5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint (By similarity). Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (By similarity). Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (By similarity). a beta-lactam + H2O = a substituted beta-amino acid Interacts with TERF2; the interaction is direct. Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5 (By similarity). Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome (By similarity). The TBM domain mediates interaction with TERF2. Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination (By similarity). Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.