The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

ftsI  -  hypothetical protein

Escherichia coli O157:H7 str. Sakai

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ftsI


High impact information on ftsI


Chemical compound and disease context of ftsI

  • However, all fusions that contained greater than or equal to 36 residues of PBP3 provided single cells of E. coli with substantial levels of resistance to ampicillin, indicating that the beta-lactamase moieties of these fusion proteins were translocated to the periplasm [9].
  • The results indicate that, similar to their counterparts in Escherichia coli, PBP2 and PBP3 are the lethal targets of amdinocillin and furazlocillin, respectively [10].
  • Induction of lysis of two E. coli mutants containing either a thermosensitive penicillin-binding protein (PBP) 2 or 3 by relatively PBP 3-specific (aztreonam) and PBP 2-specific (amdinocillin) antibiotics indicated that inhibition of only PBPs 2 and 3 can cause lysis [11].
  • In the piperacillin and azlocillin series, there was good binding to PBP 3 of E. coli (0.1 microgram/ml) and PBPs 1, 2, and 3 of S. aureus (approximately 1 microgram/ml) [12].
  • The affinity of DQ-2556 to PBP 3 of E. coli, which participates in septum formation, as suggested by morphological observation, was two times greater than that of ceftazidime [13].

Biological context of ftsI


Anatomical context of ftsI

  • All penicillin-binding proteins--except penicillin-binding protein 3, which is found almost exclusively in the cytoplasmic membrane and is involved in septum formation--are also found in gradient fractions corresponding to the outer membrane [18].
  • The in vivo activity of PBP3 also depends on the M-1-to-E-56 amino-terminal module which encompasses the cytosol, the membrane, and the periplasm and which functions as a noncleaved pseudo-signal peptide [19].
  • Yme1p, a yeast mitochondrial protein, affects the rate of DNA escape from mitochondria to the nucleus and the Escherichia coli FtsH protein is apparently involved in the post-translational processing of PBP3, a protein necessary for septation during cell division [20].
  • These compounds have maintained their high affinity for the essential PBP 3, typical of the third generation cephalosporins and have acquired an improved ability to cross the outer membranes of Gram-negative bacteria [21].

Associations of ftsI with chemical compounds

  • In addition, FtsZ rings are able to assemble in newborn cells in the presence of cephalexin, suggesting that newborn cells contain a site at which FtsZ can assemble (the nascent division site) and that the transpeptidase activity of FtsI is not required for assembly of FtsZ at these sites [22].
  • By using low concentrations of the beta-lactams cephalexin and piperacillin to specifically inhibit FtsI (PBP3), an enzyme that synthesizes peptidoglycan at the division septum, we show that FtsZ ring constriction requires the transpeptidase activity of FtsI [22].
  • In the presence of furazlocillin or other beta-lactams with a specificity for penicillin-binding protein 3 which normally cause filamentation, bulges were formed prior to rapid bacteriolysis [23].
  • In contrast to subunits of the divisome, PBP2 failed to localize at mid-cell when PBP3 was inhibited by the specific antibiotic aztreonam [24].
  • The coding region for mature TEM beta-lactamase was fused after the signal peptide and aminoterminal portion of the coding region of a weakly expressed periplasmic protein, PBP3*. The resultant plasmid was mutagenized and transformants expressing increased levels of ampicillin resistance were selected [25].

Other interactions of ftsI


Analytical, diagnostic and therapeutic context of ftsI

  • Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites [22].
  • From these plasmid-carrying strains, PBP-1a and -1b were purified by ampicillin-Sepharose affinity chromatography and PBP-3 by cephalexin-Sepharose affinity chromatography [27].
  • We conclude (i) that immunofluorescence microscopy can be used to localize proteins whose abundance is as low as approximately 100 molecules per cell; and (ii) that spatial and temporal regulation of FtsI activity in septum formation is achieved, at least in part, by timed localization of the protein to the division site [28].
  • FtsI has been estimated to be present at about 100 molecules per cell, well below the detection limit of immunoelectron microscopy [28].
  • The direct protein-protein interaction between purified PBP3 and PBP1B was characterized in vitro by surface plasmon resonance [29].


