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
KWZ74860.1Ppx/GppA phosphatase family protein; KEGG: rsa:RSal33209_0335 7.9e-65 exopolyphosphatase K01524; Psort location: Cytoplasmic, score: 9.97. (309 aa)    
Predicted Functional Partners:
KWZ74859.1
Hypothetical protein; KEGG: mlu:Mlut_05000 3.1e-38 exopolyphosphatase; K01524 exopolyphosphatase / guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase; Psort location: Cytoplasmic, score: 7.50.
 
 
  0.992
KWZ72072.1
GTP diphosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
  
 
 0.931
aroB
3-dehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
 
 
 
  0.916
ppk
Polyphosphate kinase 1; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family.
 
  
 0.907
KWZ74858.1
Septum formation initiator; Psort location: CytoplasmicMembrane, score: 8.16.
  
  
 0.871
eno
Phosphopyruvate hydratase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family.
       0.640
KWZ73122.1
KEGG: pak:HMPREF0675_4130 1.0e-64 polyphosphate:nucleotide phosphotransferase, PPK2 family; Psort location: Cytoplasmic, score: 7.50.
 
  
 0.528
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
     
 0.491
mfd
Transcription-repair coupling factor; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site; In the C-terminal section; belongs to the helicase family. RecG subfamily.
       0.443
pth
aminoacyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family.
       0.440
Your Current Organism:
Winkia neuii
NCBI taxonomy Id: 33007
Other names: ATCC 51847, Actinomyces neuii, CCUG 32252, CIP 104015, DSM 8576, W. neuii, strain 97/90
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.