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pheS protein (Bordetella pertussis Tohama) - STRING interaction network
"pheS" - phenylalanyl-tRNA synthetase subunit alpha in Bordetella pertussis Tohama
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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pheSphenylalanyl-tRNA synthetase subunit alpha; catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a heterotetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 1 subfamily (340 aa)    
Predicted Functional Partners:
pheT
phenylalanyl-tRNA synthetase subunit beta; catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily (805 aa)
  0.999
metG
Methionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation (692 aa)
   
 
  0.970
thrS
Threonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction- L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr) (649 aa)
 
 
  0.929
ihfA
Integration host factor subunit alpha; This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control (113 aa)
   
   
  0.887
valS
Valine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily (960 aa)
 
   
  0.869
lepA
Elongation factor 4; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back- translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner (597 aa)
 
   
  0.860
hisS
Histidine--tRNA ligase; histidyl-tRNA synthetase; catalyzes a two-step reaction, first charging a histidine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; class II aminoacyl-tRNA synthetase; forms homodimers; some organisms have a paralogous gene, hisZ, that is similar to hisS and produces a protein that performs the first step in histidine biosynthesis along with HisG (434 aa)
 
 
  0.848
rplB
50S ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (275 aa)
   
   
  0.837
aspS
Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps- L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily (596 aa)
   
   
  0.832
rpsH
30S ribosomal protein S8; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit (131 aa)
   
   
  0.824
Your Current Organism:
Bordetella pertussis Tohama
NCBI taxonomy Id: 257313
Other names: B. pertussis Tohama I, Bordetella pertussis Tohama, Bordetella pertussis Tohama I
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