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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
AEM77523.1PFAM: CobB/CobQ-like glutamine amidotransferase; KEGG: tbo:Thebr_0007 CobB/CobQ domain-containing protein glutamine amidotransferase. (243 aa)    
Predicted Functional Partners:
AEM77524.1
PFAM: Domain of unknown function DUF1727; Mur ligase, central; KEGG: tbo:Thebr_0008 hypothetical protein.
 0.999
murG
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily.
     
 0.903
AEM80023.1
KEGG: tbo:Thebr_2324 cyanophycin synthetase; TIGRFAM: Cyanophycin synthetase; PFAM: Mur ligase, central; Carbamoyl phosphate synthetase, large subunit, ATP-binding; ATP-grasp fold, RimK-type; Mur ligase, C-terminal; Belongs to the MurCDEF family.
  
 
 0.768
AEM78341.1
PFAM: Mur ligase, central; KEGG: tit:Thit_0772 Mur ligase middle domain-containing protein.
  
 
 0.751
murE
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily.
  
 
 0.751
AEM77525.1
Export-related chaperone CsaA; KEGG: tte:TTE0009 EMAP domain-containing protein; TIGRFAM: Secretion chaperone CsaA; PFAM: tRNA-binding region.
  
    0.696
gyrB
DNA topoisomerase IV, B subunit; 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.
       0.461
gyrA
DNA gyrase, A subunit; 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.
       0.445
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.