ftsZ

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005525 GTP binding	IBA GO_REF:0000033	ACCEPT	Summary: FtsZ is a well-established GTP-binding protein. The UniProt record documents multiple GTP binding residues with experimental evidence from crystal structures. GTP binding is essential for FtsZ polymerization and function. Reason: GTP binding is a core molecular function of FtsZ. The UniProt entry states "Binds GTP and shows GTPase activity" and documents specific GTP-binding residues determined by X-ray crystallography. The deep research review confirms that "GTP binding and hydrolysis control filament assembly dynamics, subunit turnover, and ring remodeling" (ftsZ-deep-research-falcon.md). Supporting Evidence: UniProt:P17865 Binds GTP and shows GTPase activity file:BACSU/ftsZ/ftsZ-deep-research-falcon.md GTP binding and hydrolysis control filament assembly dynamics, subunit turnover, and ring remodeling
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: FtsZ localizes to the cytoplasm where it assembles at the inner surface of the cytoplasmic membrane at midcell. The UniProt record confirms cytoplasmic localization. Reason: Cytoplasm is the appropriate cellular component annotation. FtsZ is a soluble cytoplasmic protein that assembles at the membrane-proximal midcell region. UniProt explicitly states FtsZ assembles at midcell at the inner surface of the cytoplasmic membrane. Supporting Evidence: UniProt:P17865 Note=Assembles at midcell at the inner surface of the cytoplasmic membrane
GO:0051301 cell division	IBA GO_REF:0000033	ACCEPT	Summary: FtsZ is essential for cell division in B. subtilis, forming the Z-ring that scaffolds the divisome. This is the canonical and most fundamental biological process for FtsZ. Reason: Cell division is the core biological process for FtsZ. The UniProt FUNCTION states FtsZ is an essential cell division protein. The deep research confirms FtsZ as a conserved tubulin-like GTPase that scaffolds recruitment/organization of the divisome for septal peptidoglycan synthesis and cytokinesis (ftsZ-deep-research-falcon.md). Supporting Evidence: UniProt:P17865 Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site file:BACSU/ftsZ/ftsZ-deep-research-falcon.md FtsZ is a conserved tubulin-like GTPase that polymerizes into head-to-tail protofilaments and assembles at midcell into the Z-ring, which scaffolds recruitment/organization of the divisome for septal peptidoglycan synthesis and cytokinesis
GO:0003924 GTPase activity	IBA GO_REF:0000033	ACCEPT	Summary: FtsZ exhibits intrinsic GTPase activity that is essential for its function. GTP hydrolysis drives protofilament dynamics and treadmilling. This activity is directly demonstrated biochemically. Reason: GTPase activity is a core molecular function of FtsZ. UniProt states FtsZ binds GTP and shows GTPase activity. Multiple publications demonstrate this activity, and it is critical for FtsZ protofilament dynamics. The deep research notes that GTP hydrolysis is required for polymerization dynamics and filament turnover. Supporting Evidence: UniProt:P17865 Binds GTP and shows GTPase activity file:BACSU/ftsZ/ftsZ-deep-research-falcon.md GTP hydrolysis is required for polymerization dynamics and filament turnover
GO:0032153 cell division site	IBA GO_REF:0000033	ACCEPT	Summary: FtsZ assembles at the cell division site (midcell) to form the Z-ring. This is the primary subcellular localization for its function in cytokinesis. Reason: The cell division site is the precise localization where FtsZ carries out its function. UniProt states FtsZ assembles at midcell. The deep research confirms the Z-ring forms at midcell adjacent to the inner membrane. Supporting Evidence: UniProt:P17865 Note=Assembles at midcell at the inner surface of the cytoplasmic membrane file:BACSU/ftsZ/ftsZ-deep-research-falcon.md The Z-ring forms at midcell adjacent to the inner membrane
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: FtsZ binds GTP specifically. The parent term nucleotide binding is technically correct but less informative than the more specific GTP binding annotation. Reason: While nucleotide binding is correct, it is redundant with the more specific GO:0005525 (GTP binding) annotation. However, as an IEA annotation from keyword mapping, it is acceptable to retain alongside the more specific IBA annotation for GTP binding. Supporting Evidence: UniProt:P17865 Binds GTP and shows GTPase activity
GO:0000917 division septum assembly	IEA GO_REF:0000043	ACCEPT	Summary: FtsZ is essential for division septum assembly as the Z-ring recruits the machinery for septal wall synthesis. This is a core biological process for FtsZ. Reason: Division septum assembly accurately describes a key biological process involving FtsZ. The Z-ring scaffolds recruitment of late division proteins that catalyze septal peptidoglycan synthesis. UniProt function states the Z-ring serves to recruit other cell division proteins to the septum. Supporting Evidence: UniProt:P17865 One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells
