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Literature summary extracted from

  • Padilla-Benavides, T.; Long, J.; Raimunda, D.; Sassetti, C.; Arguello, J.
    A novel P1B-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria (2013), J. Biol. Chem., 288, 11334-11347 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.22 gene ctpC, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS pSJS1240, recombinant enzyme expression from pBAD TOPO vector carrying in Escherichia coli strain W3110 DELTAzntA cells. Quantitative RT-PCR enzyme expression analysis. Lack of functional complementation of Escherichia coli DELTAzntA by ctpC Mycobacterium tuberculosis
7.2.2.22 gene ctpC, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS pSJS1240. Quantitative RT-PCR enzyme expression analysis Mycolicibacterium smegmatis

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.22 H697A site-directed mutagenesis Mycolicibacterium smegmatis
7.2.2.22 H699A site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels Mycobacterium tuberculosis
7.2.2.22 additional information a Zn2+ tolerance-decreased phenotype is oberseved in Mycobacterium tuberculosis strain H37Rv ctpC::hyg cells when grown at Zn2+ concentrations as low as 0.005 mM, but no changes are observed in the sensitivity to Cd2+. Presence of Co2+ or Cu2+ in the medium has no effect on the growth of these cells. Deletion of ctpC leads to cytoplasmic Mn2+ accumulation and a decrease in secreted Mn2+-bound proteins. A 4fold increase in cellular Mn2+ content is observed in the Mycobacterium tuberculosis ctpC mutant, along with a significant decrease in the Mn2+ bound to secreted proteins. The levels of Zn2+, Fe2+, or Cu2+ bound to secreted proteins are not affected in the Mycobacterium tuberculosis ctpC mutant strain. Fraction metal content of Mycobacterium tuberculosis strains, Mn2+ contents of wild-type and mutant enzymes, overview Mycobacterium tuberculosis
7.2.2.22 additional information the levels of Zn2+, Fe2+, or Cu2+ bound to secreted proteins are not affected in the Mycobacterium smegmatis ctpC mutant strain. Response of ctpC::hyg to metal and redox stressors Mycolicibacterium smegmatis
7.2.2.22 S700A/S701A site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels Mycobacterium tuberculosis
7.2.2.22 S700A/S701A site-directed mutagenesis Mycolicibacterium smegmatis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.22 membrane
-
 Mycobacterium tuberculosis 16020
-
7.2.2.22 membrane
-
 Mycolicibacterium smegmatis 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.22 Cu+ slight activation at 10 nM Mycobacterium tuberculosis
7.2.2.22 Cu2+ about 28% activation compared to Mn2+ at 10 nM Mycobacterium tuberculosis
7.2.2.22 Mg2+ required Mycobacterium tuberculosis
7.2.2.22 Mg2+ required Mycolicibacterium smegmatis
7.2.2.22 Mn2+ isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+ Mycobacterium tuberculosis
7.2.2.22 Mn2+ isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+ Mycolicibacterium smegmatis
7.2.2.22 additional information enzyme metal content analysis. No or poor activation by Cd2+, Fe2+, and Fe3+ at 10 nM Mycobacterium tuberculosis
7.2.2.22 additional information enzyme metal content analysis Mycolicibacterium smegmatis
7.2.2.22 Ni2+ slight activation at 10 nM Mycobacterium tuberculosis
7.2.2.22 Zn2+ isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+, about 25% activation compared to Mn2+ at 10 nM Mycobacterium tuberculosis
7.2.2.22 Zn2+ isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+ Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.22 ATP + H2O + Mn2+[side 1] Mycobacterium tuberculosis
-
 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1] Mycolicibacterium smegmatis
-
 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1] Mycobacterium tuberculosis H37Rv
-
 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1] Mycolicibacterium smegmatis mc(2)155
-
 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1] Mycolicibacterium smegmatis ATCC 700084
-
 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1] Mycobacterium tuberculosis ATCC 25618
-
 ADP + phosphate + Mn2+[side 2]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.22 Mycobacterium tuberculosis P9WPT5
