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
glnDUTP-GlnB uridylyltransferase, GlnD; 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. (843 aa)    
Predicted Functional Partners:
Slit_1653
PFAM: nitrogen regulatory protein P-II; KEGG: tmz:Tmz1t_1760 nitrogen regulatory protein P-II; Belongs to the P(II) protein family.
 
 
 0.968
map
Methionine aminopeptidase, type I; 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.
  
    0.793
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 tra [...]
 
   
 0.793
Slit_0065
PFAM: nitrogen regulatory protein P-II; KEGG: dar:Daro_0053 nitrogen regulatory protein P-II; Belongs to the P(II) protein family.
 
 
 
 0.701
Slit_2925
KEGG: mei:Msip34_2494 signal transduction histidine kinase, nitrogen specific, NtrB; PFAM: ATP-binding region ATPase domain protein; PAS fold-4 domain protein; histidine kinase A domain protein; SMART: ATP-binding region ATPase domain protein; histidine kinase A domain protein; PAS domain containing protein.
  
 
 
 0.654
Slit_0115
KEGG: mei:Msip34_2803 glutamate synthase (ferredoxin); PFAM: glutamate synthase; ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase alpha subunit domain protein.
     
 0.562
bamA
Outer membrane protein assembly complex, YaeT protein; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
    0.499
Slit_1661
KEGG: cvi:CV_0272 hypothetical protein.
       0.488
Slit_1664
PFAM: porin LamB type; KEGG: pna:Pnap_3690 maltoporin precursor.
       0.432
Slit_2923
KEGG: app:CAP2UW1_0248 glutamine synthetase, type I; TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase catalytic region; glutamine synthetase beta-Grasp.
 
   
 0.421
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus ES-1, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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