STRINGSTRING
lysC protein (Midichloria mitochondrii) - STRING interaction network
"lysC" - Aspartokinase in Midichloria mitochondrii
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Edges represent protein-protein associations
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
lysCAspartokinase (398 aa)    
Predicted Functional Partners:
midi_00488
Aspartate-semialdehyde dehydrogenase (335 aa)
 
 
  0.995
secY
Preprotein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (445 aa)
     
 
  0.916
dapA
Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta- semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- tetrahydrodipicolinate (HTPA) (294 aa)
 
   
  0.868
dapB
Dihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy- tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate (254 aa)
 
   
  0.861
aspB
Aspartate/tyrosine/aromatic aminotransferase (401 aa)
   
  0.849
midi_00489
Aspartate kinase (374 aa)
   
   
 
0.830
midi_00492
Putative diaminopimelate decarboxylase (253 aa)
   
 
  0.822
dapD
2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase (243 aa)
   
   
  0.780
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 (859 aa)
   
   
  0.662
midi_00318
Amino acid transporter (482 aa)
     
 
  0.640
Your Current Organism:
Midichloria mitochondrii
NCBI taxonomy Id: 696127
Other names: C. Midichloria, C. Midichloria mitochondrii, C. Midichloria mitochondrii IricVA, Candidatus Midichloria, Candidatus Midichloria mitochondrii, Candidatus Midichloria mitochondrii IricVA, Candidatus Midichloria mitochondrii str. IricVA, Candidatus Midichloria mitochondrii strain IricVA, Ixodes ricinus endosymbiont, Ixodes ricinus endosymbiont 1 (IricES1), Midichloria, Midichloria mitochondrii, Midichloria mitochondrii IricVA, endosymbiont of Ixodes ricinus
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