA/ClpB family.
  
 
 0.625
dnaK
Chaperone Hsp70; Acts as a chaperone.
  
 
 0.601
serA
Similar to E. coli D-3-phosphoglycerate dehydrogenase (AAC75950.1); Blastp hit to AAC75950.1 (410 aa), 96% identity in aa 1 - 410; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
      
 0.579
mopB
Chaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.549
hslU
ATPase component of the HslUV protease; 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.
   
  
 0.525
hslV
Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. Belongs to the peptidase T1B family. HslV subfamily.
   
  
 0.523
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.