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 [...]

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 [...]

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.

ATP-dependent DNA helicase, RecQ family; COGs: COG0514 Superfamily II DNA helicase; InterProIPR018329: IPR014001: IPR001650: IPR014021: IPR 011545: IPR018982; KEGG: psl:Psta_2965 ATP-dependent DNA helicase, RecQ family; PFAM: DEAD/DEAH box helicase domain protein; helicase domain protein; RQC domain; SMART: DEAD-like helicase; helicase domain protein; SPTR: ATP-dependent DNA helicase, RecQ family; TIGRFAM: ATP-dependent DNA helicase, RecQ family; PFAM: Helicase conserved C-terminal domain; RQC domain; DEAD/DEAH box helicase; TIGRFAM: ATP-dependent DNA helicase, RecQ family.

DNA ligase, NAD-dependent; 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.

DNA topoisomerase I; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...]

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.

COGs: COG0749 DNA polymerase I - 3'-5' exonuclease and polymerase domains; InterProIPR020046: IPR020047: IPR001098: IPR002421: IPR 008918: IPR002298: IPR018320: IPR019760; KEGG: plm:Plim_3011 DNA polymerase I; PFAM: DNA-directed DNA polymerase; 5'-3' exonuclease, N-terminal resolvase-like domain; 5'-3' exonuclease, SAM-fold domain; SMART: DNA-directed DNA polymerase; 5'-3' exonuclease; Helix-hairpin-helix domain protein class 2; SPTR: DNA polymerase I; TIGRFAM: DNA polymerase I; PFAM: 5'-3' exonuclease, C-terminal SAM fold; 5'-3' exonuclease, N-terminal resolvase-like domain; DNA polym [...]

DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.