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
Acel_1009Cell division-specific peptidoglycan biosynthesis regulator FtsW; TIGRFAM: cell division protein FtsW; PFAM: cell cycle protein; KEGG: fra:Francci3_1414 cell cycle protein; Belongs to the SEDS family. (411 aa)    
Predicted Functional Partners:
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.
  
 0.998
Acel_1004
Peptidoglycan synthetase FtsI; PFAM: penicillin-binding protein, transpeptidase; Penicillin-binding protein, dimerisation domain; KEGG: fra:Francci3_1409 peptidoglycan glycosyltransferase.
 
 0.994
Acel_0020
Cell elongation-specific peptidoglycan D,D-transpeptidase; PFAM: penicillin-binding protein, transpeptidase; KEGG: fra:Francci3_4434 peptidoglycan glycosyltransferase.
 
 0.987
murC
UDP-N-acetylmuramate--L-alanine ligase; Cell wall formation; Belongs to the MurCDEF family.
 
  
 0.986
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.
  
 0.983
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.
 
 
 0.980
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.
 
  
 0.962
murE
UDP-N-acetylmuramoylalanyl-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.
 
  
 0.951
ftsZ
Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.
 
 
 0.915
Acel_0751
Peptidoglycan glycosyltransferase; PFAM: penicillin-binding protein, transpeptidase; Penicillin-binding protein, dimerisation domain; KEGG: sco:SCO2608 penicillin binding protein.
 
 0.820
Your Current Organism:
Acidothermus cellulolyticus
NCBI taxonomy Id: 351607
Other names: A. cellulolyticus 11B, Acidothermus cellulolyticus 11B, Acidothermus cellulolyticus str. 11B, Acidothermus cellulolyticus strain 11B
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.