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greB protein (Methylobacter tundripaludum) - STRING interaction network
"greB" - Transcription elongation factor GreB 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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greBTranscription 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 (166 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 (81 aa)
 
 
  0.818
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 (337 aa)
 
 
 
  0.800
rpoC
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1397 aa)
   
 
 
  0.783
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 (1364 aa)
   
 
 
  0.782
guaB
Inosine-5’-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth; Belongs to the IMPDH/GMPR family (488 aa)
     
  0.770
Mettu_1405
Methionine synthase; TIGRFAM- 5-methyltetrahydrofolate--homocysteine methyltransferase; KEGG- mca-MCA1545 B12-dependent methionine synthase; PFAM- Homocysteine S-methyltransferase; Dihydropteroate synthase, DHPS; Methionine synthase, cobalamin (vitamin B12)-binding module, cap; Cobalamin (vitamin B12)-binding; Vitamin B12 dependent methionine synthase, activation region (1226 aa)
       
  0.758
Mettu_0901
Riboflavin biosynthesis protein RibD; Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5’-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)- pyrimidinedione 5’-phosphate; In the C-terminal section; belongs to the HTP reductase family (361 aa)
         
  0.606
nusG
Transcription termination/antitermination protein NusG; Participates in transcription elongation, termination and antitermination (177 aa)
   
   
  0.601
gmk
Guanylate kinase; Essential for recycling GMP and indirectly, cGMP (204 aa)
 
 
    0.595
Mettu_3581
KEGG- cja-CJA_1627 FKBP-type peptidyl-prolyl cis-trans isomerase; PFAM- Peptidyl-prolyl cis-trans isomerase, FKBP-type (159 aa)
              0.593
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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