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
OBX07304.1Purine nucleoside phosphoramidase; Derived by automated computational analysis using gene prediction method: Protein Homology. (115 aa)    
Predicted Functional Partners:
uppP
UDP pyrophosphate phosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the UppP family.
       0.728
ubiD
3-octaprenyl-4-hydroxybenzoate carboxy-lyase; Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
       0.691
msrP
TMAO/DMSO reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) [...]
   
  0.671
OBX09239.1
Lipoprotein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.617
tal
Transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
  
   0.534
leuS
leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase; Derived by automated computational [...]
 
 
   0.516
msrA
Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
  
  0.477
rppH
RNA pyrophosphohydrolase; Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage; Belongs to the Nudix hydrolase family. RppH subfamily.
  
 0.473
nudB
Catalyzes the formation of dihydroneopterin phosphate from dihydroneopterin triphosphate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.473
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
   
  0.470
Your Current Organism:
Gallibacterium salpingitidis
NCBI taxonomy Id: 505341
Other names: CCUG 15564, CCUG 36325, G. salpingitidis, Gallibacterium salpingitidis Bisgaard et al. 2009, Gallibacterium sp. 18469/18, Gallibacterium sp. 19987/2, Gallibacterium sp. BK1010/1, Gallibacterium sp. F150, NCTC 11414, strain F150
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