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
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Textmining
[Homology]
Score
glnAGlutamine synthetase; Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA- binding active state and turns on the transcription of genes required for nitrogen assimilation. Under condi [...] (444 aa)    
Predicted Functional Partners:
glnR
Transcriptional regulator (nitrogen metabolism); Transcription repressor that represses many genes including ureABC and tnrA, during nitrogen excess. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, GlnR requires a DNA sequence of 17 nucleotides as minimal binding site.
 
 
 0.998
tnrA
Nitrogen sensing transcriptional regulator; Transcription regulator that actives the transcription of genes required for nitrogen assimilation such as nrgAB (ammonium transport), nasABCDEF (nitrate/nitrite assimilation), ureABC (urea degradation) and gabP (GABA transport), during nitrogen limitation. Also represses glnRA and gltAB in the absence of ammonium. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site.
 
 
 0.994
gltA
Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family.
  
 
 0.991
gltB
Glutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
 
 0.985
rocG
Glutamate dehydrogenase; Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression [...]
  
 
 0.979
glmS
L-glutamine-D-fructose-6-phosphate amidotransferase; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
 
 
 0.970
nasD
Assimilatory nitrite reductase subunit; Required for nitrite assimilation.
    
 0.969
nasB
Assimilatory nitrate reductase (electron transfer subunit NasB); Required for nitrate assimilation.
  
 
 0.958
amtB
Ammonium transporter; Functions as an ammonium and methylammonium transporter in the absence of glutamine. Required for ammonium utilization at low concentrations or at low pH values, when ammonium is the single nitrogen source. Required for binding of NrgB to the membrane. Interaction between GlnK-AmtB complex and TnrA protects TnrA from proteolytic degradation.
  
  
 0.958
gudB
Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...]
  
 
 0.956
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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