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rpoC protein (Methylobacter tundripaludum) - STRING interaction network
"rpoC" - 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
rpoCTranscriptase subunit beta’ ; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1397 aa)    
Predicted Functional Partners:
rpoB
Transcriptase subunit beta ; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1364 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)
 
  0.998
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)
   
  0.998
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)
 
 
  0.992
rpsG
30S ribosomal protein S7 ; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA (156 aa)
 
 
  0.976
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)
 
  0.973
topA
DNA topoisomerase I ; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] (772 aa)
     
 
  0.969
pnp
Polynucleotide phosphorylase ; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3’- to 5’-direction (692 aa)
   
 
  0.969
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)
     
  0.966
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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