  1. Resistance to beta-lactam antibiotics by re-modelling the active site of an E. coli penicillin-binding protein. Hedge, P.J., Spratt, B.G. Nature (1985) [Pubmed]
  2. Expression of the Escherichia coli cell division gene sep cloned in a lambda Charon phage. Irwin, C.A., Fletcher, G., Sills, C.L., Walker, J.R. Science (1979) [Pubmed]
  3. Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Laible, G., Hakenbeck, R., Sicard, M.A., Joris, B., Ghuysen, J.M. Mol. Microbiol. (1989) [Pubmed]
  4. Differential functionalities of amphiphilic peptide segments of the cell-septation penicillin-binding protein 3 of Escherichia coli. Marrec-Fairley, M., Piette, A., Gallet, X., Brasseur, R., Hara, H., Fraipont, C., Ghuysen, J.M., Nguyen-Distèche, M. Mol. Microbiol. (2000) [Pubmed]
  5. Affinity of cefoperazone for penicillin-binding proteins. Matsubara, N., Minami, S., Matsuhashi, M., Takaoka, M., Mitsuhashi, S. Antimicrob. Agents Chemother. (1980) [Pubmed]
  6. Bacterial cell division. Bramhill, D. Annu. Rev. Cell Dev. Biol. (1997) [Pubmed]
  7. Penicillin-binding protein inactivation by human neutrophil myeloperoxidase. Rakita, R.M., Rosen, H. J. Clin. Invest. (1991) [Pubmed]
  8. Production of thiol-penicillin-binding protein 3 of Escherichia coli using a two primer method of site-directed mutagenesis. Broome-Smith, J.K., Hedge, P.J., Spratt, B.G. EMBO J. (1985) [Pubmed]
  9. Membrane topology of penicillin-binding protein 3 of Escherichia coli. Bowler, L.D., Spratt, B.G. Mol. Microbiol. (1989) [Pubmed]
  10. Interactions of Yersinia pestis penicillin-binding proteins with beta-lactam antibiotics. Ferreira, R.C., Park, J.T., Camelo, D., De Almeida, D.F., Ferreira, L.C. Antimicrob. Agents Chemother. (1995) [Pubmed]
  11. Involvement of penicillin-binding protein 2 with other penicillin-binding proteins in lysis of Escherichia coli by some beta-lactam antibiotics alone and in synergistic lytic effect of amdinocillin (mecillinam). Gutmann, L., Vincent, S., Billot-Klein, D., Acar, J.F., Mrèna, E., Williamson, R. Antimicrob. Agents Chemother. (1986) [Pubmed]
  12. Binding of monobactams to penicillin-binding proteins of Escherichia coli and Staphylococcus aureus: relation to antibacterial activity. Georgopapadakou, N.H., Smith, S.A., Cimarusti, C.M., Sykes, R.B. Antimicrob. Agents Chemother. (1983) [Pubmed]
  13. In vitro and in vivo activities of DQ-2556 and its mode of action. Tanaka, M., Otsuki, M., Nishino, T. Antimicrob. Agents Chemother. (1992) [Pubmed]
  14. Cloning and characterization of the Pseudomonas aeruginosa pbpB gene encoding penicillin-binding protein 3. Liao, X., Hancock, R.E. Antimicrob. Agents Chemother. (1995) [Pubmed]
  15. Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities. Stefanova, M.E., Tomberg, J., Olesky, M., Höltje, J.V., Gutheil, W.G., Nicholas, R.A. Biochemistry (2003) [Pubmed]
  16. The structure and function of Escherichia coli penicillin-binding protein 3. Nguyen-Distèche, M., Fraipont, C., Buddelmeijer, N., Nanninga, N. Cell. Mol. Life Sci. (1998) [Pubmed]
  17. Cloning and expression of genes responsible for altered penicillin-binding proteins 3a and 3b in Haemophilus influenzae. Malouin, F., Schryvers, A.B., Bryan, L.E. Antimicrob. Agents Chemother. (1987) [Pubmed]
  18. Location of some proteins involved in peptidoglycan synthesis and cell division in the inner and outer membranes of Escherichia coli. Rodríguez-Tébar, A., Barbas, J.A., Vázquez, D. J. Bacteriol. (1985) [Pubmed]
  19. 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 folded structure. Goffin, C., Fraipont, C., Ayala, J., Terrak, M., Nguyen-Distèche, M., Ghuysen, J.M. J. Bacteriol. (1996) [Pubmed]
  20. Sequence of the AFG3 gene encoding a new member of the FtsH/Yme1/Tma subfamily of the AAA-protein family. Guelin, E., Rep, M., Grivell, L.A. Yeast (1994) [Pubmed]
  21. Comparative affinities for penicillin-binding proteins of multipolar ionic amphoteric cephalosporins in gram-negative bacteria. Fontana, R., Valisena, S., Cornaglia, G. Journal of chemotherapy (Florence, Italy) (1996) [Pubmed]
  22. Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites. Pogliano, J., Pogliano, K., Weiss, D.S., Losick, R., Beckwith, J. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  23. A murein hydrolase is the specific target of bulgecin in Escherichia coli. Templin, M.F., Edwards, D.H., Höltje, J.V. J. Biol. Chem. (1992) [Pubmed]
  24. Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Den Blaauwen, T., Aarsman, M.E., Vischer, N.O., Nanninga, N. Mol. Microbiol. (2003) [Pubmed]
  25. A simple method for maximizing the yields of membrane and exported proteins expressed in Escherichia coli. Broome-Smith, J.K., Bowler, L.D., Spratt, B.G. Mol. Microbiol. (1989) [Pubmed]
  26. Target for bacteriostatic and bactericidal activities of beta-lactam antibiotics against Escherichia coli resides in different penicillin-binding proteins. Satta, G., Cornaglia, G., Mazzariol, A., Golini, G., Valisena, S., Fontana, R. Antimicrob. Agents Chemother. (1995) [Pubmed]
  27. On the process of cellular division in Escherichia coli: isolation and characterization of penicillin-binding proteins 1a, 1b, and 3. Tamura, T., Suzuki, H., Nishimura, Y., Mizoguchi, J., Hirota, Y. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  28. Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole. Weiss, D.S., Pogliano, K., Carson, M., Guzman, L.M., Fraipont, C., Nguyen-Distèche, M., Losick, R., Beckwith, J. Mol. Microbiol. (1997) [Pubmed]
  29. Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli. Bertsche, U., Kast, T., Wolf, B., Fraipont, C., Aarsman, M.E., Kannenberg, K., von Rechenberg, M., Nguyen-Distèche, M., den Blaauwen, T., Höltje, J.V., Vollmer, W. Mol. Microbiol. (2006) [Pubmed]
WikiGenes - Universities