InterPro : IPR005807

Name  SecE subunit of protein translocation complex Short Name  SecE_bac
Type  Family Description  Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocasepathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them tothe translocase component []. From there, the mature proteins are either targeted to the outermembrane, or remain as periplasmic proteins. The translocase protein subunits are encoded on the bacterialchromosome.The translocase itself comprises 7 proteins, including a chaperone protein (SecB), an ATPase (SecA), an integralmembrane complex (SecCY, SecE and SecG), and two additional membrane proteins that promote the release ofthe mature peptide into the periplasm (SecD and SecF) []. The chaperone protein SecB []is a highly acidic homotetrameric protein that exists as a "dimer of dimers" in the bacterial cytoplasm.SecB maintains preproteins in an unfolded state after translation, and targets these to the peripheral membraneprotein ATPase SecA for secretion []. SecE, part of the main SecYEG translocase complex, is ~106 residues in length, and spans the inner membrane of the Gram-negative bacterial envelope. Together withSecY and SecG, SecE forms a multimeric channel through which preproteinsare translocated, using both proton motive forces and ATP-driven secretion. The latter is mediated by SecA. The structure of theEscherichia coliSecYEG assembly revealed a sandwich of two membranes interacting through the extensive cytoplasmicdomains []. Each membrane is composed of dimers of SecYEG. The monomeric complex contains 15transmembrane helices.
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Proteins

InterPro protein domain ID --> Contigs

 

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1 Parent Features

Id Name Short Name Type
IPR001901 Protein translocase complex, SecE/Sec61-gamma subunit Translocase_SecE/Sec61-g Family

4 Publications

First Author Title Year Journal Volume Pages
Bieker KL The sec and prl genes of Escherichia coli. 1990 J Bioenerg Biomembr 22 291-310
Driessen AJ SecB, a molecular chaperone with two faces. 2001 Trends Microbiol 9 193-6
Müller JP Effects of pre-protein overexpression on SecB synthesis in Escherichia coli. 1999 FEMS Microbiol Lett 176 219-27
Breyton C Three-dimensional structure of the bacterial protein-translocation complex SecYEG. 2002 Nature 418 662-5



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)