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
fadELong-chain fatty acid--CoA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (509 aa)    
Predicted Functional Partners:
fadB
3-hydroxyacyl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the enoyl-CoA hydratase/isomerase family.
 
 
 0.952
fadD
glutaryl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.939
vraA
Long-chain fatty acid--CoA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.928
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 [...]
 
0.910
fadX
CoA-transferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the 3-oxoacid CoA-transferase family.
  
  
 0.843
fadA
acetyl-CoA acetyltransferase; Catalyzes the synthesis of acetoacetyl coenzyme A from two molecules of acetyl coenzyme A. It can also act as a thiolase, catalyzing the reverse reaction and generating two-carbon units from the four-carbon product of fatty acid oxidation; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family.
 
 
 0.830
AKS72691.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.800
AKS72792.1
Lipase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.800
geh
Lipase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.800
AKS74619.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ATP-dependent AMP-binding enzyme family.
 
 
0.737
Your Current Organism:
Staphylococcus schleiferi
NCBI taxonomy Id: 1295
Other names: ATCC 43808, CCUG 25351, CIP 103643, DSM 4807, LMG 13347, LMG:13347, NCTC 12218, NRRL B-14775, S. schleiferi, strain N850274
Server load: high (88%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.