GO:0003924 GTPase activity	IEA GO_REF:0000120	ACCEPT	Summary: Duplicate annotation for GTPase activity from automated methods. The IBA annotation provides equivalent support. Reason: This is a duplicate of the IBA annotation for GTPase activity. Both are correct and represent independent evidence supporting the same molecular function. It is acceptable to have multiple annotations with different evidence codes for well-established functions. Supporting Evidence: UniProt:P17865 Binds GTP and shows GTPase activity
GO:0005525 GTP binding	IEA GO_REF:0000120	ACCEPT	Summary: Duplicate annotation for GTP binding from combined automated methods. Consistent with the IBA annotation. Reason: This IEA annotation for GTP binding is a duplicate of the IBA annotation but derived from different automated methods. Both correctly annotate the same molecular function with structural evidence. Supporting Evidence: UniProt:P17865 Binds GTP and shows GTPase activity
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: Duplicate annotation for cytoplasm localization from automated methods. Reason: This IEA annotation for cytoplasm is a duplicate of the IBA annotation but derived from different automated methods. Both correctly annotate the same cellular component. Supporting Evidence: UniProt:P17865 Note=Assembles at midcell at the inner surface of the cytoplasmic membrane
GO:0030428 cell septum	IEA GO_REF:0000117	ACCEPT	Summary: FtsZ localizes to the cell septum where it forms the Z-ring that scaffolds septum formation. This is an appropriate cellular component annotation. Reason: Cell septum is an appropriate localization annotation for FtsZ, which assembles at the septum site. The deep research confirms FtsZ scaffolds recruitment/organization of the divisome for septal peptidoglycan synthesis and cytokinesis. Supporting Evidence: UniProt:P17865 Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site file:BACSU/ftsZ/ftsZ-deep-research-falcon.md FtsZ is a conserved tubulin-like GTPase that polymerizes into head-to-tail protofilaments and assembles at midcell into the Z-ring, which scaffolds recruitment/organization of the divisome for septal peptidoglycan synthesis and cytokinesis
GO:0032153 cell division site	IEA GO_REF:0000104	ACCEPT	Summary: Duplicate annotation for cell division site from automated transfer methods. Reason: This IEA annotation duplicates the IBA annotation for cell division site. Both are correct and consistent with the known localization of FtsZ at midcell. Supporting Evidence: UniProt:P17865 Note=Assembles at midcell at the inner surface of the cytoplasmic membrane
GO:0043093 FtsZ-dependent cytokinesis	IEA GO_REF:0000104	ACCEPT	Summary: This term directly references FtsZ and describes the cytokinesis process that depends on FtsZ function. This is the most specific biological process term for FtsZ. Reason: FtsZ-dependent cytokinesis is the most appropriate and specific biological process annotation for FtsZ itself. FtsZ is essential for this process and defines the pathway. The deep research confirms FtsZ's essential role in bacterial cytokinesis. Supporting Evidence: UniProt:P17865 Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site file:BACSU/ftsZ/ftsZ-deep-research-falcon.md FtsZ is a conserved tubulin-like GTPase that polymerizes into head-to-tail protofilaments and assembles at midcell into the Z-ring, which scaffolds recruitment/organization of the divisome for septal peptidoglycan synthesis and cytokinesis
GO:0051258 protein polymerization	IEA GO_REF:0000104	ACCEPT	Summary: FtsZ self-polymerizes into protofilaments in a GTP-dependent manner. This is a core aspect of FtsZ function. Reason: Protein polymerization accurately describes FtsZ's ability to self-assemble into protofilaments. UniProt states FtsZ polymerizes to form a dynamic ring structure in a GTP-dependent manner. The deep research confirms FtsZ monomers bind GTP and assemble into polar protofilaments. Supporting Evidence: UniProt:P17865 Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity) file:BACSU/ftsZ/ftsZ-deep-research-falcon.md FtsZ monomers bind GTP and assemble into polar protofilaments
GO:0051301 cell division	IEA GO_REF:0000120	ACCEPT	Summary: Duplicate annotation for cell division from combined automated methods. Reason: This IEA annotation for cell division duplicates the IBA annotation. Both are correct and well-supported by the essential role of FtsZ in bacterial cell division. Supporting Evidence: UniProt:P17865 Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site
