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Information on EC 7.2.2.22 - P-type Mn2+ transporter
for references in articles please use BRENDA:EC7.2.2.22
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EC Tree 7 Translocases
7.2 Catalysing the translocation of inorganic cations
7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
7.2.2.22 P-type Mn2+ transporter
IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, detected in mycobacteria, is a high affinity slow turnover ATPase exporting Mn2+.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
AtECA1, Ca2+/Mn2+ P-type ATPase, Ca2+/Mn2+-transporting P-type ATPase, ctpC, Golgi Ca2+/Mn2+ P-type ATPase pump, MgtA, Mn(II)-translocating P-type ATPase, Mn2+-exporting ATPase, Mn2+-transporting P-type ATPase, Mn2+/Ca2+ ATPase transporter, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+/Mn2+ P-type ATPase
Ca2+/Mn2+-transporting P-type ATPase
ctpC
Mn(II)-translocating P-type ATPase
-
-
-
-
Mn2+-exporting ATPase
-
-
-
-
Mn2+-transporting P-type ATPase
P1B-type ATPase
-
-
ambiguous
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P1B-type Mn2+-transporting ATPase
PMR1
Pmr1p
additional information
ctpC
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Mn2+[side 1] = ADP + phosphate + Mn2+[side 2]
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Mn2+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, detected in mycobacteria, is a high affinity slow turnover ATPase exporting Mn2+.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: the Arabidopsis thaliana endoplasmic reticulum-localized Ca2+-ATPase, ECA1, with homology to PMR1, can also transport Mn2+. Molecular determinants of the Mn2+ specificity of transport proteins
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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Substrates: -
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ATP + H2O + Mn2+[side 1]
ADP + phosphate + Mn2+[side 2]
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
additional information
Mn2+
isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+
Mn2+
isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+
Mn2+
Mn2+ induces accumulation of Pmr1 and Pmc1 mRNAs in a calcineurin/Prz1-dependent manner
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
Zn2+
isolated CtpC has metal-dependent ATPase activity with a strong preference for Mn2+ over Zn2+
additional information
enzyme metal content analysis. No or poor activation by Cd2+, Fe2+, and Fe3+ at 10 nM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
artemisinin
Ca2+-ATPase and Golgi localized Pmr1p appears to be targets for artemisinin
additional information
artemisinin resistance in pmr1DELTA cells is not caused by alteration in the localization or accumulation of the multidrug transporter Pdr5p as well as not by association between defects in calcium homeostasis or protein glycosylation and sensitivity to artemisinin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases
evolution
key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases
evolution
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6. Pmr1p is a key transporter for uptake of Ca2+ into the Golgi, which is important for maintaining the Ca2+ homeostasis of yeast cells
evolution
-
the enzyme is a evolutionarily conserved Ca2+/Mn2+-transporting P-type ATPase
evolution
-
key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases
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evolution
-
key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases
-
evolution
-
the enzyme is a evolutionarily conserved Ca2+/Mn2+-transporting P-type ATPase
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evolution
-
Saccharomyces cerevisiae enzyme Pmr1p is a functional homologue of Plasmodium falciparum enzyme PfATP6. Pmr1p is a key transporter for uptake of Ca2+ into the Golgi, which is important for maintaining the Ca2+ homeostasis of yeast cells
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evolution
-
key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases
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evolution
-
key metal-coordinating residues and the overall structure of CtpC are distinct from Zn2+-ATPases
-
malfunction
a T-DNA knockout of ECA1, grown on high-Mn media, displays a strong stress phenotype when compared to wild-type plants. This phenotype includes a significant reduction in fresh weight, dramatic leaf chlorosis, a significant inhibition of leaf expansion and root elongation, and a loss of root hair tip growth. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrated a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants. ILR2 might act as a regulator of Mn2+ transport, possibly acting on Mn2+ efflux from the cell mediated by either an ATPase or an ABC transporter
malfunction
the pmr1 knockout (DELTApmr1) cells exhibit hypersensitivity to EGTA. The EGTA-hypersensitive phenotype of DELTApmr1 leads to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The DELTApmr1 cells show round cell morphology. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
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
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
malfunction
cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast deleted for PMR1 are known to accumulate excess manganese ions that can function as ROS-scavenging molecules. Loss-of-function mutations in Pmr1p in yeast cells are protective against artemisinin toxicity due to reduced intracellular oxidative damage, artemisinin resistance in pmr1DELTA cells. The loss of function in Pmr1p results in reduced artemisinin sensitivity due to insufficient ROS being generated to cause significant cellular damage
malfunction
lack of SPCA1 leads to lysosomal degradation of TMEM165 (uncharacterized protein related to human glycosylation diseases)
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
-
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
-
malfunction
-
the pmr1 knockout (DELTApmr1) cells exhibit hypersensitivity to EGTA. The EGTA-hypersensitive phenotype of DELTApmr1 leads to the identification of pdt1+ gene, which encodes an Nramp-related metal transporter. The DELTApmr1 cells show round cell morphology. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
-
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
-
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
-
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
metabolism
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
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
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
-
metabolism
-
several transporter gene families have been implicated in Mn2+ transport, including cation/H+ antiporters, natural resistance-associated macrophage protein (Nramp) transporters, zinc-regulated transporter/iron-regulated transporter (ZRT/IRT1)-related protein (ZIP) transporters, the cation diffusion facilitator (CDF) transporter family, and P-type ATPases
-
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
-
physiological function
ECA1 is originally identified as Ca2+ transporter, but has subsequently been shown to also transport Mn2+. AtECA1 is an endoplasmic reticulum (ER) Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.10). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction. Mn2+ has a critical role in the water oxidation step of photosynthesis, and the chloroplast is the second-largest sink for Mn in the cell
physiological function
PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.10). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction
physiological function
enzymes Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator. The pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporte. Pmr1 is regulated by the Ca2+/calcineurin/Prz1 pathway
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
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
physiological function
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress. Wild-type cells exhibit a significant increase in ROS production following treatment with artemisinin. Enzyme Pmr1p may play a role in ROS generation or accumulation from artemisinin
physiological function
-
cellular processes regulated by Cwh43 (putative ceramide-conjugation protein) are appropriately balanced with Pmr1-mediated Mn2+ transport into the endoplasmic reticulum
physiological function
expression of TMEM165 (uncharacterized protein related to human glycosylation diseases) is linked to the function of SPCA1. TMEM165 abundance is directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. The level and subcellular Golgi localization of TMEM165 is not dependent on the Ca2+ transport function of SPCA1 or its presence
physiological function
-
MgtA may export Mn2+ under conditions of extreme Mn-stress thereby protecting cells from Mn2+ toxicity. The mgtA riboswitch may also function to regulate Ca2+ export under these conditions
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
-
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
-
physiological function
-
cellular processes regulated by Cwh43 (putative ceramide-conjugation protein) are appropriately balanced with Pmr1-mediated Mn2+ transport into the endoplasmic reticulum
-
physiological function
-
PMR1 is a Golgi Ca2+- and Mn2+-transporting P-type ATPase (see also EC 7.2.2.10). Manganese (Mn) is an essential nutrient in plants. It is of particular importance in photosynthetic organisms where a cluster of Mn atoms is required as the catalytic centre for light-induced water oxidation in photosystem II, and is required as a cofactor for a variety of enzymes, such as the Mn2+-dependent superoxide dismutase (MnSOD). Mn can be particularly toxic to plant growth and a variety of mechanisms exist to overcome such toxicity, including the conversion of the metal to a metabolically inactive compound, such as a Mn2+-chelate complex, or sequestration of the Mn2+ ion or a Mn2+-chelate complex into an internal compartment such as the vacuole. At the cellular level, Mn2+ accumulates predominantly in the vacuole and to some extent in chloroplasts, and can be associated with the cell wall fraction
-
physiological function
-
enzymes Pmr1 and Pdt1 cooperatively regulate cell morphogenesis through the control of Mn2+ homeostasis, and calcineurin functions as a Mn2+ sensor as well as a Mn2+ homeostasis regulator. The pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporte. Pmr1 is regulated by the Ca2+/calcineurin/Prz1 pathway
