Erni B, Zanolari B
J Biol Chem. 1986 Dec 15;261(35):16398-403.
The glucose-permease (IIGlc) of the bacterial phosphotransferase system mediates sugar transport across the cytoplasmic membrane concomitant with sugar phosphorylation. It also functions as a receptor for bacterial chemotaxis. The structural gene of the permease, ptsG, has been cloned on a multicopy plasmid, and transformants constitutively overproducing the protein 10-15 times over wild-type level have been isolated. Overproduction is slightly inhibited if transformants are grown in a glucose-containing medium. The complete amino acid sequence of the glucose-permease is deduced from the nucleotide sequence. It consists of 477 residues and is moderately hydrophobic. A comparison of the glucose-permease with the mannitol-permease (Lee, C. A., and Saier, M. H., Jr. (1983) J. Biol. Chem. 258, 10761-10767) does not reveal any obvious homology at the level of amino acid sequence.
细菌磷酸转移酶系统的葡萄糖通透酶（IIGlc）介导糖跨细胞质膜的转运，并伴随糖的磷酸化。它还作为细菌趋化性的受体发挥作用。通透酶的结构基因ptsG已被克隆到多拷贝质粒上，并且已经分离出组成型过量表达该蛋白且表达量比野生型水平高10 - 15倍的转化体。如果转化体在含葡萄糖的培养基中生长，过量表达会受到轻微抑制。葡萄糖通透酶的完整氨基酸序列由核苷酸序列推导得出。它由477个残基组成，具有中等疏水性。将葡萄糖通透酶与甘露醇通透酶（Lee, C. A., 和Saier, M. H., Jr. (1983) J. Biol. Chem. 258, 10761 - 10767）进行比较，在氨基酸序列水平上未发现任何明显的同源性。
