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
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Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
rbfKRNA-binding cryptic riboflavin kinase regulatory protein; May be directly involved in the regulation of the rib genes. C-terminal part of RibR specifically binds to RFN of the rib leader of the riboflavin biosynthetic operon. The RFN element is a sequence within the rib-leader mRNA reported to serve as a receptor for an FMN- dependent riboswitch. Possibly, RibR produces the comodulator FMN through its own N-terminal flavokinase activity. FMN-activated RibR may stabilize the anti-anti terminator structure of RFN mRNA, causing transcription termination of the rib genes in trans. (230 aa)    
Predicted Functional Partners:
ytnM
Putative transporter; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
  
  
 0.980
ribC
Bifunctional riboflavin kinase FAD synthase; Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
  
  
0.946
ribE
Riboflavin synthase (alpha subunit); 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.
  
 
 0.937
ytmO
Putative monooxygenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To bacterial alkanal monooxygenase alpha and beta chains.
  
  
 0.921
nfrAB
NADPH-FMN oxidoreductase (nitroreductase); Reduces FMNH(2) to FMN, with NADH or NADPH as reductant. It also reduces nitroaromatic compounds, quinones, chromates and azo dyes. It could supply the reduced form of FMN to luciferase-like protein and contribute to the degradation of aromatic compounds. Belongs to the flavin oxidoreductase frp family.
    
 0.904
nfrAA
FMN-containing NADPH-linked nitro/flavin reductase; Reduces FMNH(2) to FMN, with NADPH as reductant. It also reduces nitroaromatic compounds, quinones and azo dyes.
    
 0.904
ytlI
Transcriptional regulator (LysR family); Positively regulates the expression of ytmI operon in response to the availability of sulfur sources.
  
  
 0.897
tcyK
Sulfur-containing amino acid ABC transporter binding lipoprotein; Part of the ABC transporter complex TcyJKLMN involved in L- cystine import. Is also involved in cystathionine, djenkolate, and S- methylcysteine transport; Belongs to the bacterial solute-binding protein 3 family.
  
  
 0.878
ytnJ
Putative monooxygenase; May play a role in methionine degradation. May play a role in a sulfur salvage pathway.
  
  
 0.859
ribH
6,7-dimethyl-8-ribityllumazine synthase, beta subunit; 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.
  
  
 0.854
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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