On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3

Mol Gen Genet. 1983;191(1):1-9. doi: 10.1007/BF00330881.


We determined the nucleotide sequence of a DNA fragment containing the ftsI gene coding for the penicillin-binding protein 3 (PBP-3), an indispensable enzyme for cell division of Escherichia coli. The entire ftsI gene was within the 2.8 kilobase PvuII fragment derived from the chromosomal segment on pLC26-6 (Nishimura et al. 1977). The coding region for PBP-3 was identified by comparison with the N-terminal amino acid sequence of in vitro synthesized PBP-3. The structural gene for ftsI consisted of 1,764 base-pairs coding for a 588 amino acid residue-polypeptide with a molecular weight of 63,850. PBP-3 synthesized in vitro showed a lower mobility in SDS-gel electrophoresis than that of the authentic PBP-3, suggesting that the primary translation product of the ftsI gene may be processed to yield mature PBP-3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Base Sequence
  • Carrier Proteins / genetics*
  • Cell Division*
  • DNA, Bacterial / analysis
  • Escherichia coli / genetics*
  • Escherichia coli Proteins*
  • Genes*
  • Genes, Bacterial
  • Hexosyltransferases*
  • Molecular Weight
  • Muramoylpentapeptide Carboxypeptidase*
  • Penicillin-Binding Proteins
  • Peptidoglycan Glycosyltransferase*
  • Peptidyl Transferases*


  • Bacterial Proteins
  • Carrier Proteins
  • DNA, Bacterial
  • Escherichia coli Proteins
  • FtsI protein, E coli
  • Penicillin-Binding Proteins
  • Peptidyl Transferases
  • Hexosyltransferases
  • Peptidoglycan Glycosyltransferase
  • Muramoylpentapeptide Carboxypeptidase

Associated data

  • GENBANK/K00137