Structure of the Extracellular Region of the Bacterial Type VIIb Secretion System Subunit EsaA.
Gram-positive bacteria use type VII secretion systems (T7SSs) to export effector proteins that manipulate the physiology of nearby prokaryotic and eukaryotic cells. Several mycobacterial T7SSs have established roles in virulence. By contrast, the genetically distinct T7SSb pathway found in Firmicutes bacteria more often functions to mediate bacterial competition. A lack of structural information on the T7SSb has limited the understanding of effector export by this protein secretion apparatus. Here, we present the 2.4 Å crystal structure of the extracellular region of the T7SSb subunit EsaA from Streptococcus gallolyticus. Our structure reveals that homodimeric EsaA is an elongated, arrow-shaped protein with a surface-accessible "tip", which in some species of bacteria serves as a receptor for lytic bacteriophages. Because it is the only T7SSb subunit large enough to traverse the peptidoglycan layer of Firmicutes, we propose that EsaA plays a critical role in transporting effectors across the entirety of the Gram-positive cell envelope.
['Klein|Timothy A|TA|', 'Grebenc|Dirk W|DW|', 'Gandhi|Shil Y|SY|', 'Shah|Vraj S|VS|', 'Kim|Youngchang|Y|', 'Whitney|John C|JC|']
D000072417:Protein Domains D034367:Streptococcus intermedius D000069377:Type VII Secretion Systems
type VII secretion T7SSb X-ray crystallography bacterial pathogenesis bacterial protein secretion interbacterial antagonism microbe-microbe interactions protein structure/function