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
glnEGlutamine-synthetase 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 transducti [...] (937 aa)    
Predicted Functional Partners:
glnA
Forms a homododecamer; forms glutamine from ammonia and glutamate with the conversion of ATP to ADP and phosphate; also functions in the assimilation of ammonia; highly regulated protein controlled by the addition/removal of adenylyl groups by adenylyltransferase from specific tyrosine residues; addition of adenylyl groups results in inactivation of the enzyme; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.822
glnD
Bifunctional uridylyltransferase/uridylyl-removing protein; 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 metabolism.
 
   
 0.801
APC02370.1
ATP-dependent helicase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.611
APC01928.1
Acyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.610
APC01927.1
Membrane-like protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.606
APC00244.1
Glutamate synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.579
argA
N-acetylglutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the acetyltransferase family. ArgA subfamily.
 
   
 0.531
APC00603.1
Alkyl hydroperoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.507
tldD
Metalloprotease TldD; Responsible for the proteolytic maturation of the E. coli pMccB17 plasmid-encoded microcin B17, an exported protein that targets the essential topoisomerase II DNA gyrase; degrades the E. coli plasmid F-encoded CcdA; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.507
nadE
NAD+ synthase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
     
 0.484
Your Current Organism:
Polynucleobacter asymbioticus
NCBI taxonomy Id: 576611
Other names: Burkholderiaceae bacterium KF022, Burkholderiaceae bacterium KF023, Burkholderiaceae bacterium KF032, Burkholderiaceae bacterium KF040, Burkholderiaceae bacterium KF041, Burkholderiaceae bacterium KF042, Burkholderiaceae bacterium KF043, Burkholderiaceae bacterium KF046, Burkholderiaceae bacterium KF047, Burkholderiaceae bacterium KF069, Burkholderiaceae bacterium KF071, Burkholderiaceae bacterium KF072, CIP 109841, DSM 18221, P. asymbioticus, Polynucleobacter asymbioticus (Hahn et al. 2009) Hahn et al. 2016, Polynucleobacter necessarius subsp. asymbioticus, Polynucleobacter necessarius subsp. asymbioticus Hahn et al. 2009, Polynucleobacter sp. INAWF005, Polynucleobacter sp. INAWF006, Polynucleobacter sp. INAWF008, Polynucleobacter sp. INAWF009, Polynucleobacter sp. INAWF010, Polynucleobacter sp. INAWF011, Polynucleobacter sp. INAWF012, Polynucleobacter sp. INBF001, Polynucleobacter sp. MWH-Creno-4A3, Polynucleobacter sp. MWH-Creno-4D65, Polynucleobacter sp. MWH-Mekk-C4, Polynucleobacter sp. MWH-Mekk-D4, Polynucleobacter sp. MWH-NZ4W7a, Polynucleobacter sp. MWH-P1sevC1, Polynucleobacter sp. P1-KOL8, Polynucleobacter sp. QLW-P1DMWA-2, Polynucleobacter sp. QLW-P1DNSYA-1, Polynucleobacter sp. QLW-P1DNSYA-2, Polynucleobacter sp. QLW-P1FAT50D-2, Polynucleobacter sp. QLW-P1FMW50A-1, Polynucleobacter sp. QLW-P1FNSY20A-6, Polynucleobacter sp. SHIRF001, Polynucleobacter sp. SHIRF002, Polynucleobacter sp. SHIRF003, Polynucleobacter sp. SHIRF004, Polynucleobacter sp. SHIRF005, Polynucleobacter sp. SHIRF006, Polynucleobacter sp. SHIRF007, Polynucleobacter sp. SHIRF008, Polynucleobacter sp. SHIRF009, Polynucleobacter sp. SHIRF010, Polynucleobacter sp. SHIRF011, Polynucleobacter sp. SHIRF012, Polynucleobacter sp. SHIRF013, Polynucleobacter sp. SHIRF014, Polynucleobacter sp. SHIRF015, Polynucleobacter sp. SHIRF016, Polynucleobacter sp. SHIRF017, Polynucleobacter sp. SHIRF018, Polynucleobacter sp. SHIRF019, Polynucleobacter sp. SUWAF015, Polynucleobacter sp. SUWAF016, Polynucleobacter sp. TEGAF008, Polynucleobacter sp. TEGF001, Polynucleobacter sp. UF003, Polynucleobacter sp. UF009, Polynucleobacter sp. USHIF002, Polynucleobacter sp. USHIF003, Polynucleobacter sp. USHIF004, Polynucleobacter sp. USHIF007, Polynucleobacter sp. USHIF009, Polynucleobacter sp. USHIF010, Polynucleobacter sp. USHIF011, Polynucleobacter sp. USHIF012, beta proteobacterium MWH-HuK1, beta proteobacterium MWH-T1W11, strain QLW-P1DMWA-1
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