Kakiuchi M, Isui A, Suzuki K, Fujino T, Fujino E, Kimura T, Karita S, Sakka K, Ohmiya K
Faculty of Bioresources, Mie University, Tsu 514, Japan.
J Bacteriol. 1998 Aug;180(16):4303-8. doi: 10.1128/JB.180.16.4303-4308.1998.
The Clostridium josui cipA and celD genes, encoding a scaffolding-like protein (CipA) and a putative cellulase (CelD), respectively, have been cloned and sequenced. CipA, with an estimated molecular weight of 120,227, consists of an N-terminal signal peptide, a cellulose-binding domain of family III, and six successive cohesin domains. The molecular architecture of C. josui CipA is similar to those of the scaffolding proteins reported so far, such as Clostridium thermocellum CipA, Clostridium cellulovorans CbpA, and Clostridium cellulolyticum CipC, but C. josui CipA is considerably smaller than the other scaffolding proteins. CelD consists of an N-terminal signal peptide, a family 48 catalytic domain of glycosyl hydrolase, and a dockerin domain. N-terminal amino acid sequence analysis of the C. josui cellulosomal proteins indicates that both CipA and CelD are major components of the cellulosome.
已克隆并测序了酒井梭菌的cipA和celD基因，它们分别编码一种支架样蛋白（CipA）和一种假定的纤维素酶（CelD）。CipA的估计分子量为120,227，由一个N端信号肽、一个III型纤维素结合结构域和六个连续的黏连蛋白结构域组成。酒井梭菌CipA的分子结构与迄今报道的支架蛋白相似，如嗜热栖热梭菌CipA、食纤维梭菌CbpA和溶纤梭菌CipC，但酒井梭菌CipA比其他支架蛋白小得多。CelD由一个N端信号肽、一个糖基水解酶48家族催化结构域和一个锚定蛋白结构域组成。对酒井梭菌纤维小体蛋白的N端氨基酸序列分析表明，CipA和CelD都是纤维小体的主要成分。
