EsxG-EsxH heterodimer is secreted by ESX-3. EsxG-EsxH heterodimer of M. tuberculosis can inhibit host endosomal sorting complex required for transport (ESCRT) machinery, raising the possibility that M. tuberculosis impairs this host response. EsxG-EsxH also facilitated secretion of several members of the proline-glutamic acid (PE) and proline-proline-glutamic acid (PPE) protein families that play roles in iron acquisition. ...
Autotransporter. Interferes with the barrier functions of mucosal IgA antibodies by cleaving secretory IgA1 in the hinge region. Phagosomal escape. ...
Secreted by type II secretion pathway. Transported to the endoplasmic reticulum (ER) via a coat protein COPI-dependent retrograde pathway dependent on a KDEL motif. ...
An N-terminal signal peptide, an internal passenger domain, and a C-terminal translocator domain. MisL is an extracellular matrix adhesin involved in intestinal colonization. ...
ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ...
N-terminal 350 residues exhibits homology with invasin of Yersinia pseudotuberculosis (49.5% identity) and intimin of E. coli O111 (enteropathogenic E. coli) (48% identity). The amino termini of invasin and intimin serve as membrane-spanning anchors in the bacterial outer membrane. ...
Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ...