ABCC1 p.Pro669Ala
| Predicted by SNAP2: | A: N (53%), C: N (61%), D: D (66%), E: N (72%), F: D (63%), G: N (61%), H: N (57%), I: D (66%), K: N (93%), L: D (66%), M: N (72%), N: D (59%), Q: N (87%), R: N (72%), S: N (72%), T: D (53%), V: D (59%), W: D (71%), Y: D (59%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, K: D, L: D, M: D, N: D, Q: D, R: D, S: D, T: D, V: D, W: D, Y: D, |
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[hide] The Vibrio cholerae Mrp system: cation/proton anti... J Mol Microbiol Biotechnol. 2009;16(3-4):176-86. Epub 2008 Mar 3. Dzioba-Winogrodzki J, Winogrodzki O, Krulwich TA, Boin MA, Hase CC, Dibrov P
The Vibrio cholerae Mrp system: cation/proton antiport properties and enhancement of bile salt resistance in a heterologous host.
J Mol Microbiol Biotechnol. 2009;16(3-4):176-86. Epub 2008 Mar 3., [PMID:18311075]
Abstract [show]
The mrp operon from Vibrio cholerae encoding a putative multisubunit Na(+)/H(+) antiporter was cloned and functionally expressed in the antiporter-deficient strain of Escherichia coli EP432. Cells of EP432 expressing Vc-Mrp exhibited resistance to Na(+) and Li(+) as well as to natural bile salts such as sodium cholate and taurocholate. When assayed in everted membrane vesicles of the E. coli EP432 host, Vc-Mrp had sufficiently high antiport activity to facilitate the first extensive analysis of Mrp system from a Gram-negative bacterium encoded by a group 2 mrp operon. Vc-Mrp was found to exchange protons for Li(+), Na(+), and K(+) ions in pH-dependent manner with maximal activity at pH 9.0-9.5. Exchange was electrogenic (more than one H(+) translocated per cation moved in opposite direction). The apparent K(m) at pH 9.0 was 1.08, 1.30, and 68.5 mM for Li(+), Na(+), and K(+), respectively. Kinetic analyses suggested that Vc-Mrp operates in a binding exchange mode with all cations and protons competing for binding to the antiporter. The robust ion antiport activity of Vc-Mrp in sub-bacterial vesicles and its effect on bile resistance of the heterologous host make Vc-Mrp an attractive experimental model for the further studies of biochemistry and physiology of Mrp systems.
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No. Sentence Comment
46 Sequence analyses of the cloned operon revealed several nucleotide substitutions compared to the sequence of the genomic mrp published at http://www.tigr.org for V. cholerae biotype El Tor resulting in a few deviations at the amino acid level, namely, seven following substitutions were found: in Vc-MrpA`, I12T (ATC ] ACC), V657M (GTG ] ATG), P669A (CCG ] GCG), and V739I (GTC ] ATC); in Vc-MrpD, P105L (CCC ] CTC) and Q439P (CAA ] CCG); in Vc-MrpE, I68V (ATC ] GTC).
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ABCC1 p.Pro669Ala 18311075:46:344
status: NEW