Kroyer J, Chang S
Gene. 1981 Dec;15(4):343-7. doi: 10.1016/0378-1119(81)90177-3.
Penicillinase (beta-lactamase) is a major species of secreted protein produced by Bacillus licheniformis 749. From the pTB2 recombinant plasmid containing the cloned entire penicillinase (penP) gene, we have isolated and sequenced a 446-bp HpaII fragment carrying the beginning of penP. The 3'-end coding region of 216-bp on this DNA fragment codes for the first 72 amino acids of the prepenicillinase protein. The deduced structure of the leader peptide consists of a 34 amino acid signal sequence with a hydrophilic N-terminal region and a central hydrophobic core.
青霉素酶(β-内酰胺酶)是地衣芽孢杆菌749分泌的主要蛋白质种类。从含有克隆的完整青霉素酶(penP)基因的pTB2重组质粒中,我们分离并测序了一个携带penP起始部分的446 bp HpaII片段。该DNA片段上216 bp的3'端编码区编码前青霉素酶蛋白的前72个氨基酸。推导的前导肽结构由一个34个氨基酸的信号序列组成,其N端区域亲水,中间为疏水核心。