丝氨酸蛋白酶自动转运家族（SPATE）是指致病性肠道杆菌通过自动转运的方式产生的一类毒性蛋白。此类蛋白的氨基酸同源性可达35%～55％，均由3个部分组成：N端信号肽序列，协助分泌性毒性蛋白穿越细菌内膜；中部载乘区域，是发挥各种生物学功能的主要结构域；C端转运单位，促使载乘结构域自细菌周浆间隙向胞外分泌。α螺旋的铰链区，连接载乘区域和C端转运单位，其中14个氨基酸残基的组成序列EVNNLNKRMGDLRD非常保守，是蛋白酶水解位点，也是整个蛋白中最长的保守氨基酸序列，在SPATE的分泌和成熟过程中起着十分重要的作用,其改变往往会引起该蛋白家族不能正常分泌和成熟。目前有研究将其作为药物作用的新靶点。本文就SPATE的转运、分泌以及结构与功能的关系作一简要综述。

Serine protease auto-transporters (SPATEs) belong to a group of virulent proteins that are secreted via the type V auto-transporter pathway by pathogenic enterobacteria. Structural analysis shows that proteins in this family have amino acid identities ranging from 35% to 55%, comprising a cleavable N-terminal signal sequence, an internal passenger domain, and a C-terminal translocator domain. N-terminal signal peptides help proteins to transfer SPATEs through inner membrane structure, the structural arrangement of the passenger domain determines the protein’s virulence among other functions, and the C-terminal domain allows secretion of the passenger protein. The linker of all known SPATEs is a conserved 14 amino acid sequence EVNNLNKRMGDLRD, which plays an important role in the protein’s secretion and maturation. Researchers are now focusing on the development of new anti-microbial agents targeting this conserved 14 amino acid sequence. In this review, the special virulent proteins will be discussed by analyzing their structure, transportation, secretion, and virulent functions.