STRINGSTRING
Cgl0094 Cgl0094 dnaK dnaK hscA hscA Cgl1312 Cgl1312 Cgl0093 Cgl0093 dnaJ2 dnaJ2 dnaJ dnaJ fkpA fkpA groES groES ppiA ppiA ppiB ppiB
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
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
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[Homology]
Score
Cgl0094PUTATIVE HEAT SHOCK PROTEIN (HSP90-FAMILY). (608 aa)    
Predicted Functional Partners:
dnaK
Heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.976
hscA
Molecular chaperone, HSP70 family.
   
 0.973
Cgl1312
Putative secreted protein.
    
 0.947
Cgl0093
Putative glycerol 3-phosphate dehydrogenase.
 
 
 0.943
dnaJ2
Molecular chaperone (contain C-terminal Zn finger domain), putative transcriptional repressor; 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 react [...]
  
 0.942
dnaJ
CHAPERONE WITH DNAK, HEAT SHOCK PROTEIN (DNAJ PROTEIN); 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-depend [...]
  
 0.942
fkpA
PROBABLE FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOME; PPIases accelerate the folding of proteins; Belongs to the FKBP-type PPIase family.
   
 0.932
groES
Chaperonin 10 Kd subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.891
ppiA
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
 0.847
ppiB
PEPTIDYL-PROLYL CIS-TRANS ISOMERASE.
  
 0.847
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
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