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gatB protein (Synechocystis sp. PCC6803) - STRING interaction network
"gatB" - glutamyl-tRNA(Gln) amidotransferase subunit B in Synechocystis sp. PCC6803
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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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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gatBglutamyl-tRNA(Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity) (495 aa)    
Predicted Functional Partners:
gatA
glutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln) (By similarity) (483 aa)
 
  0.999
gatC
Hypothetical protein; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp- tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity) (104 aa)
 
  0.996
sll0828
6-aminohexanoate-cyclic-dimer hydrolase (468 aa)
 
  0.996
asnS
asparaginyl-tRNA synthetase (462 aa)
   
  0.994
aspS
aspartyl-tRNA synthetase; 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- aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn) (599 aa)
  0.977
pth
peptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis (194 aa)
     
 
    0.972
gltX
glutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (483 aa)
 
  0.962
prfB
Peptide chain release factor; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (335 aa)
     
 
    0.656
sll1069
Beta ketoacyl-acyl carrier protein synthase; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates (416 aa)
     
   
  0.642
topA
DNA topoisomerase I; 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 super [...] (898 aa)
         
  0.635
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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