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
bacAPutative undecaprenol kinase (bacitracin resistance protein); Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family. (281 aa)    
Predicted Functional Partners:
mraY
Putative undecaprenyl-phosphate-UDP-MurNAc-pentapeptide transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily.
 
 
 0.947
uppS
Putative undecaprenyl pyrophosphate synthetase; Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
   
 
 0.946
dagK
Diacylglycerol kinase; Catalyzes the phosphorylation of undecaprenol, which is probably the primary physiological substrate. Is also able to phosphorylate diacylglycerol, albeit with very low efficiency. May play a role in adaptability to environmental stress conditions such as acid tolerance, elevated temperatures and high osmolarity. Belongs to the bacterial diacylglycerol kinase family.
   
 
 0.944
SMU_1702c
Putative phosphatase; Best Blastp Hit: gb|AAC45388.1| (U81488) putative phosphatidic acid phosphatase [Lactococcus lactis subsp. cremoris].
  
 
 0.916
rgpG
Putative glycosyl transferase N-acetylglucosaminyltransferase), RgpG; Best Blastp Hit: dbj|BAA82114.1| (AB022909) RgpG [Streptococcus mutans].
  
  
 0.754
murE
Putative UDP-N-acetylmuramoylananine-D-glutamate-2,6- diaminopimelate ligase; Catalyzes the addition of L-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
  
  
 0.736
mecA
Putative negative regulator of genetic competence MecA; Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis.
  
  
 0.730
murG
Putative MurG; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily.
  
  
 0.681
SMU_243
Conserved hypothetical protein; Best Blastp Hit: gb|AAA22769.1| (M83944) subtilin [Bacillus subtilis] >gi|143565|gb|AAA22775.1| (M99263) spaD [Bacillus subtilis].
       0.645
glmU
Putative UDP-N-acetylglucosamine pyrophosphorylase; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C- terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N- acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5- triphosphate), a reaction catalyzed by the N-terminal domain. In the C-terminal section; belongs to the transferase hexapeptide repeat family.
  
  
 0.633
Your Current Organism:
Streptococcus mutans
NCBI taxonomy Id: 210007
Other names: S. mutans UA159, Streptococcus mutans UA159, Streptococcus mutans str. UA159
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