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
ftsQCell division protein (ftsQ); Essential cell division protein. (271 aa)    
Predicted Functional Partners:
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.
  
 
 0.997
murF
UDP-N-acetylmuramoylalanyl-D-glutamyl-2, 6-diaminopimelate--D-alanyl-D-alanine ligase (murF); 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.
  
 
 0.994
ftsW
Cell division protein (ftsW); Similar to PID:1165286 SP:Q44775 PID:1223601 PID:1223610 PID:1234873 percent identity: 34.57; identified by sequence similarity; putative; Belongs to the SEDS family.
  
 
 0.992
ftsK
Cell division protein, putative; Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination (By similarity). Belongs to the FtsK/SpoIIIE/SftA family.
   
 
 0.980
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.
  
  
 0.969
TP_0181
Predicted coding region TP0181; Hypothetical protein; identified by Glimmer; putative.
   
 
 0.966
murD
UDP-N-acetylmuramoylalanine--D-glutamate ligase (murD); Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family.
  
  
 0.966
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.
  
  
 0.960
pbp2
Penicillin-binding protein (pbp-3); Similar to GB:AE000783 percent identity: 30.81; identified by sequence similarity; putative.
 
 
 0.959
pbp1
Penicillin-binding protein (pbp-1); Similar to GB:AE000783 percent identity: 37.14; identified by sequence similarity; putative.
  
 
 0.952
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.