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
uvrCUvrABC system protein 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. (607 aa)    
Predicted Functional Partners:
uvrB
Excinuclease UvrABC protein 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 dissocia [...]
 0.997
uvrA
Excinuclease (uvrABC system protein A); The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate.
 
 0.958
uvrY
Two-componenent system BarA/UvrY - regulatory subunit; Function of homologous gene experimentally demonstrated in an other organism; regulator; Transcription.
 
  
 0.944
PP_3087
Putative excinuclease ABC subunit A; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
 
 
 0.846
pgsA
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Fattyacidandphospholipidmetabolism : Biosynthesis; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
  
  
 0.840
recN
Factor used in recombination and DNA repair; May be involved in recombinational repair of damaged DNA.
  
   
 0.821
PP_4100
Transcriptional regulator, Cro/CI family.
  
  
 0.793
uvrD
DNA-dependent ATPase I and helicase II, nucleotide Excision Repair Complex; Function of homologous gene experimentally demonstrated in an other organism; enzyme; DNAmetabolism : DNA replication, recombination, and repair.
 
  
 0.761
sulA
Cell division inhibitor SulA; Component of the SOS system and an inhibitor of cell division. Accumulation of SulA causes rapid cessation of cell division and the appearance of long, non-septate filaments. In the presence of GTP, binds a polymerization-competent form of FtsZ in a 1:1 ratio, thus inhibiting FtsZ polymerization and therefore preventing it from participating in the assembly of the Z ring. This mechanism prevents the premature segregation of damaged DNA to daughter cells during cell division.
      
 0.738
radA
DNA repair enzyme; 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.
 
  
 0.733
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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