SepF is known to facilitate the assembly of FtsZ filaments into a ring-like structure, crucial for bacterial cell division. In bacteria lacking FtsA, SepF plays a key role in anchoring FtsZ to the cell membrane. The protein polymerizes into large rings that bundle FtsZ filaments, aiding in the formation of the Z-ring, which is essential for cell division .
Structure: SepF forms dimers that are the basic units of its filaments. The C-terminal domain of SepF contains the FtsZ binding site and is sufficient for ring formation .
Membrane Association: SepF is membrane-associated, with an amphipathic helix at its N-terminus functioning as a membrane-binding domain .
Function in Archaea: In archaea, SepF also anchors FtsZ to the membrane, suggesting a conserved role across prokaryotes .
Nocardia farcinica is a clinically relevant species known for causing infections, particularly in immunocompromised hosts. It has been associated with brain abscesses and other severe infections . The genome of N. farcinica contains numerous genes for natural product biosynthesis, including those for siderophores and other secondary metabolites .
While there is no specific information on recombinant SepF in N. farcinica, the species' genetic capabilities suggest potential for genetic manipulation. N. farcinica's genome includes multiple genes for natural product biosynthesis, indicating a robust genetic machinery that could be leveraged for expressing recombinant proteins like SepF .
Given the lack of direct research on recombinant SepF in N. farcinica, potential applications would involve understanding SepF's role in bacterial cell division and how it might be manipulated in N. farcinica. This could include studying SepF's interaction with FtsZ in N. farcinica or exploring its use as a target for antimicrobial therapies.
Cell Division Protein SepF (sepF): A cell division protein integral to the divisome complex, recruited early to the Z-ring. It likely stimulates Z-ring formation, possibly through cross-linking of FtsZ protofilaments. Its function shows overlap with that of FtsA.
KEGG: nfa:NFA_17720
STRING: 247156.nfa17720