Peptidoglycan synthase FtsI

Details

Name
Peptidoglycan synthase FtsI
Synonyms
  • 2.4.1.129
  • PBP-3
  • pbpB
  • Penicillin-binding protein 3
  • Peptidoglycan glycosyltransferase 3
Gene Name
ftsI
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011715|Peptidoglycan synthase FtsI
MKAAAKTQKPKRQEEHANFISWRFALLCGCILLALAFLLGRVAWLQVISPDMLVKEGDMR
SLRVQQVSTSRGMITDRSGRPLAVSVPVKAIWADPKEVHDAGGISVGDRWKALANALNIP
LDQLSARINANPKGRFIYLARQVNPDMADYIKKLKLPGIHLREESRRYYPSGEVTAHLIG
FTNVDSQGIEGVEKSFDKWLTGQPGERIVRKDRYGRVIEDISSTDSQAAHNLALSIDERL
QALVYRELNNAVAFNKAESGSAVLVDVNTGEVLAMANSPSYNPNNLSGTPKEAMRNRTIT
DVFEPGSTVKPMVVMTALQRGVVRENSVLNTIPYRINGHEIKDVARYSELTLTGVLQKSS
NVGVSKLALAMPSSALVDTYSRFGLGKATNLGLVGERSGLYPQKQRWSDIERATFSFGYG
LMVTPLQLARVYATIGSYGIYRPLSITKVDPPVPGERVFPESIVRTVVHMMESVALPGGG
GVKAAIKGYRIAIKTGTAKKVGPDGRYINKYIAYTAGVAPASQPRFALVVVINDPQAGKY
YGGAVSAPVFGAIMGGVLRTMNIEPDALTTGDKNEFVINQGEGTGGRS
Number of residues
588
Molecular Weight
63876.925
Theoretical pI
10.1
GO Classification
Functions
penicillin binding / peptidoglycan glycosyltransferase activity
Processes
cell cycle / cell division / cell wall organization / peptidoglycan biosynthetic process / regulation of cell shape / response to drug
Components
cell division site / integral component of plasma membrane / intrinsic component of plasma membrane
General Function
Peptidoglycan glycosyltransferase activity
Specific Function
Essential cell division protein that is required for the synthesis of peptidoglycan at the division septum (PubMed:1103132, PubMed:9614966). Catalyzes the synthesis of cross-linked peptidoglycan from the lipid-linked precursors (PubMed:7030331). Required for localization of FtsN (PubMed:9282742).
Pfam Domain Function
Transmembrane Regions
19-39
Cellular Location
Cell inner membrane
Gene sequence
>lcl|BSEQ0011716|Peptidoglycan synthase FtsI (ftsI)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AD68
UniProtKB Entry NameFTSI_ECOLI
GenBank Gene IDK00137
General References
  1. Nakamura M, Maruyama IN, Soma M, Kato J, Suzuki H, Horota Y: 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. [Article]
  2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Ueki M, Wachi M, Jung HK, Ishino F, Matsuhashi M: Escherichia coli mraR gene involved in cell growth and division. J Bacteriol. 1992 Dec;174(23):7841-3. [Article]
  6. Guzman LM, Barondess JJ, Beckwith J: FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli. J Bacteriol. 1992 Dec;174(23):7716-28. [Article]
  7. Michaud C, Parquet C, Flouret B, Blanot D, van Heijenoort J: Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli. Biochem J. 1990 Jul 1;269(1):277-8. [Article]
  8. Spratt BG: Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999-3003. [Article]
  9. Ishino F, Matsuhashi M: Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence. Biochem Biophys Res Commun. 1981 Aug 14;101(3):905-11. [Article]
  10. Nicholas RA, Strominger JL, Suzuki H, Hirota Y: Identification of the active site in penicillin-binding protein 3 of Escherichia coli. J Bacteriol. 1985 Oct;164(1):456-60. [Article]
  11. Houba-Herin N, Hara H, Inouye M, Hirota Y: Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia coli: identification of its active site. Mol Gen Genet. 1985;201(3):499-504. [Article]
  12. Nagasawa H, Sakagami Y, Suzuki A, Suzuki H, Hara H, Hirota Y: Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli. J Bacteriol. 1989 Nov;171(11):5890-3. [Article]
