Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. (Q34675381)

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English	Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN.	scientific article

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17 November 2019

Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN (English)

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17 November 2019

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17 November 2019

author name string

Mark C Wissel

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1 January 2004

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17 November 2019

Journal of Bacteriology

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17 November 2019

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17 November 2019

490-502

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17 November 2019

2

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17 November 2019

Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams

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The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway

1 reference

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Cytokinesis in bacteria

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The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site.

1 reference

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Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins

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Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations

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Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL

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Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs

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Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole.

1 reference

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The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate

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A promoter for the first nine genes of the Escherichia coli mra cluster of cell division and cell envelope biosynthesis genes, including ftsI and ftsW.

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The complete genome sequence of Escherichia coli K-12

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7 July 2018

Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli

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Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites

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The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the f

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A hypothetical holoenzyme involved in the replication of the murein sacculus of Escherichia coli

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Topological characterization of the essential Escherichia coli cell division protein FtsN.

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7 July 2018

X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme

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Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

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Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation

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7 July 2018

Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12.

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Determinants of membrane protein topology

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Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli

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Genetic analyses of processing involving C-terminal cleavage in penicillin-binding protein 3 of Escherichia coli

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Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12

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The structure and function of Escherichia coli penicillin-binding protein 3.

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Membrane topology of penicillin-binding protein 3 of Escherichia coli.

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A set of temperature sensitive-replication/-segregation and temperature resistant plasmid vectors with different copy numbers and in an isogenic background (chloramphenicol, kanamycin, lacZ, repA, par, polA)

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Differential functionalities of amphiphilic peptide segments of the cell-septation penicillin-binding protein 3 of Escherichia coli

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12 December 2020

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Morphogenesis of Escherichia coli

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Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis

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Identifiers

10.1128/JB.186.2.490-502.2004

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17 November 2019

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17 November 2019

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17 November 2019

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