PMID:9440521

Citation	Bayle, D, Wängler, S, Weitzenegger, T, Steinhilber, W, Volz, J, Przybylski, M, Schäfer, KP, Sachs, G and Melchers, K (1998) Properties of the P-type ATPases encoded by the copAP operons of Helicobacter pylori and Helicobacter felis. J. Bacteriol. 180:317-29
Abstract	The cop operons of Helicobacter pylori and Helicobacter felis were cloned by gene library screening. Both operons contain open reading frames for a P-type ion pump (CopA) with homology to Cd2+ and Cu2+ ATPases and a putative ion binding protein (CopP), the latter representing a CopZ homolog of the copYZAB operon of Enterococcus hirae. The predicted CopA ATPases contained an N-terminal GMXCXXC ion binding motif and a membrane-associated CPC sequence. A synthetic N-terminal peptide of the H. pylori CopA ATPase bound to Cu2+ specifically, and gene disruption mutagenesis of CopA resulted in an enhanced growth sensitivity of H. pylori to Cu2+ but not to other divalent cations. As determined experimentally, H. pylori CopA contains four pairs of transmembrane segments (H1 to H8), with the ATP binding and phosphorylation domains lying between H6 and H7, as found for another putative transition metal pump of H. pylori (K. Melchers, T. Weitzenegger, A. Buhmann, W. Steinhilber, G. Sachs, and K. P. Schäfer, J. Biol. Chem. 271:446-457, 1996). The corresponding transmembrane segments of the H. felis CopA pump were identified by hydrophobicity analysis and via sequence similarity. To define functional domains, similarly oriented regions of the two enzymes were examined for sequence identity. Regions with high degrees of identity included the N-terminal Cu2+ binding domain, the regions of ATP binding and phosphorylation in the energy transduction domain, and a transport domain consisting of the last six transmembrane segments with conserved cysteines in H4, H6, and H7. The data suggest that H. pylori and H. felis employ conserved mechanisms of ATPase-dependent copper resistance.
Links	PubMed PMC106887
Keywords	Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Bacterial Proteins/genetics; Blotting, Southern; Cell Membrane/metabolism; DNA, Bacterial; Helicobacter/enzymology; Helicobacter/genetics; Metals/metabolism; Molecular Sequence Data; Operon; Sequence Homology, Amino Acid; Species Specificity
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HELPX:COPA2		GO:0006825: copper ion transport	ECO:0000315:		P		Table 2: The copA mutant was susceptible to the same concentrations of the divalent cations of Ni, Zn, Co, and Mg as the wild-type strain but had a different susceptibility to divalent cation of Cu. The wild-type strain had a divalent cation Cu MIC of 50 mM, whereas the mutant had a divalent cation Cu MIC of 7.5 mM, suggesting that the ATPase can function as a copper ion export pump.	complete CACAO 6271
HELPX:COPA2	involved_in	GO:0006825: copper ion transport	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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