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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
dusHistidine phosphokinase/phophatase (ntrB); Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. (340 aa)    
Predicted Functional Partners:
tatD1
Conserved hypothetical protein; Similar to GB:L42023 SP:P44718 PID:1003792 PID:1222386 PID:1204704 percent identity: 36.17; identified by sequence similarity; putative.
       0.852
proS
prolyl-tRNA synthetase (proS); Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and invol [...]
  
 
 0.801
polA
DNA polymerase I (polA); In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
 
 
 0.724
metG
methionyl-tRNA synthetase (metG); Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
     
 0.703
TP_0939
Pyruvate oxidoreductase; Similar to PID:1001780 SP:P52965 PID:1006618 percent identity: 58.44; identified by sequence similarity; putative.
  
  
 0.625
truA
Pseudouridylate synthase (hisT); Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
  
 
 0.622
TP_0982
glpG protein, putative; Similar to GP:606359 percent identity: 29.47; identified by sequence similarity; putative.
       0.607
TP_0981
Sensory transduction histidine kinase, putative; Similar to PID:1652841 percent identity: 33.93; identified by sequence similarity; putative.
       0.592
truB
tRNA pseudouridine 55 synthase (truB); Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
  
  
 0.577
gyrB
DNA gyrase, subunit B (gyrB); A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
     
 0.565
Your Current Organism:
Treponema pallidum
NCBI taxonomy Id: 243276
Other names: T. pallidum subsp. pallidum str. Nichols, Treponema pallidum Nichols, Treponema pallidum subsp. pallidum str. Nichols
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