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dapB protein (Granulibacter bethesdensis) - STRING interaction network
"dapB" - 4-hydroxy-tetrahydrodipicolinate reductase in Granulibacter bethesdensis
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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dapB4-hydroxy-tetrahydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy- tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family (261 aa)    
Predicted Functional Partners:
dapD
annotation not available (280 aa)
 
 
  0.994
dapA
4-hydroxy-tetrahydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta- semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- tetrahydrodipicolinate (HTPA) (329 aa)
 
 
  0.991
murJ
Probable lipid II flippase MurJ; Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane (513 aa)
              0.813
lysA
Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine (448 aa)
 
   
  0.789
ABI61498.1
annotation not available (409 aa)
   
  0.720
asd
Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L- aspartyl-4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family (345 aa)
 
   
  0.679
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6- diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan (275 aa)
 
   
  0.675
ABI63305.1
S-adenosylhomocysteine nucleosidase (242 aa)
   
        0.627
ABI62332.1
annotation not available (541 aa)
 
   
  0.609
dnaJ
Chaperone protein DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] (376 aa)
 
   
  0.593
Your Current Organism:
Granulibacter bethesdensis
NCBI taxonomy Id: 391165
Other names: G. bethesdensis CGDNIH1, Granulibacter bethesdensis, Granulibacter bethesdensis CGDNIH1, Granulibacter bethesdensis str. CGDNIH1, Granulibacter bethesdensis strain CGDNIH1
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