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cbpA protein (Klebsiella pneumoniae) - STRING interaction network
"cbpA" - Curved DNA-binding protein in Klebsiella pneumoniae
Nodes:
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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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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:
some 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 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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Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
cbpACurved DNA-binding protein; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM (305 aa)    
Predicted Functional Partners:
JG24_27590
With CpbA modulates the activity of the dnaK chaperone system; interacts with CbpA and inhibits both the DnaJ-like co-chaperone activity and the DNA binding activity of CbpA; Derived by automated computational analysis using gene prediction method- Protein Homology (101 aa)
 
 
  0.992
dnaK
Chaperone protein DnaK; Acts as a chaperone (638 aa)
 
  0.928
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11 (293 aa)
   
   
  0.844
grpE
Protein 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- dependent [...] (196 aa)
 
 
  0.830
hscA
Chaperone protein HscA; Involved in the maturation of iron-sulfur cluster-containing proteins; Derived by automated computational analysis using gene prediction method- Protein Homology (616 aa)
 
 
  0.720
clpB
Chaperone protein 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 (857 aa)
 
 
  0.694
JG24_16950
Derived by automated computational analysis using gene prediction method- Protein Homology (450 aa)
   
 
  0.690
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity (624 aa)
   
 
  0.638
fis
DNA-binding protein Fis; Activates ribosomal RNA transcription. Plays a direct role in upstream activation of rRNA promoters (98 aa)
           
  0.606
JG24_27225
UvrABC system protein A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate (941 aa)
   
 
  0.600
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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