Alkylsulfatase that cleaves the widely used detergent sodium dodecyl sulfate (SDS). a primary linear alkyl sulfate ester + H2O = a primary alcohol + H(+) + sulfate Binds 2 Zn(2+) ions per subunit. In vitro, is slightly activated in the presence of Ca(2+), but inhibited by Zn(2+). Homodimer. Contains three distinct domains: an N-terminal catalytic domain that contains a binuclear Zn(2+) cluster, a central dimerization domain and a C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain (PubMed:25066955). Although separated by the dimerization domain in terms of sequence, the N-terminal and C-terminal domains are spatially directly adjacent (PubMed:25066955). E.coli BL21 cells were shown to not grow on minimal medium agarose plates containing 0.1% SDS, indicating that the SDS was toxic to the bacteria cells. However, overexpression of YjcS in these cells rescued the cells. Belongs to the metallo-beta-lactamase superfamily. Type III sulfatase family. Extended N-terminus.