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
glnEGlutamate-ammonia-ligase adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transd [...] (985 aa)    
Predicted Functional Partners:
glnD
(protein-PII) uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
 
   
 0.928
glnA-2
L-glutamine synthetase; Evidence: Function of homologous gene experimentally demonstrated in an other organism; Localization: 2 : Cytoplasmic.
 
  
 0.868
BBta_3085
Putative two-component sensor histidine kinase; Putative heavy-metal sensor (Cu/Zn); Evidence: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
     
 0.810
BBta_0878
L-glutamine synthetase; GlnA4-like; Evidence: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the glutamine synthetase family.
  
  
 0.708
BBta_3191
L-glutamine synthetase; Evidence: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Localization: 2 : Cytoplasmic; Belongs to the glutamine synthetase family.
  
  
 0.708
glnII
L-glutamine synthetase; Evidence: Function of homologous gene experimentally demonstrated in an other organism; Localization: 2 : Cytoplasmic.
  
  
 0.584
BBta_3956
Hypothetical protein; Peroxiredoxin domain; Evidence: Similar to previously reported genes of unknown function.
      0.562
gltB
Glutamate synthase (NADH) large subunit; Evidence: Function of homologous gene experimentally demonstrated in an other organism; Localization: 2 : Cytoplasmic.
     
 0.543
BBta_3894
Putative sensor histidine kinase; Evidence: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
     
 0.512
BBta_4316
Histidine kinase; Modular protein; Evidence: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.
     
 0.512
Your Current Organism:
Bradyrhizobium sp. BTAi1
NCBI taxonomy Id: 288000
Other names: B. sp. BTAi1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.