Hantke Klaus
Mikrobiologie/Membranphysiologie, Universität Tübingen, Auf der Morgenstelle 28, D-72076 Tübingen, Germany.
Curr Opin Microbiol. 2005 Apr;8(2):196-202. doi: 10.1016/j.mib.2005.02.001.
Many bacteria use an ABC transporter for high-affinity uptake of zinc with a cluster 9 solute-binding protein. Other members of this protein family transport manganese. At present, it is not always possible to distinguish zinc-specific and manganese-specific transporters on the basis of sequence analysis. Low-affinity ZIP-type zinc transporters in bacteria have also been identified. Most high-affinity zinc uptake systems are regulated by Zur proteins, which form at least three unrelated subgroups of the Fur protein family (regulators of iron transport). High-affinity transport of zinc out of the periplasmic space poses a problem to the cell because zinc is a cofactor of several periplasmic enzymes. Certain zinc-binding proteins in the periplasm might function as chaperones to supply these enzymes with zinc.
许多细菌利用一种ABC转运蛋白，通过9簇溶质结合蛋白对锌进行高亲和力摄取。该蛋白家族的其他成员运输锰。目前，基于序列分析并不总是能够区分锌特异性转运蛋白和锰特异性转运蛋白。细菌中低亲和力的ZIP型锌转运蛋白也已被鉴定出来。大多数高亲和力锌摄取系统受Zur蛋白调控，Zur蛋白形成了铁转运调节蛋白（Fur蛋白家族）至少三个不相关的亚组。将锌从周质空间高亲和力转运出去对细胞来说是个问题，因为锌是几种周质酶的辅因子。周质中的某些锌结合蛋白可能作为伴侣蛋白为这些酶提供锌。
