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
SGO_0599Phosphoprotein phosphatase; Identified by match to protein family HMM PF00481. (246 aa)    
Predicted Functional Partners:
SGO_0600
Serine/threonine protein kinase; Identified by match to protein family HMM PF00069; match to protein family HMM PF03793.
 
 0.999
sun
Sun protein; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA.
  
  
 0.971
SGO_1130
Dihydrolipoamide dehydrogenase; Identified by match to protein family HMM PF00070; match to protein family HMM PF00364; match to protein family HMM PF01134; match to protein family HMM PF02852; match to protein family HMM PF07992; match to protein family HMM TIGR01350.
  
 0.955
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
  
   0.944
priA
Primosomal protein N'; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily.
 
    0.831
dnaJ
DnaJ chaparone 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-dependent interactions between DnaJ, D [...]
  
   0.691
deoB
Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family.
      
 0.670
SGO_1132
Acetoin dehydrogenase; Identified by match to protein family HMM PF02779; match to protein family HMM PF02780.
   
 0.637
tig
Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.
   
 
 0.608
tpiA
Triosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family.
      
 0.594
Your Current Organism:
Streptococcus gordonii
NCBI taxonomy Id: 467705
Other names: S. gordonii str. Challis substr. CH1, Streptococcus gordonii ATCC 35105, Streptococcus gordonii str. Challis substr. CH1, Streptococcus gordonii str. Challis substr. DL1, Streptococcus gordonii str. Challis substr. V288
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