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
AKS72999.1N-succinyldiaminopimelate aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology. (388 aa)    
Predicted Functional Partners:
metH
Homocysteine methyltransferase; Catalyzes the formation of 5,10-methylenetetrahydrofolate from 5-methyltetrahydrofolate and S-adenosyl-L-homocysteine and methionine from S-adenosyl-L-methionine and L-homocysteine; expressed in B. subtilis under methionine starvation conditions; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.944
metK
S-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
 0.924
metE
5-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
   
 
 0.909
AKS73371.1
Free methionine-(R)-sulfoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.900
AKS72998.1
Multidrug transporter; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family.
  
    0.748
AKS73175.1
Hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.559
gltB
Glutamate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.506
fmhB
Aminoacyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.486
AKS73366.1
Aminotransferase class V; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.480
serA
D-3-phosphoglycerate dehydrogenase; Catalyzes the formation of 3-phosphonooxypyruvate from 3-phospho-D-glycerate in serine biosynthesis; can also reduce alpha ketoglutarate to form 2-hydroxyglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.
 
 
 0.469
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: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.