Alkylbase DNA glycosidase-like protein that shows no DNA glycosylase activity for alkylated bases (PubMed:23273506, PubMed:23245849). The molecular role of mag2 appears to be abasic (AP) site recognition and protection, while possibly facilitating damage signaling by structurally sculpting the DNA substrate (PubMed:18270439, PubMed:23245849). Stimulates AP site binding to mismatch repair protein mutS (PubMed:23245849). Transcription is strongly induced following exposure to the alkylating agent methyl methanesulfonate (MMS) and oxidizing H(2)O(2). Belongs to the alkylbase DNA glycosidase AlkA family. As an homolog of the DNA glycosidase mag1, has been identified to be an alkylbase DNA glycosidase (PubMed:18270439). However, further studies revealed that it did not have any DNA glycosylase activity for alkylated bases due to the loss of the acive site 'Ser-56', and was rather involved in structural sculpting DNA to facilitate damage signaling (PubMed:23273506, PubMed:23245849).