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
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glnDprotein-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 metabolism. (872 aa)    
Predicted Functional Partners:
glnB
Nitrogen regulatory protein P-II; COG: COG0347; Pfam: PF00543; InterPro: IPR015867; Belongs to the P(II) protein family.
 
 
 0.985
glnE
Putative bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase; 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 [...]
 
   
 0.766
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.
  
    0.664
mviN
Integral membrane protein MviN; Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
 
   
 0.473
glnA
Glutamine synthetase, type I; COG: COG0174; Pfam: PF03951,PF00120; InterPro: IPR004809.
 
   
 0.460
erpA
Iron-sulfur cluster assembly accessory protein; Required for insertion of 4Fe-4S clusters for at least IspG.
       0.436
EEX50317.1
Hypothetical protein; COG: COG3112; Pfam: PF06062; InterPro: IPR008249; Belongs to the UPF0231 family.
       0.436
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
 
   
 0.433
Your Current Organism:
Pasteurella dagmatis
NCBI taxonomy Id: 667128
Other names: P. dagmatis ATCC 43325, Pasteurella dagmatis ATCC 43325, Pasteurella dagmatis str. ATCC 43325, Pasteurella dagmatis strain ATCC 43325
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