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TERTU_0175 protein (Teredinibacter turnerae) - STRING interaction network
"TERTU_0175" - Hypothetical protein in Teredinibacter turnerae
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second shell of interactors
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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
TERTU_0175Hypothetical protein (288 aa)    
Predicted Functional Partners:
gmk
Guanylate kinase; Essential for recycling GMP and indirectly, cGMP (205 aa)
 
   
  0.801
rph
Ribonuclease PH; Phosphorolytic exoribonuclease that removes nucleotide residues following the -CCA terminus of tRNA and adds nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates (239 aa)
 
        0.773
spoT
Guanosine-3’,5’-bis(diphosphate) 3’-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3’-diphosphate 5-’ diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance (704 aa)
   
        0.660
TERTU_0171
Endoribonuclease L-PSP (127 aa)
         
  0.657
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 (93 aa)
              0.646
TERTU_2824
Competence damage-inducible protein A (172 aa)
 
          0.569
rlmB
23S rRNA-methyltransferase RlmB; Specifically methylates the ribose of guanosine 2251 in 23S rRNA (247 aa)
 
        0.567
dapF
Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6- diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan (276 aa)
 
        0.548
rsmB
Ribosomal RNA small subunit methyltransferase B (433 aa)
 
        0.516
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (168 aa)
 
          0.510
Your Current Organism:
Teredinibacter turnerae
NCBI taxonomy Id: 377629
Other names: A. genera incertae sedis, Alteromonadales genera incertae sedis, T. turnerae, T. turnerae T7901, Teredinibacter, Teredinibacter Distel et al. 2002, Teredinibacter turnerae, Teredinibacter turnerae Distel et al. 2002, Teredinibacter turnerae T7901, Teredinibacter turnerae str. T7901, Teredinibacter turnerae strain T7901
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