GO:0090529 cell septum assembly	IEA GO_REF:0000104	ACCEPT	Summary: FtsZ is essential for cell septum assembly as the Z-ring initiates and scaffolds the septation process. This is a specific biological process term. Reason: Cell septum assembly is an appropriate biological process annotation for FtsZ. The Z-ring formed by FtsZ recruits the divisome machinery that carries out septum formation. UniProt states the Z-ring functions to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Supporting Evidence: UniProt:P17865 One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells
GO:0005515 protein binding	IPI PMID:16796675 A new FtsZ-interacting protein, YlmF, complements the activi...	MODIFY	Summary: This annotation reflects FtsZ interaction with YlmF (SepF) identified by cross-linking and yeast two-hybrid. However, "protein binding" is too general for this well-characterized interaction. Reason: While the interaction is valid, "protein binding" is uninformative. FtsZ interacts with YlmF/SepF, which functions as a membrane anchor and filament bundler for FtsZ. The abstract states YlmF has an overlapping function with FtsA in stimulating the formation of Z rings. A more specific term reflecting FtsZ-anchor interaction would be appropriate, but since GO lacks such a term, the annotation could be retained as evidence of FtsZ's interaction network. Proposed replacements: identical protein binding Supporting Evidence: PMID:16796675 Analysis of the results identified YlmF as a new component of the FtsZ complex
GO:0005515 protein binding	IPI PMID:17662947 A metabolic sensor governing cell size in bacteria.	MODIFY	Summary: This annotation reflects FtsZ interaction with UgtP, a metabolic sensor that inhibits FtsZ assembly. The term "protein binding" is too general. Reason: The interaction with UgtP is well-documented as a regulatory mechanism linking nutrient availability to cell division. The abstract states UgtP localizes to the division site in a nutrient-dependent manner and inhibits assembly of the tubulin-like cell division protein FtsZ. However, "protein binding" is too vague for this important regulatory interaction. UniProt documents the interaction. Proposed replacements: identical protein binding Supporting Evidence: PMID:17662947 UgtP, which localizes to the division site in a nutrient-dependent manner and inhibits assembly of the tubulin-like cell division protein FtsZ
GO:0005515 protein binding	IPI PMID:21224850 Large ring polymers align FtsZ polymers for normal septum fo...	MODIFY	Summary: This annotation reflects FtsZ interaction with SepF, which forms large ring polymers that bundle and align FtsZ filaments. "Protein binding" is too general. Reason: The interaction between FtsZ and SepF is well-characterized. The publication shows SepF is able to bundle FtsZ protofilaments into strikingly long and regular tubular structures. While the interaction is real, "protein binding" fails to capture the functional significance. Proposed replacements: identical protein binding Supporting Evidence: PMID:21224850 able to bundle FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules
GO:0005515 protein binding	IPI PMID:21630458 An expanded protein-protein interaction network in Bacillus ...	MARK AS OVER ANNOTATED	Summary: This annotation comes from a large-scale yeast two-hybrid study in B. subtilis. "Protein binding" is too general for functional annotation. Reason: This annotation derives from a high-throughput protein-protein interaction network study that identified FtsZ interactions among many others. While interactions are real, "protein binding" from high-throughput studies adds little functional information. Supporting Evidence: PMID:21630458 We have generated a protein-protein interaction network in Bacillus subtilis focused on several essential cellular processes such as cell division, cell responses to various stresses, the bacterial cytoskeleton, DNA replication and chromosome maintenance by careful application of the yeast two-hybrid approach
GO:0042802 identical protein binding	IPI PMID:16796675 A new FtsZ-interacting protein, YlmF, complements the activi...	ACCEPT	Summary: FtsZ forms homodimers and homopolymers. This annotation likely reflects FtsZ self-interaction detected in the cross-linking/mass spec study of FtsZ complexes. Reason: FtsZ self-polymerization is essential for Z-ring formation. UniProt states FtsZ is a homodimer that polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner. The IntAct database records FtsZ-FtsZ interactions with 6 experiments. Supporting Evidence: UniProt:P17865 Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity)
GO:0042802 identical protein binding	IPI PMID:17662947 A metabolic sensor governing cell size in bacteria.	ACCEPT	Summary: This annotation may reflect FtsZ self-interaction detected in the context of studying UgtP regulation of FtsZ assembly. Reason: FtsZ homo-oligomerization is well-established and central to its function. The study examining UgtP inhibition of FtsZ assembly would have detected FtsZ self-interactions as part of the polymerization assays. Supporting Evidence: UniProt:P17865 Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity)
