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uvrB protein (Methylobacter tundripaludum) - STRING interaction network
"uvrB" - Excinuclease ABC subunit B in Methylobacter tundripaludum
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Gene Fusion
Cooccurence
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[Homology]
Score
uvrBExcinuclease 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 dissociate [...] (670 aa)    
Predicted Functional Partners:
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 (613 aa)
  0.999
uvrA
Excinuclease ABC subunit 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 (938 aa)
 
  0.999
Mettu_2642
DNA helicase (725 aa)
 
 
  0.970
rep
ATP-dependent DNA helicase Rep ; Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3’ to 5’ direction (667 aa)
 
 
  0.966
clpP
Endopeptidase Clp ; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (215 aa)
       
 
  0.878
Mettu_2187
DNA polymerase I (930 aa)
 
     
  0.876
recA
Recombinase A ; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (345 aa)
 
   
  0.855
ligA
Polydeoxyribonucleotide synthase [NAD(+)] ; DNA ligase that catalyzes the formation of phosphodiester linkages between 5’-phosphoryl and 3’-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA (654 aa)
 
 
  0.810
lexA
LexA repressor ; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair (211 aa)
         
  0.805
dnaA
Chromosomal replication initiator protein DnaA ; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (438 aa)
   
   
  0.791
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum, M. tundripaludum SV96, Methylobacter, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum Wartiainen et al. 2006, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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