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
OAR05570.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (204 aa)    
Predicted Functional Partners:
OAR05571.1
Hypothetical protein; 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.
 
  
 0.981
OAR05569.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.553
ispE
4-diphosphocytidyl-2-C-methyl-D-erythritol kinase; Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
 
     0.480
OAR04679.1
Hypothetical protein; Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein.
  
     0.458
OAR05572.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
     0.445
OAR05503.1
Hypothetical protein; Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins; Belongs to the prokaryotic riboflavin transporter (P-RFT) (TC 2.A.87) family.
  
     0.441
rph
Ribonuclease 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.
  
    0.439
SA87_02105
Uncharacterized protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
    0.429
OAR04549.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.421
OAR04538.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the CtsR family.
  
     0.420
Your Current Organism:
Hydrogenibacillus schlegelii
NCBI taxonomy Id: 1484
Other names: ATCC 43741, Bacillus schlegelii, CCUG 26017, CIP 106933, DSM 2000, H. schlegelii, LMG 7133, LMG:7133, strain MA 48
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.