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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
fmnPRiboflavin transporter FmnP; Mediates uptake of riboflavin and roseoflavin, a toxic riboflavin analog; may also transport FMN. 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 (By similarity); Belongs to the prokaryotic riboflavin transporter (P- RFT) (TC 2.A.87) family (190 aa)    
Predicted Functional Partners:
thiT
Thiamine transporter ThiT; Probably a thiamine-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 (By similarity); Belongs to the vitamin uptake transporter (VUT/ECF) (TC 2.A.88) family. Thiamine transporter subfamily
  
   
 0.924
bioY
Probable biotin transporter BioY; Probable biotin transporter
      
 0.856
ecfAB
Energy-coupling factor transporter ATP-binding protein EcfA2; ATP-binding (A) component of a common 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
 
   
 0.830
ribC
Riboflavin biosynthesis protein RibC; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the RibF family
      
 0.820
ecfT
Energy-coupling factor transporter transmembrane protein EcfT; Transmembrane (T) component of an 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 (By similarity). Involved in riboflavin transport
 
   
 0.818
ribE
Riboflavin synthase; Catalyzes the dismutation of two molecules of 6,7- dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil
     
 0.807
naiP
Putative niacin/nicotinamide transporter NaiP; Probably involved in the uptake of amidated and deamidated forms of niacin. Increases the growth rate of E.coli that is unable to make niacin de novo; confers increased sensitivity to the toxic niacin analog 6-amino-nicotinamide to wild-type E.coli. There is probably another mechanism for niacin uptake
      
 0.760
ribD
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5'-phosphate; In the C-terminal section; belongs to the HTP reductase family
     
 0.742
ribH
6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8- ribityllumazine by condensation of 5-amino-6-(D- ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Is able to use the non-natural R enantiomer of 3,4-dihydroxy-2- butanone 4-phosphate as a substrate, but with less efficiency than the natural S enantiomer. Cannot use unphosphorylated 3,4- dihydroxy-2-butanone, 3,4-dihydroxy-2-butanone 3-phosphate or diacetyl as substrates
  
  
 0.737
ypzK
Protein RibT; Involved in riboflavin biosynthesis
 
   
 0.690
Your Current Organism:
Bacillus subtilis
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis, Bacillus subtilis 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (4%) [HD]