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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glnDBifunctional uridylyltransferase/uridylyl-removing enzyme; 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. (878 aa)    
Predicted Functional Partners:
glnB
Nitrogen regulatory protein P-II 1; Belongs to the P(II) protein family.
 
 
 0.984
glnK
Nitrogen regulatory protein P-II 2; Belongs to the P(II) protein family.
 
 
 
 0.848
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 [...]
 
   
 0.803
dapD
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase; Belongs to the transferase hexapeptide repeat family.
     
 0.675
glnL
Nitrogen regulation protein NR(II).
  
 
 
 0.626
glnA
Glutamine synthetase.
 
   
 0.593
map_2
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.
  
    0.573
bamA_2
Outer membrane protein assembly factor BamA precursor; 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.
 
    0.447
cysG_2
Siroheme synthase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
  
   
 0.427
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP.
   
  
 0.412
Your Current Organism:
Providencia rettgeri
NCBI taxonomy Id: 587
Other names: ATCC 29944, Bacterium rettgeri, CCUG 14804, CIP 103182, DSM 4542, LMG 3259, LMG:3259, NCTC 11801, P. rettgeri, Proteus rettgeri, Shigella rettgeri
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