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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
oatAAcyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (627 aa)    
Predicted Functional Partners:
yitT
tyrosyl-tRNA synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.789
PgdA
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.788
sigV
RNA polymerase subunit sigma; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the sigma-70 factor family. ECF subfamily.
   
  
 0.783
dltA
Alanine-phosphoribitol ligase; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP-dependent A [...]
  
   
 0.610
mprF
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.568
mprF-3
lysyl-tRNA synthetase; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
 
   
 0.567
aspS
aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
       0.549
patB
Aminotransferase class I/II; Derived by automated computational analysis using gene prediction method: Protein Homology.
      
 0.547
AOM17290.1
Rhamnogalacturonan acetylesterase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.545
mprF-2
Hypothetical protein; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
 
   
 0.515
Your Current Organism:
Enterococcus faecium
NCBI taxonomy Id: 1352
Other names: ATCC 19434, CCUG 542, CFBP 4248, CIP 103014, DSM 20477, E. faecium, JCM 5804, JCM 8727, LMG 11423, LMG:11423, NBRC 100485, NBRC 100486, NCDO 942, NCIMB 11508, NCTC 7171, Streptococcus faecium
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