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 [...]

Transcriptional repressor, LexA family; 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.

Peptidase S24/S26A/S26B, conserved region; Represses a number of genes involved in the response to DNA damage (SOS response).

Transcriptional repressor, LexA family; Represses a number of genes involved in the response to DNA damage (SOS response).

DNA-directed DNA polymerase; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.

Helicase domain protein; COGs: COG0553 Superfamily II DNA/RNA helicase SNF2 family; InterPro IPR014001:IPR001650:IPR000330:IPR014021; KEGG: sfu:Sfum_3846 helicase domain-containing protein; PFAM: helicase domain protein; SNF2-related protein; SMART: DEAD-like helicase; helicase domain protein; SPTR: A0LQ13 Helicase domain protein; manually curated; PFAM: Helicase conserved C-terminal domain; SNF2 family N-terminal domain.

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 [...]

Competence/damage-inducible protein CinA; COGs: COG1546 Uncharacterized protein (competence- and mitomycin-induced); InterPro IPR001453:IPR008136:IPR008135; KEGG: gme:Gmet_0196 competence/damage-inducible protein CinA; PFAM: CinA domain protein; molybdopterin binding domain; SPTR: C8QYB6 Competence/damage-inducible protein CinA; TIGRFAM: competence/damage-inducible protein CinA; PFAM: Probable molybdopterin binding domain; Competence-damaged protein; TIGRFAM: competence/damage-inducible protein CinA N-terminal domain; competence/damage-inducible protein CinA C-terminal domain; molybden [...]

Nuclease SbcCD, D subunit; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family.