STRINGSTRING
sll0227 protein (Synechocystis sp. PCC6803) - STRING interaction network
"sll0227" - Peptidyl-prolyl cis-trans isomerase B in Synechocystis sp. PCC6803
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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
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
sll0227Peptidyl-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)    
Predicted Functional Partners:
rbpA
RNA binding protein (101 aa)
     
  0.886
slr0193
RNA-binding protein (151 aa)
     
  0.886
ssr1480
RNA-binding protein (83 aa)
     
  0.886
speB1
Arginase (306 aa)
   
        0.861
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)
   
  0.824
sll0830
Elongation factor EF-G (669 aa)
   
  0.810
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)
   
  0.810
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)
 
  0.794
dnaK2
DnaK protein; Acts as a chaperone (636 aa)
 
  0.791
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 3’ to 5’ and 5’ to 3’ exonuclease activity (986 aa)
 
  0.785
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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