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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
glnDUridylyltransferase; 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 assimilation and metabolism. (882 aa)    
Predicted Functional Partners:
glnB
Nitrogen regulatory protein P-II.1; Belongs to the P(II) protein family.
 
 
 0.985
glnK
Nitrogen regulatory protein P-II 2; Belongs to the P(II) protein family.
 
 
 
 0.859
glnE
Glutamate-ammonia-ligase adenylyltransferase (glutamine-synthetase adenylyltransferase) (ATASE); 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. Th [...]
 
   
 0.847
gltB
Glutamate synthase [NADPH] large chain precursor (glutamate synthase alpha subunit) (NADPH-GOGAT) (GLTS alpha chain).
 
   
 0.760
glnL
Nitrogen regulation protein.
  
 
 
 0.680
glnA
Glutamine synthetase (glutamate--ammonia ligase).
 
   
 0.670
dapD
2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family.
     
 0.662
map
Methionine aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
  
    0.653
amtB
Probable ammonium transport protein AmtB.
 
   
 0.638
yaeT
Probable outer membrane protein precursor YaeT; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.
 
    0.551
Your Current Organism:
Photorhabdus laumondii
NCBI taxonomy Id: 243265
Other names: P. laumondii subsp. laumondii TTO1, Photorhabdus laumondii subsp. laumondii TTO1, Photorhabdus luminescens subsp. laumondii TTO1
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