G3DSA:3.30.70.1070

Sporulation related repeat

CATH-Gene3D entry
Member databaseCATH-Gene3D
CATH-Gene3D typehomologous superfamily

Description
Imported from IPR036680

This 70 residue domain, known as SPOR domain, is composed of two 35 residue repeats that are found in bacterial proteins involved in sporulation and cell division, such as FtsN, CwlM and RlpA. The SPOR domains in the FtsN cell division proteins from Escherichia coli and Caulobacter crescentus have been shown to bind peptidoglycan. SPOR domains can localise to the division site by binding preferentially to septal peptidoglycan
[3, 4, 6]
.

FtsN is an essential cell division protein with a simple bitopic topology: a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. The repeats lie at the periplasmic C terminus, which has an RNP-like fold
[5]
. FtsN localises to the septum ring complex. The CwlM protein is a cell wall hydrolase, where the C-terminal region, including the repeats, determines substrate specificity
[2]
. RlpA is a rare lipoprotein A protein that may be important for cell division. Its N-terminal cysteine may be attached to thioglyceride and N-fatty acyl residues
[1]
.

References
Imported from IPR036680

1.Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome. Takase I, Ishino F, Wachi M, Kamata H, Doi M, Asoh S, Matsuzawa H, Ohta T, Matsuhashi M. J. Bacteriol. 169, 5692-9, (1987). View articlePMID: 3316191

2.Genetic structure, isolation and characterization of a Bacillus licheniformis cell wall hydrolase. Kuroda A, Sugimoto Y, Funahashi T, Sekiguchi J. Mol. Gen. Genet. 234, 129-37, (1992). PMID: 1495475

3.Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA. Arends SJ, Williams K, Scott RJ, Rolong S, Popham DL, Weiss DS. J. Bacteriol. 192, 242-55, (2010). View articlePMID: 19880599

4.Bacterial SPOR domains are recruited to septal peptidoglycan by binding to glycan strands that lack stem peptides. Yahashiri A, Jorgenson MA, Weiss DS. Proc. Natl. Acad. Sci. U.S.A. 112, 11347-52, (2015). View articlePMID: 26305949

5.Solution structure and domain architecture of the divisome protein FtsN. Yang JC, Van Den Ent F, Neuhaus D, Brevier J, Lowe J. Mol. Microbiol. 52, 651-60, (2004). View articlePMID: 15101973

6.Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli. Liu B, Persons L, Lee L, de Boer PA. Mol Microbiol 95, 945-70, (2015). PMID: 25496160

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