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PROSITE documentation PDOC51724

SPOR domain profile





Description

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 βαββαβ-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 β-sheet buttressed on one side by two α-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.

Last update:

July 2014 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

SPOR, PS51724; SPOR domain profile  (MATRIX)


References

1AuthorsYang J.C. Van Den Ent F. Neuhaus D. Brevier J. Lowe J.
TitleSolution structure and domain architecture of the divisome protein FtsN.
SourceMol. Microbiol. 52:651-660(2004).
PubMed ID15101973
DOI10.1111/j.1365-2958.2004.03991.x

2AuthorsMishima M. Shida T. Yabuki K. Kato K. Sekiguchi J. Kojima C.
TitleSolution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
SourceBiochemistry 44:10153-10163(2005).
PubMed ID16042392
DOI10.1021/bi050624n

3AuthorsGerding M.A. Liu B. Bendezu F.O. Hale C.A. Bernhardt T.G. de Boer P.A.J.
TitleSelf-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.
SourceJ. Bacteriol. 191:7383-7401(2009).
PubMed ID19684127
DOI10.1128/JB.00811-09

4AuthorsArends S.J.R Williams K. Scott R.J. Rolong S. Popham D.L. Weiss D.S.
TitleDiscovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA.
SourceJ. Bacteriol. 192:242-255(2010).
PubMed ID19880599
DOI10.1128/JB.01244-09

5AuthorsWilliams K.B. Yahashiri A. Arends S.J.R. Popham D.L. Fowler C.A. Weiss D.S.
TitleNuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights into septal localization.
SourceBiochemistry 52:627-639(2013).
PubMed ID23290046
DOI10.1021/bi301609e



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