close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
AOM16318.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (267 aa)    
Predicted Functional Partners:
ysdC
Peptidase M28; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.893
AOM16317.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.858
lplJ
Lipoate--protein ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.838
DsbG
Thioredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.540
dltD_1
D-alanyl transfer protein DltD; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.490
dltC
Cytochrome C552; Carrier protein involved in the D-alanylation of lipoteichoic acid (LTA). The loading of thioester-linked D-alanine onto DltC is catalyzed by D-alanine--D-alanyl carrier protein ligase DltA. The DltC- carried D-alanyl group is further transferred to cell membrane phosphatidylglycerol (PG) by forming an ester bond, probably catalyzed by DltD. 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.
       0.485
pip
Phage infection protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.423
AOM16395.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.420
dltB
Alanine transporter; Could be involved in the transport of activated D-alanine through the membrane.
       0.412
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 [...]
       0.408
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
Server load: low (34%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.