Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
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Provides IBA annotations based on phylogenetic analysis of the MinC family
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IBA annotations for division septum site selection, enzyme inhibitor activity, cytosol localization, cytokinesis division site positioning, and cell pole localization
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
Combined Automated Annotation using Multiple IEA Methods
Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
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Identified MinC binding site on B. subtilis FtsZ maps to H9/H10 helices and C-terminal peptide
"These experiments suggest that the MinC binding site in B. subtilis FtsZ has the same bipartite layout as in E. coli FtsZ, involving residues in the vicinity of helix H10 and in the proteińs CTP."
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Isolated 13 Min-resistant FtsZ mutants through genetic screen
"Selection of a library of FtsZ mutants for survival in the presence of Min overexpression resulted in the isolation of 13 Min-resistant mutants."
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Demonstrated MinC inhibits FtsZ polymer bundling and higher-order structure formation
"Indeed, EM and rheology measurements showed that FtsZ polymers formed in the presence of MinC are less bundled, and have fewer lateral contacts and interconnections [33]."
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Showed biochemically that FtsZ mutants have reduced MinC interaction but normal polymerization
"Biochemical characterization of some of the mutant proteins showed that they exhibited normal polymerization properties but reduced interaction with MinC, as expected for binding site mutations."
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Established that MinC-FtsZ interaction architecture is conserved between E. coli and B. subtilis but mechanism differs
"Thus, our study shows that the overall architecture of the MinC-FtsZ interaction is conserved in E. coli and B. subtilis."
Protein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talk.
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Detected MinD-MinC complex by far Western blotting
"In this assay we detected the expected MinD-MinC complex and confirmed the physical interaction between MinD and PtkA, but not TkmA, in agreement with the two-hybrid."
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Identified MinD as hub protein in tyrosine kinase network
"The BY-kinase PtkA also interacted with SalA and MinD, two MRP-like/MinD-family ATPases that bear structural resemblance with BY-kinases (Mijakovic et al., 2005b)."
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Showed MinD interacts with BY-kinases PtkA and PtkB
"Additionally, MinD was found to interact with PtkB and PtpZ."
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Demonstrated MinD-dependent polar localization of PtkA
"This network highlighted a role of tyrosine phosphorylation in the spatial regulation of the Z-ring during cytokinesis."
Deep research on minC function