Editing Secretion (section)

==={{anchor|T5SS}}Type V secretion system (T5SS)===
{{See also|Trimeric autotransporter adhesin#Type V secretion system (T5SS)}}
[[Image:T5SS.svg|250px|right]]
Also called the autotransporter system,<ref name=Thanassi2005>{{cite journal | vauthors = Thanassi DG, Stathopoulos C, Karkal A, Li H | title = Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review) | journal = Molecular Membrane Biology | volume = 22 | issue = 1–2 | pages = 63–72 | year = 2005 | pmid = 16092525 | doi = 10.1080/09687860500063290 | s2cid = 2708575 }}</ref> type V secretion involves use of the ''Sec'' system for crossing the inner membrane. Proteins which use this pathway have the capability to form a [[beta-barrel]] with their C-terminus which inserts into the outer membrane, allowing the rest of the peptide (the passenger domain) to reach the outside of the cell. Often, autotransporters are cleaved, leaving the beta-barrel domain in the outer membrane and freeing the passenger domain. Some researchers believe remnants of the autotransporters gave rise to the [[porin (protein)|porins]] which form similar beta-barrel structures.{{citation needed|date=October 2019}} A common example of an autotransporter that uses this secretion system is the [[Trimeric Autotransporter Adhesins (TAA)|Trimeric Autotransporter Adhesins]].<ref name="pmid17482513">{{cite journal | vauthors = Gerlach RG, Hensel M | title = Protein secretion systems and adhesins: the molecular armory of Gram-negative pathogens | journal = International Journal of Medical Microbiology | volume = 297 | issue = 6 | pages = 401–15 | date = October 2007 | pmid = 17482513 | doi = 10.1016/j.ijmm.2007.03.017 }}</ref>