The P-Type ATPase Superfamily

  title={The P-Type ATPase Superfamily},
  author={Henry Chan and V. O. Babayan and Elya Blyumin and Charmy Gandhi and Kunal Hak and Danielle Harake and Krishma Kumar and P. D. Lee and Tze T. Li and H. Liu and Tony Chung Tung Lo and Cynthia J. Meyer and Steven Stanford and Krista S Zamora and Milton H. Saier, Jr.},
  journal={Journal of Molecular Microbiology and Biotechnology},
  pages={5 - 104}
P-type ATPases function to provide homeostasis in higher eukaryotes, but they are essentially ubiquitous, being found in all domains of life. Thever and Saier [J Memb Biol 2009;229:115–130] recently reported analyses of eukaryotic P-type ATPases, dividing them into nine functionally characterized and 13 functionally uncharacterized (FUPA) families. In this report, we analyze P-type ATPases in all major prokaryotic phyla for which complete genome sequence data are available, and we compare the… 
Role of Prokayotic P-Type ATPases
The various roles of P-type ATPases in prokaryotes are put together to confer on them the ability to withstand high concentrations of heavy metals, to overcome high phagosomal metal levels and to aid in the assembly of periplasmic and secreted metalloproteins.
Origin and evolution of metal P-type ATPases in Plantae (Archaeplastida)
Large-scale phylogenetics is used to show that metal P-type ATPases form a homogenous group among P- type ATPases and that their specialization into either monovalent or divalent metal transport stems from a gene duplication that took place early in the evolution of Life.
In silico identification and characterization of the ion transport specificity for P-type ATPases in the Mycobacterium tuberculosis complex
The high content of heavy metal transporters found in the MTBC suggests that they could play an important role in the ability of M. tuberculosis to survive inside macrophages, where tubercle bacilli face high levels of toxic metals.
The KdpFABC complex – K+ transport against all odds
Evidence supporting contradictory models of the KdpFABC complex is discussed and key experiments are identified needed to resolve discrepancies and produce a unified model for this fascinating mechanistic hybrid.
P-type transport ATPases in Leishmania and Trypanosoma
P-type ATPases are critical to the maintenance and regulation of cellular ion homeostasis and membrane lipid asymmetry due to their ability to move ions and phospholipids against a concentration
Evolution of the α-Subunit of Na/K-ATPase from Paramecium to Homo sapiens: Invariance of Transmembrane Helix Topology
Na/K-ATPase is a key plasma membrane enzyme involved in cell signaling, volume regulation, and maintenance of electrochemical gradients. The α-subunit, central to these functions, belongs to a large
Characterization of the PIB-Type ATPases Present in Thermus thermophilus
In each case, the deletion increased the sensitivity of the strain to growth in the presence of copper in the medium, indicating that each of the three P-type ATPases can pump copper out of the cells and play a role in copper detoxification.
A comprehensive phylogenetic analysis of copper transporting P1B ATPases from bacteria of the Rhizobiales order uncovers multiplicity, diversity and novel taxonomic subtypes
In silico analysis, the presence of five copies of Cu‐ATPases in the symbiotic nitrogen‐fixing bacteria Sinorhizobium meliloti is remarkable and suggests a high divergence of CopZ and CusF homologs, or the existence of unexplored proteins involved in cellular copper transport.
Bioinformatic Characterization of the Trimeric Intracellular Cation-Specific Channel Protein Family
Analysis of TRIC channels revealed that these proteins possess seven putative transmembrane segments, which arose by intragenic duplication of a three-TMS polypeptide-encoding genetic element followed by addition of a seventh TMS to give the precursor of all current TRIC family homologs.


Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review)
Generic features of P-type ATPases are compared with the rather unique KdpFABC complex of the enterobacterium Escherichia coli and a comprehensive overview of common principles of catalysis is given as well as of special aspects connected to distinct enzyme functions.
P-type ATPases of eukaryotes and bacteria: Sequence analyses and construction of phylogenetic trees
Correlative functional analyses of the most conserved regions of these ATPases, based on published site-specific mutagenesis data, provided preliminary evidence for their functional roles in the transport mechanism.
Bioinformatic Characterization of P-Type ATPases Encoded Within the Fully Sequenced Genomes of 26 Eukaryotes
This study analyzes the fully sequenced genomes of 26 eukaryotes for P-type ATPases to report the organismal distributions, phylogenetic relationships, probable topologies and conserved motifs of nine functionally characterized families and 13 uncharacterized families of these enzyme transporters.
Prokaryotic Kdp-ATPase: Recent Insights into the Structure and Function of KdpB
It can be concluded that KdpB is currently misgrouped as class IA because of the conserved 395KGXXD/E motif and thus the nucleotide-binding mode seems to be conserved in all P-type ATPases, except the heavy metal-transporting (class IB) ATPases.
K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer.
A close vicinity of two KdpB subunits within the functional KdpFABC complex could be demonstrated by chemical cross-linking of native cysteine residues using copper 1,10-phenanthroline, and the cysteines responsible for cross-link formation were identified by mutagenesis.
The K+-translocating KdpFABC complex from Escherichia coli: A P-type ATPase with unique features
The latest results are in favor of the notion that KdpC might act as a catalytical chaperone, which cooperatively interacts with the nucleotide to be hydrolyzed and, thus, increases the rather untypical weak nucleotide binding affinity of the KdpB nucleotidebinding domain.
18O-Exchange Evidence That Mutations of Arginine in a Signature Sequence for P-Type Pumps Affect Inorganic Phosphate Binding†
To test the prediction that the positively charged guanidinium group of R596 in human alpha(1) Na,K-ATPase participates in phosphoryl group transfer, the charge was progressively decreased by site-directed mutagenesis.