Protein Family Models

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]. This entry represents the N-terminal alpha/beta region which contains a pocket, termed the N-domain pocket, lined with residues important for ZapC function as an FtsZ bundler [2,3]. [1]. 21216997. 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. 2011;193:1393-1404. [2]. 26655719. 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. 2016;291:2485-2498. [3]. 26619764. 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. 2015;589:3822-3828. (from Pfam)

Date:

2024-10-16

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]. This is the C-terminal domain which contains a pocket with a hydrophobic centre surrounded by conserved basic residues, critical for FtsZ binding [2,3]. [1]. 21216997. 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. 2011;193:1393-1404. [2]. 26655719. 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. 2016;291:2485-2498. [3]. 26619764. 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. 2015;589:3822-3828. (from Pfam)

Date:

2024-10-16

cell division protein ZapC contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ; it acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ

Date:

2016-04-22

Gene:

zapC

Date:

2023-08-31