close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
Swol_0248C-terminal processing peptidase-2. Serine peptidase. MEROPS family S41A; KEGG: chy:CHY_0170 carboxyl-terminal protease; Belongs to the peptidase S41A family. (389 aa)    
Predicted Functional Partners:
Swol_0249
KEGG: chy:CHY_0171 hypothetical protein.
     
 0.679
Swol_0247
Peptidase M23B; KEGG: mta:Moth_0246 peptidase M23B.
 
  
 0.629
uvrB
Excinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...]
     
 0.621
uvrA
Excinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
     
 0.614
Swol_0250
Hypothetical protein; KEGG: mta:Moth_1766 ATPase.
       0.577
Swol_0558
KEGG: chy:CHY_1999 oxaloacetate decarboxylase, alpha subunit.
  
    0.476
Swol_0246
Cell division protein FtsX; Part of the ABC transporter FtsEX involved in asymmetric cellular division facilitating the initiation of sporulation. Belongs to the ABC-4 integral membrane protein family. FtsX subfamily.
 
     0.450
Swol_0890
KEGG: mta:Moth_1042 peptidase M50, putative membrane-associated zinc metallopeptidase.
 
  
 0.426
Swol_0659
KEGG: gme:Gmet_0815 PpiC-type peptidyl-prolyl cis-trans isomerase.
 
 
 0.409
uvrC
Excinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
  
    0.405
Your Current Organism:
Syntrophomonas wolfei Goettingen
NCBI taxonomy Id: 335541
Other names: S. wolfei subsp. wolfei str. Goettingen G311, Syntrophomonas wolfei str. Goettingen, Syntrophomonas wolfei subsp. wolfei Goettingen, Syntrophomonas wolfei subsp. wolfei str. Goettingen, Syntrophomonas wolfei subsp. wolfei str. Goettingen G311, Syntrophomonas wolfei subsp. wolfei str. Gottingen, Syntrophomonas wolfei subsp. wolfei strain Goettingen
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.