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:
some 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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[Homology]
Score
moeBMolybdopterin-synthase adenylyltransferase; Adenylyltransferase involved in the biosynthesis of several sulfur compounds. Is required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T). This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures. TtuC catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein TtuB. Is also involved in the biosynthesis of thiamine, mol [...] (271 aa)    
Predicted Functional Partners:
TT_C1947
annotation not available
 0.999
TT_C0087
annotation not available
 
 0.993
TT_C1835
annotation not available
 
 
 0.938
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP)
  
 0.929
ttuB
Sulfur carrier protein; Required for the 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T) . This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is essential for cell growth at high temperatures . Thiocarboxylated TtuB functions as the sulfur donor in the sulfurtransferase reaction catalyzed by TtuA TtuB also functions as a protein modifier covalently attached to lysine residues of the target proteins TtuA and TtuC . TtuB conjugation might play a regulatory role t [...]
  
 
 0.925
thiG
Thiazole biosynthesis protein thig; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S
 
  
 0.884
ttuA
TRNA-5-methyluridine54 2-sulfurtransferase; Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2- thiouridine (m(5)s(2)U or s(2)T) . This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures . TtuA transfers the S atom from the thiocarboxylated C-terminus of TtuB to tRNA
  
 
 0.878
TT_C1609
Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for proces [...]
  
 
  0.818
TT_C1133
Hypothetical protein; Probable metalloprotease that cleaves the ubiquitin-like modifier protein TtuB from protein conjugates, hydrolyzing the isopeptide bond between a lysine residue of the target protein and the C-terminal glycine of the modifier protein. Does not seem to work for all the TtuB conjugates
  
 
 0.815
moeA
Molybdopterin biosynthesis moea protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP
  
 0.806
Your Current Organism:
Thermus thermophilus HB27
NCBI taxonomy Id: 262724
Other names: T. thermophilus HB27, Thermus thermophilus str. HB27, Thermus thermophilus strain HB27
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