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.
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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.
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Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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yjaDPutative NTP pyrophosphohydrolases containing a Zn-finger; Probably nucleic-acid-binding; NADH pyrophosphatase. (SW:NUDC_SALTY). (257 aa)    
Predicted Functional Partners:
cobB
Putative nicotinate-nucleotide dimethylbenzimidazolephosphoribosltransferase; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form (By similarity). Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Overexpression compensates for a cobT deletion, suggesting it may have [...]
  
  0.917
pncB
Nicotinate phosphoribosyltransferase; Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
    
 0.912
surE
Survival protein, protein damage control; Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates with highest affinity to 3'-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3'-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs.
   
 
  0.910
mazG
Putative pyrophosphatase; Similar to E. coli orf, hypothetical protein (AAC75823.1); Blastp hit to AAC75823.1 (263 aa), 93% identity in aa 2 - 263.
     
 0.908
nadD
Putative nicotinic acid mononucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
     
 0.906
nadE
NAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
  
 
 0.905
ushA
UDP-sugar hydrolase 5'-nucleotidase; Silent protein USHA(0) precursor. (SW:USHA_SALTY); Belongs to the 5'-nucleotidase family.
    
  0.903
ygaD
Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC75742.1); Blastp hit to AAC75742.1 (165 aa), 92% identity in aa 1 - 165; Belongs to the CinA family.
   
 
 0.903
nadR
Trifunctional protein; This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the A [...]
   
 
 0.902
yfjB
Putative kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates as a source of phosphorus. NADH cannot replace NAD as a substrate.
     
 0.901
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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