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
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
hslUATP-dependent protease ATP-binding subunit HslU; Heat shock protein involved in degradation of misfolded proteins; Derived by automated computational analysis using gene prediction method: Protein Homology. (440 aa)    
Predicted Functional Partners:
FP66_07140
ATP-dependent protease subunit HslV; Heat shock protein involved in degradation of misfolded proteins; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
FP66_13320
Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.967
FP66_13310
Molecular chaperone GrpE; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.962
FP66_14970
Heat shock protein 90; Molecular chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.957
groEL
Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...]
   
  
 0.952
FP66_15800
Clp protease ATP-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.951
groES
Molecular chaperone GroES; 10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.939
FP66_14640
Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
   0.911
dnaK
Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.884
FP66_09870
Lon protease; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.847
Your Current Organism:
Halomonas salina
NCBI taxonomy Id: 42565
Other names: ATCC 49509, CIP 106092, DSM 5928, Deleya salina, H. salina, JCM 21221, strain F8-11
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