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
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ftsZCell 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. (403 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
AEF86757.1
MutL protein; Identified by match to protein family HMM TIGR01319.
  
 
 0.949
AEF85114.1
MutL protein; Identified by match to protein family HMM TIGR01319.
  
 
 0.949
murG
Undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; 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.
 
 
 0.895
topA
DNA topoisomerase; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA superc [...]
 
   
 0.884
hslU
Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
  
 
 0.868
AEF83606.1
Putative cell division protein FtsQ; Essential cell division protein.
  
  
 0.864
AEF84097.1
Stage V sporulation protein E; Identified by match to protein family HMM PF01098; Belongs to the SEDS family.
 
 
 0.854
AEF85172.1
Integrase/recombinase XerD; Identified by match to protein family HMM PF00589; match to protein family HMM PF02899; Belongs to the 'phage' integrase family.
     
 0.796
xerC
Site-specific recombinase, phage integrase family; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
     
 0.795
Your Current Organism:
Treponema primitia ZAS2
NCBI taxonomy Id: 545694
Other names: T. primitia ZAS-2, Treponema primitia ZAS-2, Treponema primitia str. ZAS-2, Treponema primitia strain ZAS-2, Treponema sp. ZAS-2
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