ABCC1 p.Asp61Glu
| Predicted by SNAP2: | A: N (87%), C: N (87%), E: N (93%), F: N (72%), G: N (87%), H: N (87%), I: N (66%), K: N (93%), L: N (78%), M: N (72%), N: N (93%), P: N (82%), Q: N (93%), R: N (93%), S: N (97%), T: N (93%), V: N (82%), W: D (66%), Y: N (66%), |
| Predicted by PROVEAN: | A: N, C: D, E: N, F: D, G: N, H: N, I: D, K: N, L: D, M: N, N: N, P: N, Q: N, R: N, S: N, T: N, V: D, W: D, Y: D, |
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[hide] The MrpA, MrpB and MrpD subunits of the Mrp antipo... Microbiology. 2009 Jul;155(Pt 7):2137-47. Epub 2009 Apr 23. Kajiyama Y, Otagiri M, Sekiguchi J, Kudo T, Kosono S
The MrpA, MrpB and MrpD subunits of the Mrp antiporter complex in Bacillus subtilis contain membrane-embedded and essential acidic residues.
Microbiology. 2009 Jul;155(Pt 7):2137-47. Epub 2009 Apr 23., [PMID:19389778]
Abstract [show]
Bacillus subtilis Mrp is a unique Na+/H+ antiporter with a multicomponent structure consisting of the mrpABCDEFG gene products. We have previously reported that the conserved and putative membrane-embedded Glu-113, Glu-657, Asp-743 and Glu-747 of MrpA (ShaA) are essential for the transport function. In this study, we further investigated the functional involvement of the equivalent conserved acidic residues of other Mrp proteins in heterologous Escherichia coli and natural B. subtilis backgrounds. Asp-121 of MrpB and Glu-137 of MrpD were additionally identified to be essential for the transport function in both systems. Glu-137 of MrpD and Glu-113 of MrpA were found to be conserved in the homologous MrpD/MrpA proteins as well as in the homologous subunits of H+-translocating primary active transporters such as Nuo and Mbh, suggesting their critical role in ion binding. The remaining essential acidic residues clustered in the C-terminal domain of MrpA (Glu-657, Asp-743 and Glu-747) and MrpB (Asp-121); these subunits are fused in some Gram-negative species. It is possible that the MrpA, MrpB and MrpD subunits, which contain essential transmembrane acidic residues, form the ion translocation site(s) of the Mrp antiporter complex.
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No. Sentence Comment
207 The H+ -translocating F0F1-ATPase in E. coli contains the essential Asp-61 residue, which is equivalent to the Glu-65 residue that participates in Na+ binding in I. tartaricus F-ATPase (Meier et al., 2005); the Asp-61 to Glu mutant retains a partial activity of the polypeptide (Miller et al., 1990).
X
ABCC1 p.Asp61Glu 19389778:207:211
status: NEW