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
PTH_0793Predicted phosphoesterase. (157 aa)    
Predicted Functional Partners:
PTH_0792
Xanthosine triphosphate pyrophosphatase; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family.
  
  
 0.954
Rph
RNase PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
  
    0.846
ElaC
Metal-dependent hydrolases; Beta-lactamase superfamily III.
 
     0.730
PTH_1236
Hypothetical protein; Containing COG0517and COG0617 domains; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.
  
 
 0.678
HgdB-2
benzoyl-CoA reductase/2-hydroxyglutaryl-CoA dehydratase subunit; BcrC/BadD/HgdB.
       0.569
PTH_0789
Activator of 2-hydroxyglutaryl-CoA dehydratase; HSP70-class ATPase domain.
  
    0.564
PTH_0142
Hypothetical protein; Containing predicted ATPase (COG3899), FhlA, FOG: GAF domain (COG2203), S_TKc, serine/threonine protein kinases, catalytic domain, His Kinase A (phosphoacceptor), HATPase_c, Histidine kinase-like ATPase, REC, signal receiver domain, and ArcB, FOG: HPt domain (COG2198).
     
 0.491
MurI
Glutamate racemase; Provides the (R)-glutamate required for cell wall biosynthesis.
       0.461
TopA
Topoisomerase IA; 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 superco [...]
       0.428
ribBA
GTP cyclohydrolase II and 3,4-dihydroxy-2-butanone 4-phosphate synthase; Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate; In the C-terminal section; belongs to the GTP cyclohydrolase II family.
       0.428
Your Current Organism:
Pelotomaculum thermopropionicum
NCBI taxonomy Id: 370438
Other names: P. thermopropionicum SI, Pelotomaculum thermopropionicum SI, Pelotomaculum thermopropionicum str. SI, Pelotomaculum thermopropionicum strain SI
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.