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
murEUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. (470 aa)    
Predicted Functional Partners:
murF
Hypothetical protein; 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.
 
0.999
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.
 
0.997
murC
UDP-N-acetylmuramate--alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
  
0.995
AMW34831.1
Penicillin-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.987
mraY
phospho-N-acetylmuramoyl-pentapeptide- transferase; First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan; Belongs to the glycosyltransferase 4 family. MraY subfamily.
 
  
 0.974
murG
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily.
 
 
 0.973
ddl
D-alanine--D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family.
 
  
 0.944
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan.
    
 0.932
AMW34827.1
Cell division protein FtsW; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the SEDS family.
 
  
 0.930
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine.
     
 0.915
Your Current Organism:
Haematospirillum jordaniae
NCBI taxonomy Id: 1549855
Other names: CCUG 66838, DSM 28903, H. jordaniae, Haematospirillum jordaniae Humrighouse et al. 2016, Rhodospirillaceae bacterium H2509, Rhodospirillaceae bacterium H2784, Rhodospirillaceae bacterium H3173, Rhodospirillaceae bacterium H3694, Rhodospirillaceae bacterium H4485, Rhodospirillaceae bacterium H4555, Rhodospirillaceae bacterium H4833, Rhodospirillaceae bacterium H4890, Rhodospirillaceae bacterium H5569, Rhodospirillaceae bacterium H5791, Rhodospirillaceae bacterium H5945, Rhodospirillaceae bacterium H6167, Rhodospirillaceae bacterium H6172, Rhodospirillaceae bacterium H6179, strain H5569
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.