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slr1251 protein (Synechocystis sp. PCC6803) - STRING interaction network
"slr1251" - Peptidyl-prolyl cis-trans isomerase 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]
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slr1251Peptidyl-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)    
Predicted Functional Partners:
hslO
Hypothetical protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress (302 aa)
           
  0.940
ytfC
FKBP-type peptidyl-prolyl cis-trans isomerase (201 aa)
 
 
 
  0.929
rbpA
RNA binding protein (101 aa)
     
  0.886
slr0193
RNA-binding protein (151 aa)
     
  0.886
ssr1480
RNA-binding protein (83 aa)
     
  0.886
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)
   
  0.810
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
dnaK3
DnaK protein; Acts as a chaperone (771 aa)
 
  0.804
dnaK2
DnaK protein; Acts as a chaperone (636 aa)
 
  0.803
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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