-
-
7.2.2.22 Mycobacterium tuberculosis ATCC 25618 P9WPT5
-
-
7.2.2.22 Mycobacterium tuberculosis H37Rv P9WPT5
-
-
7.2.2.22 Mycolicibacterium smegmatis I7GFC6 Mycobacterium smegmatis
-
7.2.2.22 Mycolicibacterium smegmatis ATCC 700084 I7GFC6 Mycobacterium smegmatis
-
7.2.2.22 Mycolicibacterium smegmatis mc(2)155 I7GFC6 Mycobacterium smegmatis
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.2.22 recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS pSJS1240 by ultracentrifugation at 229000 x g, nickel affinity chromatography, and ultrafiltration Mycolicibacterium smegmatis
7.2.2.22 recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 (DE3) pLysS pSJS1240 by ultracentrifugation at 229000 x g, nickel affinity chromatography, and ultrafiltration, the tag is cleaved by TEV protease Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.22 ATP + H2O + Mn2+[side 1]
-
 Mycobacterium tuberculosis ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1]
-
 Mycolicibacterium smegmatis ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1]
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1]
-
 Mycolicibacterium smegmatis mc(2)155 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1]
-
 Mycolicibacterium smegmatis ATCC 700084 ADP + phosphate + Mn2+[side 2]
-
 ?
7.2.2.22 ATP + H2O + Mn2+[side 1]
-
 Mycobacterium tuberculosis ATCC 25618 ADP + phosphate + Mn2+[side 2]
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.2.22 ? x * 80000, recombinant enzyme, SDS-PAGE Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
7.2.2.22 ctpC
-
 Mycobacterium tuberculosis
7.2.2.22 ctpC
-
 Mycolicibacterium smegmatis
7.2.2.22 P1B-type Mn2+-transporting ATPase
-
 Mycobacterium tuberculosis
7.2.2.22 P1B-type Mn2+-transporting ATPase
-
 Mycolicibacterium smegmatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.2.2.22 37
-
 assay at Mycobacterium tuberculosis
7.2.2.22 37
-
 assay at Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2.2.22 8
-
 assay at Mycobacterium tuberculosis
7.2.2.22 8
-
 assay at Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.2.22 ATP
-
 Mycobacterium tuberculosis
7.2.2.22 ATP
-
 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
7.2.2.22 evolution key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases Mycobacterium tuberculosis
7.2.2.22 evolution key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases Mycolicibacterium smegmatis
7.2.2.22 malfunction mutation of CtpC leads to a decrease of Mn2+ bound to secreted proteins and of the activity of secreted Fe/Mn-superoxide dismutase. CtpC deficiency renders Mycobacterium tuberculosis sensitive to Zn2+ and oxidative stress Mycobacterium tuberculosis
7.2.2.22 malfunction mutation of CtpC leads to a decrease of Mn2+ bound to secreted proteins and of the activity of secreted Fe/Mn-superoxide dismutase, especially in Mycobacterium smegmatis Mycolicibacterium smegmatis
7.2.2.22 metabolism link between the observed Mn2+-dependent ATPase activity and the binding of Mn2+ to a transmembrane transport site distinct from those in Cu+- or Zn2+-ATPases Mycobacterium tuberculosis
7.2.2.22 additional information importance of the distinct HXXSS sequence in TM8 of Mycobacterium tuberculosis CtpC Mycobacterium tuberculosis
7.2.2.22 physiological function transition metals are central for bacterial virulence and host defense. P1B-ATPases are responsible for cytoplasmic metal efflux and play roles either in limiting cytosolic metal concentrations or in the maturation of secreted metalloproteins. The P1B-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria and for Mycobacterium tuberculosis survival in a mouse model (infection of C57BL/6 female mice). CtpC is a unique Mn2+-ATPase Mycobacterium tuberculosis
7.2.2.22 physiological function transition metals are central for bacterial virulence and host defense. P1B-ATPases are responsible for cytoplasmic metal efflux and play roles either in limiting cytosolic metal concentrations or in the maturation of secreted metalloproteins. The P1B-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria. CtpC is a unique Mn2+-ATPase Mycolicibacterium smegmatis