DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA-mediated DNA strand exchange. ATP + H2O = ADP + H(+) + phosphate Mg(2+); Mn(2+), Cu(2+), Ni(2+) or Co(2+) also support ATPase activity. Inhibited by EDTA. kcat is 43 sec(-1) with ATP. Optimum pH is 7.5. Optimum temperature is 37 degrees Celsius. Monomer. Interacts with RecA. Up-regulated during mouse infection. Forms small colonies, liquid growth is unchanged. Increased sensitivity to UV light, mitomycin C, nitrosative and oxidative stress; a double uvrA/uvrD1 mutant is even more sensitive. Single uvrD1 mutant is strongly attenuated in late stages of mouse infection, the double uvrA/uvrD1 mutant is strongly attenuated at all stages of infection. Belongs to the helicase family. UvrD subfamily.