-
physiological function
-
artemisinins are widely used to treat Plasmodium infections due to their high clinical efficacy. Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress. Wild-type cells exhibit a significant increase in ROS production following treatment with artemisinin. Enzyme Pmr1p may play a role in ROS generation or accumulation from artemisinin
-
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
-
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
-
additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
additional information
a subfamily of P-type ATPases, the P1B-ATPases, catalyse transition metal efflux in many organisms including plants, and are predicted to transport either Zn2+/Cd2+/Pb2+/Co2+ or Cu2+/Ag2+, but there is no evidence that Mn2+ is a substrate for P1B-ATPases from any organism
additional information
importance of the distinct HXXSS sequence in TM8 of Mycobacterium tuberculosis CtpC
additional information
-
importance of the distinct HXXSS sequence in TM8 of Mycobacterium tuberculosis CtpC
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additional information
-
importance of the distinct HXXSS sequence in TM8 of Mycobacterium tuberculosis CtpC
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CTPC_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
718
0
76495
Swiss-Prot
-
CTPC_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
718
0
76495
Swiss-Prot
-
CTPC_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
718
0
76495
Swiss-Prot
-
A0A0E4CM31_MYCLN
731
0
77611
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0H3A2D7_MYCA1
Mycobacterium avium (strain 104)
712
0
75849
TrEMBL
other Location (Reliability: 5)
A0A0H3MHJ0_MYCBP
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
718
0
76495
TrEMBL
-
A0A1V3XWC4_MYCKA
312
0
33585
TrEMBL
other Location (Reliability: 2)
A0A1X1Z7Z1_9MYCO
708
0
75312
TrEMBL
other Location (Reliability: 1)
A0A2A2ZE02_MYCAV
712
0
75906
TrEMBL
Mitochondrion (Reliability: 1)
A0A2A3L0E4_MYCAV
726
0
77288
TrEMBL
-
A0A2U3NAV4_9MYCO
698
0
74555
TrEMBL
-
A0A2U3P3P7_9MYCO
728
0
77353
TrEMBL
-
A0A447GAX9_9MYCO
732
0
78149
TrEMBL
other Location (Reliability: 4)
A0A654Z8Y1_MYCTX
554
0
59130
TrEMBL
other Location (Reliability: 2)
A0A679LKN4_MYCBO
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
718
0
76495
TrEMBL
-
A0A829C4B1_9MYCO
718
0
76521
TrEMBL
-
A0A9P2HBD8_MYCTX
718
0
76495
TrEMBL
-
A0AA41XN00_9MYCO
718
0
76583
TrEMBL
other Location (Reliability: 5)
A0AAI8SR73_MYCAV
697
0
74351
TrEMBL
-
A0AAU0Q422_9MYCO
718
0
76521
TrEMBL
other Location (Reliability: 3)
A0AAW5S0Q8_MYCBC
726
0
77246
TrEMBL
-
A0AB72XPJ9_MYCCP
Mycobacterium canettii (strain CIPT 140010059)
726
0
77419
TrEMBL
-
A5U7U4_MYCTA
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
718
0
76495
TrEMBL
-
Q73UI4_MYCPA
Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
726
0
77294
TrEMBL
-
X7ZPE6_MYCKA
698
0
74799
TrEMBL
other Location (Reliability: 3)
I7GFC6_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
712
0
75513
TrEMBL
other Location (Reliability: 3)
ATC1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
950
7
104571
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R123I
site-directed mutagenesis, when Arg123 of ShMTP1 is mutated to Ile, the ability to confer Mn2+ tolerance to either yeast or Arabidopsis is completely lost
Q747A
the mutant which exhibits an enhanced Mn2+ pumping activity, fully rescues TMEM165 stability and Golgi subcellular localization
H699A
site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels
S700A/S701A
site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels
H699A
-
site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels
-
S700A/S701A
-
site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels
-
H699A
-
site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels
-
S700A/S701A
-
site-directed mutagenesis, the mutant shows no ATPase activity at saturating Mn2+ levels
-
D100A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D136A
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
D100A
-
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
-
D136A
-
site-directed mutagenesis, substitution of Asp100 or Asp136 with Ala in IRT1 eliminates the ability of IRT1 to complement both Fe- and Mn-sensitive yeast mutants, but retains the ability to complement a Zn-sensitive yeast strain
-
additional information
additional information
recombinant ECA1 shows ability to confer tolerance to toxic concentrations of Mn when heterologously expressed in a Mn-sensitive mutant yeast strain. The Arabidopsis IAA-leucine resistant 2 (ilr2) mutant has a slight tolerance to Mn stress. Transport characterization of microsomal membrane vesicles from ilr2 plants demonstrated a significant increase in ATP-dependent Mn2+ transport compared to wild-type plants
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
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
-
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
-
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
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
-
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
-
additional information
construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
additional information
Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
additional information
-
construction of a pmr1 knockout (DELTApmr1) cells exhibiting hypersensitivity to EGTA. Overexpression of pdt1+ gene suppresses the EGTA-sensitive growth defects of DELTApmr1 cells. Although DELTApdt1 cells appear normal in the regular medium, they show round cell morphology similar to that of the DELTApmr1 cells when Mn2+ is removed from the medium. The removal of Mn2+ also exacerbates the round morphology of the DELTApmr1 cells. The DELTApmr1/DELTApdt1 double mutants grow very slowly and shows extremely aberrant cell morphology with round, enlarged and depolarized shape. The addition of Mn2+, but not Ca2+, to the medium completely suppresses the morphological defects, while both Mn2+ and Ca2+ markedly improve the slow growth of the double mutants. Growth of the DELTApmr1/DELTApdt1 double mutants is affected by Mn2+, Ca2+, FK506, and calcineurin overexpression
-
additional information
-
Saccharomyces cerevisiae strain BY4742 cells lacking Pmr1p are less susceptible to growth inhibition from artemisinin and its derivatives. No association between sensitivity to artemisinin and altered trafficking of the drug efflux pump Pdr5p, calcium homeostasis, or protein glycosylation is found in pmr1DELTA yeast mutant. Basal ROS levels are elevated in pmr1DELTA yeast and artemisinin exposure does not enhance ROS accumulation. Yeast mutant pmr1DELTA phenotype, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
gene ctpC, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 (DE3) pLysS pSJS1240. Quantitative RT-PCR enzyme expression analysis
the pmr1+ gene has strong genetic interactions with pdt1+ gene that encodes the Nramp-related divalent metal transporter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
addition of Mn2+, as well as Ca2+, to the medium induces pmr1+ gene expression in a calcineurin/Prz1-dependent manner
the mgtA riboswitch aptamer domain adopts a canonical yybP-ykoY structure containing a three-way junction that is compacted in the presence of Ca2+ or Mn2+ at a physiological Mg2+ concentration. Although Ca2+ binds to the RNA aptamer with higher affinity than Mn2+, in vitro activation of transcription read-through of mgtA by Mn2+ is much greater than by Ca2+. mgtA mRNA and protein levels increase about 5fold during cellular Mn stress, but only in genetic background of Streptococcus pneumoniae that exhibits Mn2+ sensitivity
-
addition of Mn2+, as well as Ca2+, to the medium induces pmr1+ gene expression in a calcineurin/Prz1-dependent manner
addition of Mn2+, as well as Ca2+, to the medium induces pmr1+ gene expression in a calcineurin/Prz1-dependent manner
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals
biotechnology
the ability to manipulate metal transporters, such as by altering substrate specificity, is an essential step in developing genetically engineered plants that can be used for phytoremediation strategies for specific metals
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maeda, T.; Sugiura, R.; Kita, A.; Saito, M.; Deng, L.; He, Y.; Yabin, L.; Fujita, Y.; Takegawa, K.; Shuntoh, H.; Kuno, T.
Pmr1, a P-type ATPase, and Pdt1, an Nramp homologue, cooperatively regulate cell morphogenesis in fission yeast the importance of Mn2+ homeostasis
Genes Cells
9
71-82
2004
Saccharomyces cerevisiae (P13586), Saccharomyces cerevisiae ATCC 204508 (P13586)
brenda
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
J. Biol. Chem.
288
11334-11347
2013
Mycobacterium tuberculosis (P9WPT5), Mycolicibacterium smegmatis (I7GFC6), Mycobacterium tuberculosis H37Rv (P9WPT5), Mycolicibacterium smegmatis mc(2)155 (I7GFC6), Mycolicibacterium smegmatis ATCC 700084 (I7GFC6), Mycobacterium tuberculosis ATCC 25618 (P9WPT5)
brenda
Pongwattanakewin, O.; Phyu, T.; Suesattayapirom, S.; Jensen, L.; Jensen, A.
Possible role of the Ca2+/Mn2+ P-type ATPase Pmr1p on artemisinin toxicity through an induction of intracellular oxidative stress
Molecules
24
1233
2019
Saccharomyces cerevisiae (P13586), Saccharomyces cerevisiae ATCC 204508 (P13586)
brenda
Pittman, J.K.
Managing the manganese molecular mechanisms of manganese transport and homeostasis
New Phytol.
167
733-742
2005
Arabidopsis thaliana (P92939), Saccharomyces cerevisiae (P13586), Saccharomyces cerevisiae ATCC 204508 (P13586)
brenda
Lebredonchel, E.; Houdou, M.; Hoffmann, H.H.; Kondratska, K.; Krzewinski, M.A.; Vicogne, D.; Rice, C.M.; Klein, A.; Foulquier, F.
Investigating the functional link between TMEM165 and SPCA1
Biochem. J.
476
3281-3293
2019
Homo sapiens (P98194)
brenda
Nakazawa, N.; Xu, X.; Arakawa, O.; Yanagida, M.
Coordinated roles of the putative ceramide-conjugation protein, Cwh43, and a Mn2+-transporting, P-type ATPase, Pmr1, in fission Yeast
G3 (Bethesda)
9
2667-2676
2019
Schizosaccharomyces pombe, Schizosaccharomyces pombe 972
brenda
Martin, J.; Le, M.; Bhattarai, N.; Capdevila, D.; Shen, J.; Winkler, M.; Giedroc, D.
A Mn-sensing riboswitch activates expression of a Mn2+/Ca2+ ATPase transporter in Streptococcus
Nucleic Acids Res.
47
6885-6899
2019
Streptococcus pneumoniae
brenda
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