{PDOC51724}
{PS51724; SPOR}
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* SPOR domain profile *
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The SPOR  domain  is  named after the founding member of the protein family, a
Bacillus subtilis  cell  wall  amidase  named CwlC that is produced relatively
late in  the  process  of  sporulation. SPOR domain proteins are widespread in
bacteria, many  of  these  proteins  are  involved  in  sporulation  and  cell
division, and  SPOR  domains  are  sufficient for septal localization, probaly
because SPOR domains bind to septal peptidoglycan (PG) [1,2,3,4,5].

The SPOR  domain  is ~75 amino acid long. It comprises two tandem repeats that
fold into  a  pseudo-2-fold  symmetric  single-domain structure consisting of a
BetaAlphaBetaBetaAlphaBeta-fold containing   numerous   contacts  between  the
repeats (see   <PDB:1X60>).  Hydrophobic  residues  important  for  structural
integrity are  conserved  between  the repeats, and are located symmetrically.
The SPOR   domain  assembles  into  a  four-stranded  antiparallel  beta-sheet
buttressed on one side by two alpha-helices [1,2,5].

Some proteins kwown to contain a SPOR domain are listed below:

 - Bacteria  CwlC, a sporulation protein which comprises an N-terminal amidase
   domain and  a  C-terminal SPOR domain. It facilitates release of the mature
   spore by degrading PG in the mother cell.
 - Bacteria DamX, a bitopic inner membrane division protein.
 - Bacteria  FtsN,  a  bitopic  inner  membrane  protein  essential  for  cell
   division.
 - Bacteria DedD, a bitopic inner membrane protein that contributes to the
   cell constriction process.
 - Bacteria RlpA, a predicted outer membrane lipoprotein.

The profile we developed covers the entire SPOR domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: July 2014 / First entry.

[ 1] Yang J.C., Van Den Ent F., Neuhaus D., Brevier J., Lowe J.
     "Solution structure and domain architecture of the divisome protein
     FtsN."
     Mol. Microbiol. 52:651-660(2004).
     PubMed=15101973; DOI=10.1111/j.1365-2958.2004.03991.x
[ 2] Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., Kojima C.
     "Solution structure of the peptidoglycan binding domain of Bacillus
     subtilis cell  wall lytic enzyme CwlC: characterization of the
     sporulation-related repeats by NMR."
     Biochemistry 44:10153-10163(2005).
     PubMed=16042392; DOI=10.1021/bi050624n
[ 3] Gerding M.A., Liu B., Bendezu F.O., Hale C.A., Bernhardt T.G.,
     de Boer P.A.J.
     "Self-enhanced accumulation of FtsN at Division Sites and Roles for
     Other Proteins with a SPOR domain (DamX, DedD, and RlpA) in
     Escherichia coli cell constriction."
     J. Bacteriol. 191:7383-7401(2009).
     PubMed=19684127; DOI=10.1128/JB.00811-09
[ 4] Arends S.J.R, Williams K., Scott R.J., Rolong S., Popham D.L.,
     Weiss D.S.
     "Discovery and characterization of three new Escherichia coli septal
     ring proteins that contain a SPOR domain: DamX, DedD, and RlpA."
     J. Bacteriol. 192:242-255(2010).
     PubMed=19880599; DOI=10.1128/JB.01244-09
[ 5] Williams K.B., Yahashiri A., Arends S.J.R., Popham D.L., Fowler C.A.,
     Weiss D.S.
     "Nuclear magnetic resonance solution structure of the
     peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights
     into septal localization."
     Biochemistry 52:627-639(2013).
     PubMed=23290046; DOI=10.1021/bi301609e

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