Identification
Name:Peptidoglycan synthase ftsI
Synonyms:
  • Penicillin-binding protein 3
  • PBP-3
  • Peptidoglycan glycosyltransferase 3
Gene Name:ftsI
Enzyme Class:
Biological Properties
General Function:Involved in penicillin binding
Specific Function:Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates
Cellular Location:Cell inner membrane; Single-pass membrane protein; Periplasmic side.
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol1.0di-trans,poly-cis-Undecaprenyl diphosphate+1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol
1.0Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + 1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol ↔ 1.0di-trans,poly-cis-Undecaprenyl diphosphate + 1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-A2pm-D-Ala-D-Ala)]n-diphosphoundecaprenol
ReactionCard
1.0[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-g-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol+1.0Thumb1.0Thumb
SMPDB Reactions:
1.0 a peptidoglycan dimer (meso-diaminopimelate containing)1.0Thumb+1.0a peptidoglycan with D,D cross-links (meso-diaminopimelate containing)
1.0 a peptidoglycan dimer (meso-diaminopimelate containing) → 1.0D-Alanine + 1.0a peptidoglycan with D,D cross-links (meso-diaminopimelate containing)
ReactionCard
EcoCyc Reactions:
1.0a peptidoglycan dimer (meso-diaminopimelate containing)+1.0Thumb1.0a peptidoglycan with D,D cross-links (meso-diaminopimelate containing)+1.0Thumb+1.0Thumb
1.0a peptidoglycan dimer (meso-diaminopimelate containing) + 1.0Water → 1.0a peptidoglycan with D,D cross-links (meso-diaminopimelate containing) + 1.0Undecaprenyl diphosphate + 1.0D-Alanine
ReactionCard
1.0peptidoglycan D-alanyl-DAP crosslink+1.0Thumb1.0peptidoglycan tetrapeptide, glycan chain 2+1.0peptidoglycan tetrapeptide, glycan chain 1
1.0peptidoglycan D-alanyl-DAP crosslink + 1.0Water ↔ 1.0peptidoglycan tetrapeptide, glycan chain 2 + 1.0peptidoglycan tetrapeptide, glycan chain 1
ReactionCard
Complex Reactions:
1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)1.0Thumb+1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain)
1.0two linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 1.0D-Alanine + 1.0two disacharide linked murein units, pentapeptide crosslinked tetrapeptide (A2pm->D-ala) (middle of chain)
ReactionCard
1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain)2.0Thumb+1.0three disacharide linked murein units (pentapeptide crosslinked tetrapeptide (A2pm->D-ala) tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain)
1.0three linked disacharide pentapeptide murein units (uncrosslinked, middle of chain) → 2.0D-Alanine + 1.0three disacharide linked murein units (pentapeptide crosslinked tetrapeptide (A2pm->D-ala) tetrapeptide corsslinked tetrapeptide (A2pm->D-ala)) (middle of chain)
ReactionCard
1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol+1.0Thumb1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol+1.0Thumb
1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + 1.0GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol → 1.0(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + 1.0Undecaprenyl diphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01310D-AlanineMetaboCard
ECMDB23024GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenolMetaboCard
ECMDB01469Undecaprenyl diphosphateMetaboCard
ECMDB20212Undecaprenyl-diphospho-N-acetylmuramoyl-(N-acetylglucosamine)-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanineMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
drug binding
penicillin binding
Process
cell wall biogenesis
cell wall organization or biogenesis
cellular cell wall organization or biogenesis
cellular component organization or biogenesis
peptidoglycan-based cell wall biogenesis
Gene Properties
Blattner:b0084
Gene OrientationClockwise
Centisome Percentage:1.97
Left Sequence End91413
Right Sequence End93179
Gene Sequence:
>1767 bp
ATGAAAGCAGCGGCGAAAACGCAGAAACCAAAACGTCAGGAAGAACATGCCAACTTTATC
AGTTGGCGTTTTGCGTTGTTATGCGGCTGTATTCTCCTGGCGCTGGCTTTTCTGCTCGGA
CGCGTAGCGTGGTTACAAGTTATCTCCCCGGATATGCTGGTGAAAGAGGGCGACATGCGT
TCTCTTCGCGTTCAGCAAGTTTCCACCTCCCGCGGCATGATTACTGACCGTTCTGGTCGC
CCGTTAGCGGTGAGCGTGCCGGTAAAAGCGATTTGGGCTGACCCGAAAGAAGTGCATGAC
GCTGGCGGTATCAGCGTCGGTGACCGCTGGAAGGCGCTGGCTAACGCGCTCAATATTCCG
