A putative lipoprotein of Sphingomonas sp. strain A1 binds alginate rather than a lipid moiety |
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Authors: | He Jinshan Ochiai Akihito Fukuda Yasuki Hashimoto Wataru Murata Kousaku |
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Affiliation: | Laboratory of Basic and Applied Molecular Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, Japan. |
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Abstract: | Gram-negative Sphingomonas sp. strain A1 accumulates alginate in the cell surface pit and directly incorporates the polysaccharide into its cytoplasm through a 'superchannel'. A cell surface protein Algp7 (27 kDa) is inducibly expressed in the presence of alginate. Although the protein Algp7 was initially classified as a lipoprotein based on its primary structure, Algp7 purified from strain A1 cells did not possess a lipid moiety. Algp7 bound alginate efficiently at a neutral pH with a K(d) of 3.6 x 10(-8) M, suggesting that the cell surface protein contributed to accumulation of alginate in the pit. |
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