|PROSITE documentation PDOC51779|
The polypeptide-transport-associated (POTRA) domain is a module found in members of the FtsQ/DivIB, ShlB, CGI51 (with one repeat), Toc75, YTFM (with three repeats) and D15 (with five repeats) protein families. The POTRA domains are hypothesized to mediate protein-protein interactions, nucleate β-strands formation in nascent outer membrane proteins (OMPs) and have chaperone-like activity [1,2,3,4,5].
The POTRA domain fold comprises a three-stranded β-sheet overlaid with a pair of antiparallel helices. The order of secondary-structure elements is β-α-α-β-β; the first and second β strands form the two edges of the sheet, with the β3 strand sandwiched between them (see <PDB:4QKY>). The conserved residues that define the POTRA domains are primarily in the hydrophobic core or loop regions, suggesting that they are important for the structural integrity of POTRA domain [2,3,4,5].
Some proteins known to contain a POTRA domain are listed below:
The profile we developed covers the entire POTRA domain.Last update:
October 2015 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Sanchez-Pulido L. Devos D. Genevrois S. Vicente M. Valencia A.|
|Title||POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins.|
|Source||Trends Biochem. Sci. 28:523-526(2003).|
|2||Authors||Kim S. Malinverni J.C. Sliz P. Silhavy T.J. Harrison S.C. Kahne D.|
|Title||Structure and function of an essential component of the outer membrane protein assembly machine.|
|3||Authors||Gatzeva-Topalova P.Z. Walton T.A. Sousa M.C.|
|Title||Crystal structure of YaeT: conformational flexibility and substrate recognition.|
|4||Authors||van den Ent F. Vinkenvleugel T.M.F. Ind A. West P. Veprintsev D. Nanninga N. den Blaauwen T. Loewe J.|
|Title||Structural and mutational analysis of the cell division protein FtsQ.|
|Source||Mol. Microbiol. 68:110-123(2008).|
|5||Authors||Gatzeva-Topalova P.Z. Warner L.R. Pardi A. Sousa M.C.|
|Title||Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane.|