STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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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Cooccurrence
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Experiments
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[Homology]
Score
tsaDSecreted metalloendopeptidase Gcp, putative; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. (327 aa)    
Predicted Functional Partners:
tsaB
Conserved hypothetical protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity).
 
 
 0.996
TM_1632
Conserved hypothetical protein; Similar to GP:1945107 percent identity: 60.53; identified by sequence similarity; putative.
 
 
 0.972
clpX
ATP-dependent Clp protease, ATPase subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
       0.827
rsfS
Conserved hypothetical protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
       0.752
glmS
Glucosamine--fructose-6-phosphate aminotransferase, isomerizing; Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
       0.739
rpmF
Ribosomal protein L32; Similar to GB:AE000657 percent identity: 72.41; identified by sequence similarity; putative; Belongs to the bacterial ribosomal protein bL32 family.
     
 0.723
plsX
Fatty acid/phospholipid synthesis protein; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
  
    0.720
TM_0852
Conserved hypothetical protein; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
  
 
 0.712
TM_0151
Conserved hypothetical protein; Similar to GP:3006125 percent identity: 58.08; identified by sequence similarity; putative.
       0.700
rsmA
Dimethyladenosine transferase; Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
 
  
 0.602
Your Current Organism:
Thermotoga maritima
NCBI taxonomy Id: 243274
Other names: T. maritima MSB8, Thermotoga maritima DSM 3109, Thermotoga maritima MSB8, Thermotoga maritima str. MSB8, Thermotoga maritima strain MSB8
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.