STRINGSTRING
BACCAP_00794 protein (Pseudoflavonifractor capillosus) - STRING interaction network
"BACCAP_00794" - Uncharacterized protein in Pseudoflavonifractor capillosus
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
BACCAP_00794Uncharacterized protein (285 aa)    
Predicted Functional Partners:
BACCAP_00793
Macro domain protein (260 aa)
    0.991
BACCAP_00792
4Fe-4S binding domain protein (214 aa)
 
          0.950
nadE
NAD+ synthase (641 aa)
   
  0.874
BACCAP_00791
Riboflavin transporter ; Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (187 aa)
              0.781
BACCAP_04640
Hydrolase, HD family (389 aa)
   
  0.718
BACCAP_03218
DnaK family protein (437 aa)
     
  0.717
BACCAP_02789
Heat shock protein 70 ; Acts as a chaperone (619 aa)
     
  0.717
BACCAP_01521
Heat shock protein 70 ; Acts as a chaperone (572 aa)
     
  0.717
BACCAP_02740
Inosine-guanosine phosphorylase ; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (274 aa)
   
    0.680
dnaJ
Chaperone protein DnaJ ; 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-dependent interactions between DnaJ, [...] (387 aa)
   
    0.679
Your Current Organism:
Pseudoflavonifractor capillosus
NCBI taxonomy Id: 411467
Other names: Bacillus capillosus, Bacteroides capillosus, Bacteroides capillosus ATCC 29799, P. capillosus, P. capillosus ATCC 29799, Pseudobacterium capillosum, Pseudoflavonifractor, Pseudoflavonifractor Carlier et al. 2010, Pseudoflavonifractor capillosus, Pseudoflavonifractor capillosus ATCC 29799, Pseudoflavonifractor capillosus str. ATCC 29799, Pseudoflavonifractor capillosus strain ATCC 29799, Ristella capillosa
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