Target type: cellularcomponent
A protein complex required for prokaryotic cell division (FtsZ-dependent cytokinesis). These complexes are assembled and recruited to the cell septum in a strictly controlled sequence and co-ordinate invagination of the cell membrane, inward growth of the peptidoglycan layer, constriction of the outer membrane and separation of daughter cells. [GOC:bhm, PMID:15165235, PMID:21784946]
The divisome complex is a dynamic and intricate assembly of proteins that orchestrates bacterial cell division. It is localized at the future division site and comprises several key components:
**1. FtsZ:**
- A tubulin-like protein that forms a ring-like structure, known as the Z-ring, at the division site.
- This ring is crucial for defining the division plane and recruiting other divisome components.
- It acts as a scaffold, organizing and concentrating other essential proteins.
**2. FtsA:**
- An adaptor protein that links FtsZ to the cytoplasmic membrane.
- It stabilizes the Z-ring and facilitates its constriction.
- Plays a role in recruiting other divisome proteins, including FtsK and ZipA.
**3. ZipA:**
- Another adaptor protein that anchors FtsZ to the membrane.
- It strengthens the Z-ring and enhances its stability.
- Works in conjunction with FtsA to ensure proper Z-ring assembly and constriction.
**4. FtsK:**
- A DNA translocase that ensures proper segregation of chromosomes during division.
- It helps to disentangle and separate the replicated DNA molecules, preventing them from being trapped in the dividing cells.
- Interacts with the Z-ring and other divisome components.
**5. FtsI (PBP3):**
- A penicillin-binding protein (PBP) that synthesizes peptidoglycan, the major component of the bacterial cell wall.
- It is responsible for the insertion of new peptidoglycan units, leading to the formation of the septum that separates the dividing cells.
- Acts as a transpeptidase, catalyzing the cross-linking of peptidoglycan chains.
**6. FtsQ, FtsL, and FtsB:**
- These proteins form a complex that interacts with FtsI and other divisome components.
- They are essential for the proper assembly and function of the divisome complex.
- Contribute to the regulation of peptidoglycan synthesis and septum formation.
**7. Other Divisome Proteins:**
- Several other proteins are involved in the divisome complex, including:
- **FtsN:** A peptidoglycan hydrolase that helps to remodel the septum during division.
- **FtsW:** A protein that interacts with FtsI and contributes to peptidoglycan synthesis.
- **FtsX:** A protein that regulates the activity of FtsI.
The divisome complex undergoes dynamic changes throughout the division process, with the recruitment and activity of its components tightly regulated. These proteins work together to ensure precise localization of the division site, proper chromosome segregation, and the synthesis of a new cell wall, ultimately leading to the formation of two daughter cells.'
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Protein | Definition | Taxonomy |
---|---|---|
Cell division protein FtsZ | A cell division protein FtsZ that is encoded in the genome of Escherichia coli K-12. [PRO:DNx, UniProtKB:P0A9A6] | Escherichia coli K-12 |
Compound | Definition | Classes | Roles |
---|---|---|---|
dapi | DAPI: RN given refers to parent cpd. | indoles | fluorochrome |
Berberine chloride (TN) | organic molecular entity | ||
dichamanetin | dichamanetin: structure in first source | diarylheptanoid | metabolite |
cinnamaldehyde | (E)-cinnamaldehyde : The E (trans) stereoisomer of cinnamaldehyde, the parent of the class of cinnamaldehydes. 3-phenylprop-2-enal : A member of the class of cinnamaldehydes that is prop-2-enal in which a hydrogen at position 3 has been replaced by a phenyl group. The configuration of the double bond is not specified; the name "cinnamaldehyde" is widely used to refer to the E (trans) isomer. | 3-phenylprop-2-enal; cinnamaldehydes | antifungal agent; EC 4.3.1.24 (phenylalanine ammonia-lyase) inhibitor; flavouring agent; hypoglycemic agent; plant metabolite; sensitiser; vasodilator agent |
chrysophaentin a | chrysophaentin A: structure in first source |