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aspS aspS pet112 pet112 hisS hisS G07_orf479 G07_orf479 alaS alaS gatA gatA proS proS D09_orf451 D09_orf451 efp efp pheT pheT valS valS
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
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gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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aspSaspartyl-tRNA synthetase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (557 aa)    
Predicted Functional Partners:
pet112
Glu-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); Belongs to the GatB/GatE family. GatB subfamily.
 
 
 0.993
hisS
histidyl-tRNA synthetase; MPN045(new), 109(Himmelreich et al., 1996).
  
  
 0.949
G07_orf479
Glu-tRNA amidotransferase subunit C; MPN236(new), 596(Himmelreich et al., 1996); contains unknown TM contacting N terminal domain.
  
 
 0.948
alaS
alanyl-tRNA synthetase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.843
gatA
Glu-tRNA 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).
 
 
 0.814
proS
Putative prolyl-tRNA synthetase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
  
  
 0.810
D09_orf451
Nicotinate phosphoribosyl transferase-like protein; MPN047(new), 107(Himmelreich et al., 1996); Belongs to the NAPRTase family.
       0.774
efp
Elongation factor P; Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase (By similarity).
  
  
 0.747
pheT
phenylalanyl-tRNA synthetase beta chain; MPN106(new), 049(Himmelreich et al., 1996); Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
 
  
 0.742
valS
valyl-tRNA synthetase; 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.
  
  
 0.733
Your Current Organism:
Mycoplasma pneumoniae M129
NCBI taxonomy Id: 272634
Other names: M. pneumoniae M129, Mycoplasma pneumoniae ATCC 29342, Mycoplasma pneumoniae str. M129, Mycoplasma pneumoniae strain M129
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