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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
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[Homology]
Score
BMQ_2016Small heat shock protein; Belongs to the small heat shock protein (HSP20) family. (144 aa)    
Predicted Functional Partners:
cotP
Spore coat protein P; Belongs to the small heat shock protein (HSP20) family.
  
  
  0.969
BMQ_2931
Small heat shock protein; Belongs to the small heat shock protein (HSP20) family.
  
  
 
0.926
BMQ_2560
Hypothetical protein; Belongs to the small heat shock protein (HSP20) family.
  
  
 
0.908
clpC
ATP-dependent Clp protease ATP-binding subunit ClpC; Belongs to the ClpA/ClpB family.
  
 
 0.670
clpB
ATP-dependent chaperone 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.
  
 
 0.670
clpE
ATP-dependent Clp protease, ATP-binding subunit ClpE; Belongs to the ClpA/ClpB family.
  
 
 0.670
hslV
ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.567
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 
 0.537
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.530
hslU
Heat shock protein HslVU, ATPase 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.
  
  
 0.516
Your Current Organism:
Bacillus megaterium QM B1551
NCBI taxonomy Id: 545693
Other names: B. megaterium QM B1551, Bacillus megaterium str. QM B1551, Bacillus megaterium strain QM B1551
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