8.A.201.1.1 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).
|
Accession Number: | P96874 |
Protein Name: | Conserved protein |
Length: | 93 |
Molecular Weight: | 9750.00 |
Species: | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) [83332] |
Number of TMSs: | 1 |
Substrate |
|
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1: MAIQVFLAKA TTTVITGLAG VTAYEILKKA AAKAPLRQTA VSAAALGLRG TRKAEEAAES
61: ARLKVADVMA EARERIGEES PTPAISDLHD HDH