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mfd protein (Pelagibaca bermudensis) - STRING interaction network
"mfd" - Transcription-repair-coupling factor in Pelagibaca bermudensis
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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mfdTranscription-repair-coupling factor ; Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site (1158 aa)    
Predicted Functional Partners:
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 (958 aa)
 
 
  0.986
mutL
DNA mismatch repair protein MutL ; 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 (621 aa)
   
   
  0.927
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 (626 aa)
 
 
  0.916
mutS
DNA mismatch repair protein MutS ; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity (874 aa)
   
   
  0.892
recA
Protein RecA ; 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 (213 aa)
   
 
 
  0.868
ruvC
Holliday junction resolvase RuvC ; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5’-terminal phosphate and a 3’-terminal hydroxyl group (163 aa)
   
     
  0.865
R2601_08246
Recombination protein N ; May be involved in recombinational repair of damaged DNA (553 aa)
 
 
  0.855
fpg
DNA-(apurinic or apyrimidinic site) lyase MutM ; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3’- and 5’-phosphates (283 aa)
   
     
  0.839
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 dissociate [...] (732 aa)
   
   
  0.826
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 (231 aa)
 
   
  0.824
Your Current Organism:
Pelagibaca bermudensis
NCBI taxonomy Id: 314265
Other names: P. bermudensis HTCC2601, Pelagibaca, Pelagibaca Cho and Giovannoni 2006, Pelagibaca bermudensis, Pelagibaca bermudensis Cho and Giovannoni 2006, Pelagibaca bermudensis HTCC2601, Pelagibaca bermudensis str. HTCC2601, Pelagibaca bermudensis strain HTCC2601, Roseovarius sp. HTCC2601
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