SMART: Pfam domain T2SSL

T2SSL

PFAM accession number:	PF05134
Interpro abstract (IPR024230):	The general secretion pathway of Gram-negative bacteria is responsible for extracellular secretion of a number of different proteins, including proteases and toxins. This pathway supports secretion of proteins across the cell envelope in two distinct steps, in which the second step, involving translocation through the outer membrane, is assisted by at least 13 different gene products. GspL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein GspE. It is thought that the tri-molecular complex of GspL, GspE and GspM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation [ (PUBMED:10322014) ]. This N-terminal domain is found in general secretion pathway protein L sequences from several Gram-negative bacteria. It is a cytoplasmic domain that shows structural homology with the superfamily of actin-like ATPases. However, it is entirely missing domains 1B and 2B of the actin-like ATPases. As domain 2B of the actin-like superfamily is critically important for binding the adenosine part of ATP and absent altogether in cyto-EpsL, it is therefore unlikely that EpsL is an ATP-binding protein [ (PUBMED:15533433) ].

PFAM accession number:

PF05134

Interpro abstract (IPR024230):

The general secretion pathway of Gram-negative bacteria is responsible for extracellular secretion of a number of different proteins, including proteases and toxins. This pathway supports secretion of proteins across the cell envelope in two distinct steps, in which the second step, involving translocation through the outer membrane, is assisted by at least 13 different gene products. GspL is predicted to contain a large cytoplasmic domain and has been shown to interact with the autophosphorylating cytoplasmic membrane protein GspE. It is thought that the tri-molecular complex of GspL, GspE and GspM might be involved in regulating the opening and closing of the secretion pore and/or transducing energy to the site of outer membrane translocation [ (PUBMED:10322014) ].

This N-terminal domain is found in general secretion pathway protein L sequences from several Gram-negative bacteria. It is a cytoplasmic domain that shows structural homology with the superfamily of actin-like ATPases. However, it is entirely missing domains 1B and 2B of the actin-like ATPases. As domain 2B of the actin-like superfamily is critically important for binding the adenosine part of ATP and absent altogether in cyto-EpsL, it is therefore unlikely that EpsL is an ATP-binding protein [ (PUBMED:15533433) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry T2SSL