CTGGATCAGCTTTCAGCCCGCATTAACGCCAACCCGAAAGGGCGCTTTATTTATCTGGCG
CGTCAGGTGAACCCTGACATGGCGGACTACATCAAAAAACTGAAACTGCCGGGGATTCAT
CTGCGTGAAGAGTCTCGCCGTTACTATCCGTCCGGCGAAGTGACTGCTCACCTCATCGGC
TTTACTAACGTCGATAGTCAAGGGATTGAGGGCGTTGAGAAGAGTTTCGATAAATGGCTT
ACCGGGCAGCCGGGTGAGCGCATTGTGCGTAAAGACCGCTATGGTCGCGTAATTGAAGAT
ATTTCTTCTACTGACAGCCAGGCAGCGCACAACCTGGCGCTGAGTATTGATGAACGCCTG
CAGGCGCTGGTTTATCGCGAACTGAACAACGCGGTGGCCTTTAACAAGGCTGAATCTGGT
AGCGCCGTGCTGGTGGATGTCAACACCGGTGAAGTGCTGGCGATGGCTAACAGCCCGTCA
TACAACCCTAACAATCTGAGCGGCACGCCGAAAGAGGCGATGCGTAACCGTACCATCACC
GACGTGTTTGAACCGGGCTCAACGGTTAAACCGATGGTGGTAATGACCGCGTTGCAACGT
GGCGTGGTGCGGGAAAACTCGGTACTCAATACCATTCCTTATCGAATTAACGGCCACGAA
ATCAAAGACGTGGCACGCTACAGCGAATTAACCCTGACCGGGGTATTACAGAAGTCGAGT
AACGTCGGTGTTTCCAAGCTGGCGTTAGCGATGCCGTCCTCAGCGTTAGTAGATACTTAC
TCACGTTTTGGACTGGGAAAAGCGACCAATTTGGGGTTGGTCGGAGAACGCAGTGGCTTA
TATCCTCAAAAACAACGGTGGTCTGACATAGAGAGGGCCACCTTCTCTTTCGGCTACGGG
CTAATGGTAACACCATTACAGTTAGCGCGAGTCTACGCAACTATCGGCAGCTACGGCATT
TATCGCCCACTGTCGATTACCAAAGTTGACCCCCCGGTTCCCGGTGAACGTGTCTTCCCG
GAATCCATTGTCCGCACTGTGGTGCATATGATGGAAAGCGTGGCGCTACCAGGCGGCGGC
GGCGTGAAGGCGGCGATTAAAGGCTATCGTATCGCCATTAAAACCGGTACCGCGAAAAAG
GTCGGGCCGGACGGTCGCTACATCAATAAATATATTGCTTATACCGCAGGCGTTGCGCCT
GCGAGTCAGCCGCGCTTCGCGCTGGTTGTTGTTATCAACGATCCGCAGGCGGGTAAATAC
TACGGCGGCGCCGTTTCCGCGCCGGTCTTTGGTGCCATCATGGGCGGCGTATTGCGTACC
ATGAACATCGAGCCGGATGCGCTGACAACGGGCGATAAAAATGAATTTGTGATTAATCAA
GGCGAGGGGACAGGTGGCAGATCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:588
Protein Molecular Weight:63877
Protein Theoretical pI:10
Signaling Regions:
  • None
Transmembrane Regions:
  • 19-39
Protein Sequence:
>Peptidoglycan synthase ftsI
MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMR
SLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIP
LDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIG
FTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERL
QALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTIT
DVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSS
NVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYG
LMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGG
GVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKY
YGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS
References
External Links:
ResourceLink
Uniprot ID:P0AD68
Uniprot Name:FTSI_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321965
Ecogene ID:EG10341
Ecocyc:EG10341
ColiBase:b0084
Kegg Gene:b0084
EchoBASE ID:EB0337
CCDB:FTSI_ECOLI
BacMap:16128077
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bowler, L. D., Spratt, B. G. (1989). "Membrane topology of penicillin-binding protein 3 of Escherichia coli." Mol Microbiol 3:1277-1286. Pubmed: 2677607
  • Guzman, L. M., Barondess, J. J., Beckwith, J. (1992). "FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli." J Bacteriol 174:7716-7728. Pubmed: 1332942
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Houba-Herin, N., Hara, H., Inouye, M., Hirota, Y. (1985). "Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia coli: identification of its active site." Mol Gen Genet 201:499-504. Pubmed: 3911028
  • Michaud, C., Parquet, C., Flouret, B., Blanot, D., van Heijenoort, J. (1990). "Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli." Biochem J 269:277-278. Pubmed: 2198024
  • Nagasawa, H., Sakagami, Y., Suzuki, A., Suzuki, H., Hara, H., Hirota, Y. (1989). "Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli." J Bacteriol 171:5890-5893. Pubmed: 2681146
  • Nakamura, M., Maruyama, I. N., Soma, M., Kato, J., Suzuki, H., Horota, Y. (1983). "On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3." Mol Gen Genet 191:1-9. Pubmed: 6350821
  • Taschner, P. E., Ypenburg, N., Spratt, B. G., Woldringh, C. L. (1988). "An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli." J Bacteriol 170:4828-4837. Pubmed: 3049550
  • Ueki, M., Wachi, M., Jung, H. K., Ishino, F., Matsuhashi, M. (1992). "Escherichia coli mraR gene involved in cell growth and division." J Bacteriol 174:7841-7843. Pubmed: 1447153
  • Yura, T., Mori, H., Nagai, H., Nagata, T., Ishihama, A., Fujita, N., Isono, K., Mizobuchi, K., Nakata, A. (1992). "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Nucleic Acids Res 20:3305-3308. Pubmed: 1630901