Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
-
YlmF (SepF) identified as FtsZ-interacting protein
"Analysis of the results identified YlmF as a new component of the FtsZ complex"
-
YlmF has overlapping function with FtsA in Z-ring formation
"YlmF has an overlapping function with FtsA in stimulating the formation of Z rings in B. subtilis"
A metabolic sensor governing cell size in bacteria.
-
UgtP identified as metabolic sensor that inhibits FtsZ assembly
"UgtP, which localizes to the division site in a nutrient-dependent manner and inhibits assembly of the tubulin-like cell division protein FtsZ"
-
Links nutrient availability to cell division control
"Nutrient availability is one of the strongest determinants of cell size"
A sensor histidine kinase co-ordinates cell wall architecture with cell division in Bacillus subtilis.
-
YycG kinase localizes to division septum
"YycG sensor histidine kinase is a component of the division septum in growing cells"
-
FtsZ depletion produces septum-less cells
"wild type and FtsZ-depleted, septum-less cells"
Large ring polymers align FtsZ polymers for normal septum formation.
-
SepF forms large ring polymers that bundle FtsZ protofilaments
"able to bundle FtsZ protofilaments into strikingly long and regular tubular structures reminiscent of eukaryotic microtubules"
-
SepF rings required for regular arrangement of FtsZ filaments
"We propose that SepF rings are required for the regular arrangement of FtsZ filaments"
An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach.
-
High-throughput protein-protein interaction network in B. subtilis
"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"
-
FtsZ identified as hub protein in cell division pathway
"A striking feature of the network is a group of highly connected hubs (GoH) linking many different cellular processes"
Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.
-
C-terminal variable region mediates lateral interactions between FtsZ polymers
"residues at the C terminus of Bacillus subtilis FtsZ (C-terminal variable region (CTV)) are both necessary and sufficient for stimulating lateral interactions in vitro in the absence of modulatory proteins"
-
CTV mutations cause filamentation and reduced Z-ring formation
"B. subtilis cells expressing the B. subtilis FtsZ chimera had a low frequency of FtsZ ring formation and a high degree of filamentation relative to wild-type cells"
Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
-
MinC inhibits FtsZ polymerization
"The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in the spatial control of Z ring formation"
-
Identified MinC binding site on FtsZ
"determine the binding site for MinC on B. subtilis FtsZ"
-
GTPase activity measured for FtsZ mutants
"GTPase activity and Cc of FtsZ mutants"
UniProt entry for B. subtilis FtsZ
-
Essential cell division protein forming Z-ring
"Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site"
-
GTP binding and GTPase activity
"Binds GTP and shows GTPase activity"
-
Interacts with FtsA, SepF, EzrA, ZapA, UgtP
"Interacts directly with several other division proteins (By similarity). Interacts with FtsA"
-
Regulated by MciZ during sporulation
"During sporulation, is negatively regulated by MciZ, which binds to FtsZ and inhibits its polymerization and the formation of the Z ring"
-
Crystal structure solved to 1.7 angstroms
"PDB; 2VXY; X-ray; 1.70 A; A=1-382"
Deep research review of FtsZ in B. subtilis
-
FtsZ is a conserved tubulin-like GTPase essential for bacterial cell division
"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"
-
GTP binding and hydrolysis control filament dynamics
"GTP binding and hydrolysis control filament assembly dynamics, subunit turnover, and ring remodeling"
-
Multiple membrane tethers anchor the Z-ring
"FtsZ lacks an intrinsic membrane anchor and is tethered via membrane-associated partners, notably FtsA and SepF, with EzrA also acting as a multifunctional tether/regulator in B. subtilis"