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
- Functionspenicillin binding / peptidoglycan glycosyltransferase activityProcessescell cycle / cell division / cell wall organization / peptidoglycan biosynthetic process / regulation of cell shape / response to drugComponentscell 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
Resource Link UniProtKB ID P0AD68 UniProtKB Entry Name FTSI_ECOLI GenBank Gene ID K00137 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- Bowler LD, Spratt BG: Membrane topology of penicillin-binding protein 3 of Escherichia coli. Mol Microbiol. 1989 Sep;3(9):1277-86. [Article]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB04918 Ceftobiprole approved, investigational unknown Details DB00267 Cefmenoxime approved yes inhibitor Details DB01416 Cefpodoxime approved, vet_approved yes inhibitor Details DB01329 Cefoperazone approved, investigational yes inhibitor Details DB01327 Cefazolin approved yes inhibitor Details DB01331 Cefoxitin approved yes inhibitor Details DB01328 Cefonicid approved, investigational yes inhibitor Details DB01413 Cefepime approved, investigational yes inhibitor Details DB01415 Ceftibuten approved, investigational yes inhibitor Details DB00430 Cefpiramide approved yes inhibitor Details DB00438 Ceftazidime approved yes inhibitor Details DB00274 Cefmetazole approved, investigational yes inhibitor Details DB00303 Ertapenem approved, investigational yes inhibitor Details DB00578 Carbenicillin approved, investigational yes inhibitor Details DB09319 Carindacillin approved, investigational yes inhibitor Details DB09050 Ceftolozane approved, investigational unknown Details DB01602 Bacampicillin approved, investigational yes inhibitor Details DB01000 Cyclacillin approved yes inhibitor Details DB00671 Cefixime approved, investigational yes binder Details