GO:0042802 identical protein binding	IPI PMID:21224850 Large ring polymers align FtsZ polymers for normal septum fo...	ACCEPT	Summary: FtsZ self-polymerization is essential for forming the protofilaments that are bundled by SepF. This study directly examined FtsZ polymerization. Reason: The publication explicitly studied FtsZ polymerization and its bundling by SepF. The methods describe FtsZ polymerization and GTPase assays with FtsZ. Self-interaction is a prerequisite for the bundled structures observed. Supporting Evidence: PMID:21224850 B. subtilis FtsZ was purified as described previously (Wang and Lutkenhaus, 1993; Scheffers, 2008)
GO:0042802 identical protein binding	IPI PMID:21630458 An expanded protein-protein interaction network in Bacillus ...	ACCEPT	Summary: FtsZ self-interaction detected in the high-throughput two-hybrid network study. Reason: FtsZ homo-oligomerization is a well-established core function. Detection in the two-hybrid study is consistent with established biochemistry. IntAct records 6 experiments supporting FtsZ-FtsZ interaction. Supporting Evidence: UniProt:P17865 Polymerizes to form a dynamic ring structure in a strictly GTP-dependent manner (By similarity)
GO:0051301 cell division	EXP PMID:22298780 Extreme C terminus of bacterial cytoskeletal protein FtsZ pl...	ACCEPT	Summary: This study examined the role of the FtsZ C-terminal variable region in lateral interactions between protofilaments and Z-ring integrity, directly demonstrating FtsZ's role in cell division. Reason: The publication provides direct experimental evidence for FtsZ's role in cell division in B. subtilis. It states bacterial cell division typically requires assembly of the cytoskeletal protein FtsZ into a ring at the nascent division site and shows that C-terminal mutations cause a low frequency of FtsZ ring formation and a high degree of filamentation. Supporting Evidence: PMID:22298780 Bacterial cell division typically requires assembly of the cytoskeletal protein FtsZ into a ring (Z-ring) at the nascent division site that serves as a foundation for assembly of the division apparatus
GO:0003924 GTPase activity	IDA PMID:23577149 Genetic and biochemical characterization of the MinC-FtsZ in...	ACCEPT	Summary: This study directly assayed FtsZ GTPase activity and critical concentration as part of characterizing MinC-FtsZ interactions. The GTPase activity measurements provide direct experimental evidence. Reason: The publication directly measured GTPase activity of wild-type and mutant FtsZ. The methods describe GTPase Activity and Critical Concentration assays, and results include GTPase activity measurements of FtsZ mutants. This provides direct biochemical evidence (IDA) for the GTPase molecular function. Supporting Evidence: PMID:23577149 GTPase activity and Cc of FtsZ mutants
GO:0051301 cell division	IMP PMID:18573169 A sensor histidine kinase co-ordinates cell wall architectur...	ACCEPT	Summary: This study used FtsZ depletion to examine YycG kinase function, providing mutant phenotype evidence for FtsZ's role in cell division. Reason: The abstract describes using FtsZ-depleted, septum-less cells to study YycG kinase activity, indicating that FtsZ depletion prevents septum formation. This mutant phenotype evidence (IMP) supports the cell division annotation. Supporting Evidence: PMID:18573169 RT-PCR quantification of YycF approximately PO(4)-regulated gene transcription, in wild type and FtsZ-depleted, septum-less cells, indicated that YycG kinase activity on YycF is dependent on YycG localization to a division septum
GO:0030428 cell septum	IDA PMID:18573169 A sensor histidine kinase co-ordinates cell wall architectur...	ACCEPT	Summary: The study examining YycG localization demonstrates that the septum forms at the FtsZ ring location, supporting FtsZ localization at the cell septum. Reason: The publication shows that YycG sensor histidine kinase is a component of the division septum and that its activity depends on localization to the septum where FtsZ forms the Z-ring. The study of septum-less cells in FtsZ-depleted conditions confirms FtsZ's role at the septum. Supporting Evidence: PMID:18573169 YycG sensor histidine kinase is a component of the division septum in growing cells

Gene Description

Existing Annotations Review

Core Functions

FtsZ is a tubulin-like GTPase whose enzymatic activity drives protofilament dynamics through GTP hydrolysis. This is the primary molecular function.

FtsZ homo-oligomerization is essential for protofilament formation and Z-ring assembly. This self-polymerization underlies all downstream functions.

References

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Deep Research

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