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
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. (612 aa)    
Predicted Functional Partners:
uvrB
UvrABC system 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 dissociate and [...]
 0.996
uvrA_2
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.
 
 0.949
uvrA_1
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.
 
 0.923
uvrY_1
Response regulator UvrY.
    
 0.922
pgsA
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family.
     
 0.870
uvrD_3
DNA helicase II.
 
  
 0.807
recN
DNA repair protein RecN; May be involved in recombinational repair of damaged DNA.
 
   
 0.755
polA
DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.
 
   
 0.727
recR
Recombination protein RecR; May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
 
 
 
 0.724
radA
Hypothetical 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.
 
  
 0.708
Your Current Organism:
Pseudomonas fluorescens
NCBI taxonomy Id: 294
Other names: ATCC 13525, Bacillus fluorescens, Bacillus fluorescens liquefaciens, Bacterium fluorescen, CCEB 546, CFBP 2102, CIP 69.13, DSM 50090, IAM 12022, IFO 14160, JCM 5963, Liquidomonas fluorescens, NBRC 14160, NCCB 76040, NCIB 9046, NCIB:9046, NCIMB 9046, NCTC 10038, NRRL B-14678, P. fluorescens, Pseudomonas sp. AU2390, Pseudomonas sp. BZ64, Pseudomonas sp. FY32, Pseudomonas sp. HSA2/2016, Pseudomonas sp. HSA3/2016, Pseudomonas sp. ISSDS-433, Pseudomonas sp. JCM 17186, Pseudomonas sp. JCM 2779, Pseudomonas sp. KH-20150KS3, Pseudomonas sp. LBUM223, Pseudomonas sp. LBUM636, Pseudomonas sp. SM2/2016, RH 818, VKM B-894, bacterium P1-1, strain M. Rhodes 28/5
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