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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
alrAla racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (376 aa)    
Predicted Functional Partners:
murF
D-ala-d-ala adding enzyme; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily.
   
 0.988
ddl
D-alanine-d-alanine ligase; Cell wall formation.
 
 
 0.977
acpS
Holo-acyl-carrier protein; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family.
 
  
 0.977
dltA
D-alanine-D-alanyl carrier protein 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 [...]
    
 0.931
murI
Gluracemase; Provides the (R)-glutamate required for cell wall biosynthesis.
 
   
 0.911
dltC
D-alanyl carrier protein; 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.
    
 0.908
thyA
Thymidylate synthase; Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by- product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
     
 0.845
LBA1695
Aspartate aminotransferase.
    
 0.831
mscL
Channel protein; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
     
 0.823
murD
UDP-N-acetylmuramoylalanine-D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.
 
 
 
 0.813
Your Current Organism:
Lactobacillus acidophilus
NCBI taxonomy Id: 272621
Other names: L. acidophilus NCFM, Lactobacillus acidophilus NCFM, Lactobacillus acidophilus str. NCFM, Lactobacillus acidophilus strain NCFM
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.