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

ATP-dependent DNA helicase recQ (EC 3.6.1.-). INVOLVED IN THE RECF RECOMBINATION PATHWAY; ITS GENE EXPRESSION IS UNDER THE REGULATION OF THE SOS SYSTEM. IT IS A DNA HELICASE. recq: ATP-dependent DNA helicase RecQ; High confidence in function and specificity.

Recombinase A; 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 topoisomerase I (EC 5.99.1.2) (Omega-protein) (Relaxing enzyme) (Untwisting enzyme) (Swivelase). THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. MAY PLAY AN IMPORTANT ROLE IN EITHER THE MAINTENANCE OF OR EXPRESSION FROM THE VIRULENCE PLASMID. ITS INFLUENCE ON EXPRESSION COULD BE SPECIFIC TUNING LOCAL SUPERHELICITY OR MORE GENERALLY MODIFYING THE SUPERHELICITY OF THE ENTIRE PLASMID IN RESPONSE TO ENVIRONMENTAL STIMULI THUS COULD BE A FUNDAMENTAL FACTOR INVOLVED IN VIRULENCE. InterPro: Prokaryotic DNA topoisomerase I; High [...]

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 [...]

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.

Putative DNA-directed polymerase III; Excinuclease cho (EC 3.1.25.-) (Endonuclease cho) (UvrC homolog protein). Incises the DNA at the 3 side of a lesion during nucleotide excision repair. Incises the DNA farther away from the lesion than uvrC. Not able to incise the 5 site of a lesion. When a lesion remains because uvrC is not able to induce the 3 incision cho incises the DNA. Then uvrC makes the 5 incision. The combined action of cho and uvrC broadens the substrate range of nucleotide excision repair (By similarity); Specificity unclear.

Transcription-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; In the C-terminal section; belongs to the helicase family. RecG subfamily.