RT Journal Article SR Electronic(1) A1 Bonza, Maria Cristina A1 Martin, Holger A1 Kang, Ming A1 Lewis, Gentry A1 Greiner, Timo A1 Giacometti, Sonia A1 Van Etten, James L. A1 De Michelis, Maria Ida A1 Thiel, Gerhard A1 Moroni, AnnaYR 2010 T1 A functional calcium-transporting ATPase encoded by chlorella viruses JF Journal of General Virology, VO 91 IS 10 SP 2620 OP 2629 DO https://doi.org/10.1099/vir.0.021873-0 PB Microbiology Society, SN 1465-2099, AB Calcium-transporting ATPases (Ca2+ pumps) are major players in maintaining calcium homeostasis in the cell and have been detected in all cellular organisms. Here, we report the identification of two putative Ca2+ pumps, M535L and C785L, encoded by chlorella viruses MT325 and AR158, respectively, and the functional characterization of M535L. Phylogenetic and sequence analyses place the viral proteins in group IIB of P-type ATPases even though they lack a typical feature of this class, a calmodulin-binding domain. A Ca2+ pump gene is present in 45 of 47 viruses tested and is transcribed during virus infection. Complementation analysis of the triple yeast mutant K616 confirmed that M535L transports calcium ions and, unusually for group IIB pumps, also manganese ions. In vitro assays show basal ATPase activity. This activity is inhibited by vanadate, but, unlike that of other Ca2+ pumps, is not significantly stimulated by either calcium or manganese. The enzyme forms a 32P-phosphorylated intermediate, which is inhibited by vanadate and not stimulated by the transported substrate Ca2+, thus confirming the peculiar properties of this viral pump. To our knowledge this is the first report of a functional P-type Ca2+-transporting ATPase encoded by a virus., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.021873-0