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
groSMolecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (98 aa)    
Predicted Functional Partners:
groEL-2
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 [...]
 
 
 0.999
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 [...]
 
 
 0.998
grpE
Molecular 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 [...]
 
 
 0.983
dnaK
Fe-S protein assembly chaperone HscA; 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.
 
 
 0.983
APH01085.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.824
APH00834.1
Serine hydroxymethyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.817
rplL
50S ribosomal protein L7; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
  
  
 0.813
APH00576.1
Cardiolipin synthase B; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
  0.790
APH02267.1
NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.789
APH02573.1
ATP-dependent chaperone ClpB; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.789
Your Current Organism:
Janibacter terrae
NCBI taxonomy Id: 103817
Other names: ATCC BAA-130, CCUG 45369, CIP 107018, DSM 13876, DSM 13953 [[Janibacter brevis Imamura et al. 2000]], J. terrae, JCM 10705, JCM 12887 [[Janibacter brevis Imamura et al. 2000]], Janibacter brevis, Janibacter brevis Imamura et al. 2000, Janibacter terrae Yoon et al. 2000 emend. Lang et al. 2003, KCCM 80001, KCTC 19953, NBRC 107853, strain 10N [[Janibacter brevis Imamura et al. 2000]], strain CS12
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