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
ftsLCell division protein FtsL; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. (105 aa)    
Predicted Functional Partners:
fstQ
Cell division protein FtsQ; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
 
 
 0.994
ftsB
Septum formation initiator; Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic.
  
 
 
 0.973
ftsI
Penicillin-binding protein, transpeptidase domain protein; Catalyzes cross-linking of the peptidoglycan cell wall at the division septum; Belongs to the transpeptidase family. FtsI subfamily.
 
 
 0.941
mraW
S-adenosyl-methyltransferase MraW; Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
  
  
 0.933
ftsW
Cell division protein FtsW; Peptidoglycan polymerase that is essential for cell division. Belongs to the SEDS family. FtsW subfamily.
  
 
 0.866
PlpE
Hypothetical protein.
  
 
 0.844
murE
UDP-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.
 
  
 0.834
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.
  
  
 0.778
rseA
Anti sigma-E protein RseA domain protein; An anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic pro [...]
  
 
   0.769
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.
  
    0.764
Your Current Organism:
Pasteurella dagmatis
NCBI taxonomy Id: 667128
Other names: P. dagmatis ATCC 43325, Pasteurella dagmatis ATCC 43325, Pasteurella dagmatis str. ATCC 43325, Pasteurella dagmatis strain ATCC 43325
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.