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rpoB protein (Methylobacter tundripaludum) - STRING interaction network
"rpoB" - Transcriptase subunit beta in Methylobacter tundripaludum
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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
rpoBTranscriptase subunit beta ; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1364 aa)    
Predicted Functional Partners:
rpoC
Transcriptase subunit beta’ ; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1397 aa)
  0.999
rpoA
Transcriptase subunit alpha ; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (337 aa)
 
  0.999
nusG
Transcription termination/antitermination protein NusG ; Participates in transcription elongation, termination and antitermination (177 aa)
 
  0.997
rpoD
Sigma-70 ; 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 (602 aa)
 
 
  0.997
rpoZ
Transcriptase 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 (81 aa)
   
  0.996
Mettu_1336
Elongation factor 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 (698 aa)
 
  0.994
pyrG
UTP--ammonia ligase ; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (543 aa)
     
  0.993
Mettu_2595
Elongation factor 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 (694 aa)
 
  0.990
rpsE
30S ribosomal protein S5 ; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body (168 aa)
   
   
  0.989
rpsC
30S ribosomal protein S3 ; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (223 aa)
 
   
  0.988
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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