PFAM: UvrD/REP helicase; KEGG: fra:Francci3_3799 UvrD/REP helicase; Belongs to the helicase family. UvrD subfamily.

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 [...]

RecA protein; 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; Belongs to the RecA family.

PFAM: BRCT domain protein; Exonuclease, RNase T and DNA polymerase III; SMART: Exonuclease; KEGG: tfu:Tfu_0714 exonuclease.

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.

ATP-dependent DNA helicase, RecQ-like protein; PFAM: helicase domain protein; DEAD/DEAH box helicase domain protein; SMART: DEAD-like helicases-like; KEGG: sma:SAV2450 putative ATP-dependent DNA helicase.

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.

DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...]

DNA polymerase III, epsilon subunit; KEGG: fal:FRAAL5108 putative DNA-directed DNA polymerase; TIGRFAM: DNA polymerase III, epsilon subunit; PFAM: Excinuclease ABC, C subunit domain protein; UvrB/UvrC protein; Exonuclease, RNase T and DNA polymerase III; SMART: Exonuclease.