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一种新的细胞表面蛋白酶:德氏乳杆菌保加利亚亚种prtB基因的测序与分析

A new cell surface proteinase: sequencing and analysis of the prtB gene from Lactobacillus delbruekii subsp. bulgaricus.

作者信息

Gilbert C, Atlan D, Blanc B, Portailer R, Germond J E, Lapierre L, Mollet B

机构信息

Laboratoire de Microbiologie et Génétique Moléculaire, UMR CNRS 106,Université Claude Bernard-Lyon I, France.

出版信息

J Bacteriol. 1996 Jun;178(11):3059-65. doi: 10.1128/jb.178.11.3059-3065.1996.

Abstract

Investigation of the chromosomal region downstream of the lacZ gene from Lactobacillus delbrueckii subsp. bulgaricus revealed the presence of a gene (prtB) encoding a proteinase of 1,946 residues with a predicted molecular mass of 212 kDa. The deduced amino acid sequence showed that PrtB proteinase displays significant homology with the N termini and catalytic domains of lactococcal PrtP cell surface proteinases and is probably synthesized as a preproprotein. However, the presence of a cysteine near the histidine of the PrtB active site suggests that PrtB belongs to the subfamily of cysteine subtilisins. The C-terminal region strongly differs from those of PrtP proteinases by having a high lysine content, an imperfect duplication of 41 residues, and a degenerated sequence compared with the consensus sequence for proteins anchoring in the cell walls of gram-positive bacteria. Finally, the product of the truncated prtM-like gene located immediately upstream of the prtB gene seems too short to be involved in the maturation of PrtB.

摘要

对德氏乳杆菌保加利亚亚种中lacZ基因下游染色体区域的研究表明,存在一个基因(prtB),其编码一种含有1946个残基的蛋白酶,预测分子量为212 kDa。推导的氨基酸序列显示,PrtB蛋白酶与乳球菌PrtP细胞表面蛋白酶的N末端和催化结构域具有显著同源性,可能以前原蛋白的形式合成。然而,PrtB活性位点组氨酸附近存在半胱氨酸,这表明PrtB属于半胱氨酸枯草杆菌蛋白酶亚家族。C末端区域与PrtP蛋白酶的C末端区域有很大不同,其赖氨酸含量高,有41个残基的不完全重复,并且与革兰氏阳性细菌细胞壁锚定蛋白的共有序列相比有一个退化序列。最后,位于prtB基因紧上游的截短的prtM样基因的产物似乎太短,无法参与PrtB的成熟。

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