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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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from curated databases
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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ntrCNitrogen regulation protein NR(I); Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes. (470 aa)    
Predicted Functional Partners:
ntrB
Nitrogen regulation protein NR(II); Identified by similarity to SP:P06712; match to protein family HMM PF00512; match to protein family HMM PF02518; match to protein family HMM TIGR00229.
 0.997
rpoN
RNA polymerase sigma-54 factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
 
   
 0.918
lexA
LexA repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
  
   
 0.694
glnD
protein-P-II 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.
  
   
 0.689
nusB
N utilization substance protein B; Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons.
  
   
 0.663
glnA
Glutamine synthetase, type I; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia; Belongs to the glutamine synthetase family.
  
  
 0.651
glnE
Glutamate-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 [...]
      
 0.643
amt-1
Ammonium transporter; Identified by match to protein family HMM PF00909; match to protein family HMM TIGR00836.
   
  
 0.630
amt-2
Ammonium transporter; Identified by match to protein family HMM PF00909; match to protein family HMM TIGR00836.
   
  
 0.630
amt-3
Ammonium transporter; Identified by match to protein family HMM PF00909; match to protein family HMM TIGR00836.
   
  
 0.630
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
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