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dksA protein (Klebsiella pneumoniae) - STRING interaction network
"dksA" - C4-type zinc finger protein, DksA/TraR family in Klebsiella pneumoniae
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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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
dksAC4-type zinc finger protein, DksA/TraR family; Derived by automated computational analysis using gene prediction method- Protein Homology (151 aa)    
Predicted Functional Partners:
rpoZ
DNA-directed RNA polymerase subunit omega; Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta’ subunit thereby facilitating its interaction with the beta and alpha subunits (91 aa)
 
 
  0.981
rpoA
DNA-directed RNA polymerase subunit alpha; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (329 aa)
   
 
 
  0.955
JG24_26820
DNA-directed RNA polymerase beta’ subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Subunit beta’ binds to sigma factor allowing it to bind to the -10 region of the promoter; Derived by automated computational analysis using gene prediction method- Protein Homology (1407 aa)
   
 
 
  0.953
JG24_30165
This tRNA synthetase lacks the tRNA anticodon interaction domain; instead this enzyme modifies tRNA(Asp) with glutamate by esterifying glutamate to the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of queosine generating a modified nucleoside at the first anticodon position of tRNAAsp; the modified tRNA does not bind elongation factor Tu; Derived by automated computational analysis using gene prediction method- Protein Homology; Belongs to the class-I aminoacyl-tRNA synthetase family (293 aa)
       
  0.943
rpoB
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates; beta subunit is part of the catalytic core which binds with a sigma factor to produce the holoenzyme; Derived by automated computational analysis using gene prediction method- Protein Homology (1342 aa)
   
 
 
  0.929
pcnB
Polymerase that creates the 3’ poly(A) tail found in some mRNA’s; Derived by automated computational analysis using gene prediction method- Protein Homology (453 aa)
     
  0.917
rpoD
RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (613 aa)
   
 
  0.885
rpoS
RNA polymerase sigma factor RpoS; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released; this sigma factor controls a regulon of genes required for protection against external stresses; Derived by automated computational analysis using gene prediction method- Protein Homology (330 aa)
       
 
  0.771
greB
Transcription elongation factor GreB; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3’terminus. GreB releases sequences of up to 9 nucleotides in length (157 aa)
     
 
  0.722
greA
Transcription elongation factor GreA; Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3’terminus. GreA releases sequences of 2 to 3 nucleotides (158 aa)
   
 
  0.695
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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