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
KRM89748.1HTH containing DNA-binding domain and MocR-like aminotransferase. (394 aa)    
Predicted Functional Partners:
KRM89749.1
LysR family transcriptional regulator; Belongs to the LysR transcriptional regulatory family.
 
  
 0.740
KRM88782.1
Transport protein.
    
 0.698
trpA
Tryptophan synthase; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
   
 
 0.614
dltA
D-alanine-activating enzyme; 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 AMP [...]
   
 
 0.600
KRM86293.1
Prephenate dehydrogenase.
    
 0.591
KRM89155.1
Bifunctional acetaldehyde-CoA alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
  
 
 0.581
pyrC
Dihydroorotase; Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate; Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class I DHOase subfamily.
   
 0.576
KRM88703.1
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family.
  
 0.569
aroE
Shikimate dehydrogenase 1; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
   
 
 0.563
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
   
 
 0.562
Your Current Organism:
Lactobacillus vini
NCBI taxonomy Id: 1133569
Other names: L. vini DSM 20605, Lactobacillus sp. CECT 5924, Lactobacillus sp. DSM 20605, Lactobacillus vini CECT 5924, Lactobacillus vini DSM 20605, Lactobacillus vini str. DSM 20605, Lactobacillus vini strain DSM 20605
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