  13. Taschner PE, Ypenburg N, Spratt BG, Woldringh CL: An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli. J Bacteriol. 1988 Oct;170(10):4828-37. [Article]
  14. Bowler LD, Spratt BG: Membrane topology of penicillin-binding protein 3 of Escherichia coli. Mol Microbiol. 1989 Sep;3(9):1277-86. [Article]
  15. Addinall SG, Cao C, Lutkenhaus J: FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol. 1997 Jul;25(2):303-9. [Article]
  16. Weiss DS, Pogliano K, Carson M, Guzman LM, Fraipont C, Nguyen-Disteche M, Losick R, Beckwith J: Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole. Mol Microbiol. 1997 Aug;25(4):671-81. [Article]
  17. Nguyen-Disteche M, Fraipont C, Buddelmeijer N, Nanninga N: The structure and function of Escherichia coli penicillin-binding protein 3. Cell Mol Life Sci. 1998 Apr;54(4):309-16. [Article]
  18. Wang L, Khattar MK, Donachie WD, Lutkenhaus J: FtsI and FtsW are localized to the septum in Escherichia coli. J Bacteriol. 1998 Jun;180(11):2810-6. [Article]
  19. Weiss DS, Chen JC, Ghigo JM, Boyd D, Beckwith J: Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J Bacteriol. 1999 Jan;181(2):508-20. [Article]
  20. Chen JC, Beckwith J: FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol Microbiol. 2001 Oct;42(2):395-413. [Article]
  21. Mercer KL, Weiss DS: The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. J Bacteriol. 2002 Feb;184(4):904-12. [Article]
  22. Wissel MC, Weiss DS: Genetic analysis of the cell division protein FtsI (PBP3): amino acid substitutions that impair septal localization of FtsI and recruitment of FtsN. J Bacteriol. 2004 Jan;186(2):490-502. [Article]
  23. Wissel MC, Wendt JL, Mitchell CJ, Weiss DS: The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring. J Bacteriol. 2005 Jan;187(1):320-8. [Article]
  24. D'Ulisse V, Fagioli M, Ghelardini P, Paolozzi L: Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology. 2007 Jan;153(Pt 1):124-38. [Article]
  25. Fraipont C, Alexeeva S, Wolf B, van der Ploeg R, Schloesser M, den Blaauwen T, Nguyen-Disteche M: The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli. Microbiology. 2011 Jan;157(Pt 1):251-9. doi: 10.1099/mic.0.040071-0. Epub 2010 Sep 16. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04918Ceftobiproleapproved, investigationalunknownDetails
DB00267CefmenoximeapprovedyesinhibitorDetails
DB01416Cefpodoximeapproved, vet_approvedyesinhibitorDetails
DB01329Cefoperazoneapproved, investigationalyesinhibitorDetails
DB01327CefazolinapprovedyesinhibitorDetails
DB01331CefoxitinapprovedyesinhibitorDetails
DB01328Cefonicidapproved, investigationalyesinhibitorDetails
DB01413Cefepimeapproved, investigationalyesinhibitorDetails
DB01415Ceftibutenapproved, investigationalyesinhibitorDetails
DB00430CefpiramideapprovedyesinhibitorDetails
DB00438CeftazidimeapprovedyesinhibitorDetails
DB00274Cefmetazoleapproved, investigationalyesinhibitorDetails
DB00303Ertapenemapproved, investigationalyesinhibitorDetails
DB00578Carbenicillinapproved, investigationalyesinhibitorDetails
DB09319Carindacillinapproved, investigationalyesinhibitorDetails
DB09050Ceftolozaneapproved, investigationalunknownDetails
DB01602Bacampicillinapproved, investigationalyesinhibitorDetails
DB01000CyclacillinapprovedyesinhibitorDetails