{PDOC51779}
{PS51779; POTRA}
{BEGIN}
************************
* POTRA domain profile *
************************

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  beta-
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 beta-sheet overlaid with a
pair of  antiparallel  helices.  The  order of secondary-structure elements is
beta-alpha-alpha-beta-beta; the  first  and  second  beta strands form the two
edges of  the  sheet,  with  the  beta3  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:

 - Escherichia  coli  outer membrane protein assembly factor BamA, involved in
   assembly and insertion of beta-barrel proteins into the outer membrane.
 - Escherichia coli cell division protein FtsQ.
 - Bacillus subtilis cell division protein DivIB.
 - Serratia  marcescens hemolysin transporter protein ShlB, a virulence-factor
   transporter that is present in the outer membrane.
 - Arabidopsis thaliana chloroplastic protein TOC75, mediates the insertion of
   proteins targeted to the outer membrane of chloroplasts.
 - Human  sorting and assembly machinery component 50 (SAM50), plays a crucial
   role in  the  maintenance of the structure of mitochondrial cristae and the
   proper assembly of the mitochondrial respiratory chain complexes.

The profile we developed covers the entire POTRA domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2015 / First entry.

[ 1] Sanchez-Pulido L., Devos D., Genevrois S., Vicente M., Valencia A.
     "POTRA: a conserved domain in the FtsQ family and a class of
     beta-barrel outer membrane proteins."
     Trends Biochem. Sci. 28:523-526(2003).
     PubMed=14559180
[ 2] Kim S., Malinverni J.C., Sliz P., Silhavy T.J., Harrison S.C.,
     Kahne D.
     "Structure and function of an essential component of the outer
     membrane protein assembly machine."
     Science 317:961-964(2007).
     PubMed=17702946; DOI=10.1126/science.1143993
[ 3] Gatzeva-Topalova P.Z., Walton T.A., Sousa M.C.
     "Crystal structure of YaeT: conformational flexibility and substrate
     recognition."
     Structure 16:1873-1881(2008).
     PubMed=19081063; DOI=10.1016/j.str.2008.09.014
[ 4] van den Ent F., Vinkenvleugel T.M.F., Ind A., West P., Veprintsev D.,
     Nanninga N., den Blaauwen T., Loewe J.
     "Structural and mutational analysis of the cell division protein
     FtsQ."
     Mol. Microbiol. 68:110-123(2008).
     PubMed=18312270; DOI=10.1111/j.1365-2958.2008.06141.x
[ 5] Gatzeva-Topalova P.Z., Warner L.R., Pardi A., Sousa M.C.
     "Structure and flexibility of the complete periplasmic domain of BamA:
     the protein insertion machine of the outer membrane."
     Structure 18:1492-1501(2010).
     PubMed=21070948; DOI=10.1016/j.str.2010.08.012

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}