D
IPR048373

Cell-division protein ZapC, N-terminal

InterPro entry
Short nameZapC_N

Description

This entry represents the N-terminal α/β region which contains a pocket, termed the N-domain pocket, lined with residues important for ZapC function as an FtsZ bundler
[2, 3]
. This domain is related to chromo domains (
IPR016197
), whereas the C-terminal domain of ZapC has similarity to Tudor domains (
IPR002999
).

ZapC is one of four FtsZ-binding components of the Z ring in bacteria. Formation of the Z ring on the cytoplasmic surface of the membrane is the starting process for assembly of the cell-division apparatus. It binds directly to the Z ring, and although it is not essential for absolute cell division it contributes to it by enhancing the interactions between the FtsZ protofilaments (or polymers) which aggregate to form the ring conformation in the Z ring
[1]
.

References

1.Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymers. Hale CA, Shiomi D, Liu B, Bernhardt TG, Margolin W, Niki H, de Boer PA. J. Bacteriol. 193, 1393-404, (2011). View articlePMID: 21216997

2.Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC. Schumacher MA, Zeng W, Huang KH, Tchorzewski L, Janakiraman A. J Biol Chem 291, 2485-98, (2016). PMID: 26655719

3.Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli. Ortiz C, Kureisaite-Ciziene D, Schmitz F, McLaughlin SH, Vicente M, Lowe J. FEBS Lett 589, 3822-8, (2015). PMID: 26619764

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.