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
pyrHUridylate kinase; Catalyzes the reversible phosphorylation of UMP to UDP, with ATP or dATP as the most efficient phosphate donors. Is also able to phosphorylate 5-fluoro-UMP and 6-aza-UMP. (240 aa)    
Predicted Functional Partners:
frr
Ribosome recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family.
  
 0.999
tsf
Elongation factor Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity); Belongs to the EF-Ts family.
  
 0.995
rpsB
Ribosomal protein S2; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.
 
  
 0.985
upp
Uracil phosphoribosyltransferase; Catalyzes the conversion of uracil and 5-phospho-alpha-D- ribose 1-diphosphate (PRPP) to UMP and diphosphate.
  
 
 0.970
pyrF
Orotidine 5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP); Belongs to the OMP decarboxylase family. Type 1 subfamily.
  
 
 0.958
udk
Uridine kinase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme.
   
 
 0.958
pyrR
Transcriptional attenuator and uracil phosphoribosyltransferase activity; Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes; Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.
   
 
 0.939
ndk
Nucleoside diphosphate kinase; Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate; Belongs to the NDK family.
  
 
 0.937
yfkN
Exported 2',3'-cyclic-nucleotide 2'-phosphodiesterase, 2' (or 3') nucleotidase and 5' nucleotidase; Catalyzes the release of inorganic phosphate from 2',3'- cyclic nucleotides through consecutive 2',3'-phosphodiesterase and 3'- (or 2') nucleotidase activities. Also possesses a 5'-nucleotidase activity. Does not catalyze the release of inorganic phosphate from 3',5'-cyclic nucleotides. Probably plays a role in the cellular reprocessing of nucleotides present in the medium, under conditions of phosphate shortage.
   
 
  0.900
pyrG
CTP synthetase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
  
  
 0.892
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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