PacL1 (Rv3269) of 93 aas and 1 N-terminal TMS. It functions with a high affinity, slow turnover heavy metal transporting ATPase CtpC (Rv3270; TC#3.A.3.32.2), which is required for virulence. It controls the Mn²⁺ cytoplasmic quota and is involved in the uploading of Mn²⁺ into secreted metalloproteins (Padilla-Benavides et al. 2013). It shows a preference for Mn²⁺, but Zn²⁺, Co²⁺ and Cu²⁺ can act as alternative substrates although at slower turnover rates (Padilla-Benavides et al. 2013). Boudehen et al. 2022 showed that zinc resistance also depends on a chaperone-like protein, PacL1 (Rv3269). PacL1 contains an N-terminal TMS, a cytoplasmic region with glutamine/alanine repeats and a C-terminal metal-binding motif (MBM). PacL1 binds Zn²⁺, but the MBM is required only at high zinc concentrations. PacL1 co-localizes with CtpC, a heavy metal cation-transporting P-type ATPase, in dynamic foci in the mycobacterial plasma membrane, and the two proteins form high molecular weight complexes. Foci formation does not require flotillin or the PacL1 MBM. However, deletion of the PacL1 Glu/Ala repeats leads to loss of CtpC and sensitivity to zinc. Genes pacL1 and ctpC appear to be in the same operon, and homologous gene pairs are found in the genomes of other bacteria. PacL1 colocalizes and functions redundantly with other PacL orthologs in M. tuberculosis. Thus, PacL proteins may act as scaffolds that assemble P-ATPase-containing metal efflux platforms, mediating bacterial resistance to metal poisoning (Boudehen et al. 2022).