Gene Ontology annotation through association of InterPro records with GO terms
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
Combined Automated Annotation using Multiple IEA Methods
Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.
Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis.
Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins.
The essential cell division protein FtsN interacts with the murein (peptidoglycan) synthase PBP1B in Escherichia coli.
The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN.
Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery.
Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli.
Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET.
The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli.
The β-lactam resistance protein Blr, a small membrane polypeptide, is a component of the Escherichia coli cell division machinery.
The binary protein-protein interaction landscape of Escherichia coli.
SEDS proteins are a widespread family of bacterial cell wall polymerases.
Interplay between Penicillin-binding proteins and SEDS proteins promotes bacterial cell wall synthesis.
Assembly and activation of the Escherichia coli divisome.
ZapG (YhcB/DUF1043), a novel cell division protein in gamma-proteobacteria linking the Z-ring to septal peptidoglycan synthesis.
Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation.
Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence.
FtsI and FtsW are localized to the septum in Escherichia coli.
Membrane topology of penicillin-binding protein 3 of Escherichia coli.
FtsN, a late recruit to the septum in Escherichia coli.
The structure and function of Escherichia coli penicillin-binding protein 3.
Activity of penicillin-binding protein 3 from Escherichia coli.
Deep research on ftsI function