COGs: COG0847 DNA polymerase III epsilon subunit and related 3'-5' exonuclease; InterPro IPR013520:IPR001357:IPR006055; KEGG: clj:CLJU_c36230 putative exonuclease with a BRCT domain; PFAM: Exonuclease, RNase T/DNA polymerase III; BRCT; SMART: Exonuclease; BRCT; SPTR: Exonuclease; IMG reference gene:2504106969; PFAM: Exonuclease; BRCA1 C Terminus (BRCT) domain.

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; Belongs to the RecA family.

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 [...]

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 [...]

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 polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family.

Superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.

COGs: COG0514 Superfamily II DNA helicase; InterProIPR011545:IPR001650:IPR018982:IPR002121:IPR 014001:IPR006293:IPR004589; KEGG: bfs:BF3249 putative ATP-dependent DNA helicase; PFAM: DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase, C-terminal; RQC domain; Helicase/RNase D C-terminal, HRDC domain; SMART: RQC domain; DEAD-like helicase, N-terminal; Helicase, C-terminal; Helicase/RNase D C-terminal, HRDC domain; SPTR: ATP-dependent DNA helicase RecQ; TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; IMG reference gene:2504106414 [...]

COGs: COG0514 Superfamily II DNA helicase; InterProIPR006293:IPR004589:IPR011545:IPR001650:IPR 018982:IPR002121:IPR014001; KEGG: bfs:BF3892 putative ATP-dependent DNA helicase; PFAM: RQC domain; Helicase, C-terminal; DNA/RNA helicase, DEAD/DEAH box type, N-terminal; Helicase/RNase D C-terminal, HRDC domain; SMART: DEAD-like helicase, N-terminal; Helicase, C-terminal; RQC domain; Helicase/RNase D C-terminal, HRDC domain; SPTR: ATP-dependent DNA helicase RecQ; TIGRFAM: DNA helicase, ATP-dependent, RecQ type, bacterial; DNA helicase, ATP-dependent, RecQ type; IMG reference gene:2504105861 [...]