STRINGSTRING
rbpA protein (Synechocystis sp. PCC6803) - STRING interaction network
"rbpA" - RNA binding protein in Synechocystis sp. PCC6803
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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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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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[Homology]
Score
rbpARNA binding protein (101 aa)    
Predicted Functional Partners:
crhR
ATP-dependent RNA helicase DeaD; An ATP-dependent bidirectional RNA helicase with RNA- dependent ATPase activity; does not unwind dsDNA, uses only (d)ATP (PubMed-15542859). Also has ATP-dependent RNA annealing activity; concurrent annealing and helicase activity promote strand-exchange activity (PubMed-15542859). In vitro has low helicase processivity, annealing processivity is probably higher (PubMed-15542859). Required for correct cold adaptation, probably by aiding translation of mRNAs required for photosynthesis and electron transport (PubMed-22575444). Probably regulates the cold- [...] (492 aa)
   
  0.944
fusA
Elongation factor EF-G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity) (695 aa)
     
    0.918
sll0830
Elongation factor EF-G (669 aa)
     
    0.918
fusB
Elongation factor EF-G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity) (691 aa)
     
    0.918
sll0408
Hypothetical protein; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Required for the assembly and stabilization of PSII (By similarity) (402 aa)
     
  0.886
slr1251
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (171 aa)
     
  0.886
sll0227
Peptidyl-prolyl cis-trans isomerase B; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (246 aa)
     
  0.886
pnp
Polyribonucleotide nucleotidyltransferase; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3’- to 5’-direction (718 aa)
     
 
  0.812
rplW
50S ribosomal protein L23; One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome (101 aa)
     
  0.774
rplO
50S ribosomal protein L15; Binds to the 23S rRNA (147 aa)
     
  0.764
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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