Characterisation of mutant alleles of the cell division protein FtsA, a regulator and structural component of the Escherichia coli septator.
Two alleles of ftsA, a gene that encodes an essential cell division protein in Escherichia coli, have-been mapped at the nucleotide level. The mutations are located inside domains that are conserved in an ATP-binding protein family. The ftsA2 mutation lies in the adenine-binding domain, and the ftsA3 in the ribose-binding domain. The defect in ampicillin binding to PBP3 described for allele ftsA3 is allele-specific. This supports the hypothesis of the existence of different domains in FtsA having different functions.
Sánchez
M
M
Departamento de Biología Celular y del Desarrollo, CIB, CSIC, Madrid, Spain.
Dopazo
A
A
Pla
J
J
Robinson
A C
AC
Vicente
M
M
D000483:Alleles; D000667:Ampicillin / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics*; D002451:Cell Compartmentation / Q000235:genetics; D002455:Cell Division / Q000502:physiology; D002874:Chromosome Mapping; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D005809:Genes, Regulator; D009154:Mutation; D011869:Radioligand Assay
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C065103:FtsA protein, Bacteria; C489310:FtsA protein, E coli; D000667:Ampicillin