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
AQS00463.1Host cell surface-exposed lipoprotein. (201 aa)    
Predicted Functional Partners:
fruA_3
PTS system fructose-specific EIIABC component.
 
     0.523
pfkA1
6-phosphofructokinase 1; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.
   
    0.446
pfkA
6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
   
    0.446
rplD
50S ribosomal protein L4; Forms part of the polypeptide exit tunnel.
  
    0.443
pheT
phenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
       0.435
pfp
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
   
    0.426
Your Current Organism:
Clostridium saccharobutylicum
NCBI taxonomy Id: 169679
Other names: ATCC BAA-117, C. saccharobutylicum, Clostridium saccharobutylicum Keis et al. 2001, DSM 13864, strain NCP 262
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