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
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Textmining
[Homology]
Score
adaBO6-methylguanine-DNA methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. (179 aa)    
Predicted Functional Partners:
adaA
methylphosphotriester-DNA alkyltransferase and transcriptional regulator (AraC/XylS family); Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs the methylphosphotriester lesions in DNA by a direct and irreversible transfer of the methyl group to one of its own cysteine residues.
  
 0.999
alkA
DNA-3-methyladenine glycosylase; Is involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Catalyzes the hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine and 7- methylguanine from the damaged DNA polymer formed by alkylation lesions.
  
  
 0.966
aag
3-alkylated purines and hypoxanthine DNA glycosidase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the DNA glycosylase MPG family.
     
 0.929
queG
Epoxyqueuosine reductase; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
 
    0.913
uvrB
Excinuclease ABC (subunit B); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociat [...]
     
 0.522
ykuK
Putative RNAse; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
   
  
 0.483
nhaX
Stress response protein, UspA family; Evidence 2b: Function of strongly homologous gene; factor.
  
    0.461
yxiE
Phosphate starvation protein (universal stress protein A family); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor; Belongs to the universal stress protein A family.
  
    0.461
dinG
Damage inducible ATP-dependent 3'->5' nuclease; 3'-5' exonuclease.
     
 0.456
uvrC
Excinuclease ABC (subunit C); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
  
  
 0.450
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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