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
ogtO6-alkylguanine DNA alkyltransferase; 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. (165 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.
  
 0.992
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).
      0.906
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.
  
  
 0.886
kinE
Two-component sensor histidine kinase; Phosphorylates the sporulation-regulatory protein spo0A under biofilm growth conditions. Also able to weakly phosphorylate spo0F.
  
    0.830
mutY
A/G-specific adenine glycosylase or DNA-(apurinic or apyrimidinic site) lyase; Base excision repair (BER) glycosylase that initiates repair of A:oxoG to C:G by removing the inappropriately paired adenine base from the DNA backbone, generating an abasic site product. 8-oxoguanine (oxoG) is a genotoxic DNA lesion resulting from oxidation of guanine; this residue is misread by replicative DNA polymerases, that insert adenine instead of cytosine opposite the oxidized damaged base. Shows a powerful dicrimination of A versus C, since it does not cleave cytosine in oxoG:C pairs. May also be a [...]
 
   
 0.772
mutT
Putative NTP pyrophosphohydrolase; May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo- dGTP to the monophosphate (By similarity). Functions, in conjunction with ytkD, to protect vegetatively growing cells from DNA-damaging agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins do not [...]
     
 0.771
mutL
DNA mismatch repair factor; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). Overexpression of mutSL partially suppresses the high spontaneous mutation frequency of a ytkD/mutM/mutY triple disruption which lacks the system required to prevent damage by oxidized guanine (8-oxo [...]
   
 
 0.720
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 [...]
  
  
 0.602
ileS
isoleucyl-tRNA synthetase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
      0.600
radA
DNA repair protein; DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function.
  
  
 0.500
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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