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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
AQG72930.1Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (379 aa)    
Predicted Functional Partners:
acpS
ACP synthase; Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein; Belongs to the P-Pant transferase superfamily. AcpS family.
 
  
 0.993
murF
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D- alanine ligase; 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.
  
 0.985
ddl
D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
  
 
 0.966
dltA
D-alanine--poly(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-de [...]
    
 0.921
dltC
D-alanine--poly(phosphoribitol) ligase subunit 2; 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.
    
 0.904
AQG71563.1
tRNA threonylcarbamoyladenosine biosynthesis protein TsaE; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.815
murC
UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
 
 
 0.797
murI
Glutamate racemase; Provides the (R)-glutamate required for cell wall biosynthesis; Belongs to the aspartate/glutamate racemases family.
 
   
 0.768
coaD
Phosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4'- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. Belongs to the bacterial CoaD family.
 
  
 0.730
dapB
4-hydroxy-tetrahydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family.
  
 
 0.729
Your Current Organism:
Lactobacillus rhamnosus
NCBI taxonomy Id: 47715
Other names: ATCC 7469, CCUG 21452, CIP A157, DSM 20021, IFO 3425, L. rhamnosus, LMG 6400, LMG:6400, Lactobacillus casei rhamnosus, Lactobacillus casei subsp. rhamnosus, Lactobacillus sp. NCIM 2587, Lactobacillus sp. W6, Lactobacillus sp. X9, NBRC 3425, NCAIM B.01147, NCCB 46033, NCDO 243, NCIB 6375, NCIMB 6375, NCTC 12953, NCTC 13764, NRRL B-442, VKM B-574
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