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
ddlD-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (350 aa)    
Predicted Functional Partners:
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.
 
 0.996
murB
UDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation.
  
 0.980
murC
UDP-N-acetylmuramate--L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
  
 0.976
APX71213.1
Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family.
 
 
 0.963
dltA
D-alanine--poly(phosphoribitol) ligase subunit 1; 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 [...]
   
 
 0.942
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.
   
 
 0.906
murE
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
 
  
 0.850
divIB
Hypothetical protein; Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex; Belongs to the FtsQ/DivIB family. DivIB subfamily.
 
  
 0.813
murD
UDP-N-acetylmuramoyl-L-alanine--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.
 
  
 0.785
ftsA
Cell division protein FtsA; Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. Belongs to the FtsA/MreB family.
  
  
 0.762
Your Current Organism:
Lactobacillus allii
NCBI taxonomy Id: 1847728
Other names: JCM 31938, KCTC 21077, L. allii, Lactobacillus allii Jung et al. 2017, Lactobacillus sp. WiKim39, strain WiKim39
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.