Peptidoglycan D,D-transpeptidase FtsI
Also known as: JW0082, b0084, ftsI, pbpB
Function
Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum. Required for localization of FtsN.
Classification
- Family (Pfam)
- PF03717 PBP_dimer, PF00905 Transpeptidase
- InterPro
- Beta-lactam/transpept, Beta-lactam/transpept-like, FtsI_transpept, PBP_dimer, PBP_dimer_sf, PCN-bd_Tpept
- Functional cluster
- Oxidoreductases, Catalases & Peroxidases
Experimental structures · PDB · 6
A predicted model is available from AlphaFold.
Gene Ontology · 13
- GO:0032153 cell division site
- GO:0005886 plasma membrane
- GO:0008658 penicillin binding
- GO:0008955 peptidoglycan glycosyltransferase activity
- GO:0009002 serine-type D-Ala-D-Ala carboxypeptidase activity
- GO:0051301 cell division
- GO:0071555 cell wall organization
- GO:0000917 division septum assembly
- GO:0043093 FtsZ-dependent cytokinesis
- GO:0009252 peptidoglycan biosynthetic process
- GO:0006508 proteolysis
- GO:0008360 regulation of cell shape
- GO:0009410 response to xenobiotic stimulus
Drugs targeting this protein · 85
- CEFOTAXIME SODIUM inhibitor
- AMOXICILLIN inhibitor
- CEFUROXIME AXETIL inhibitor
- PENICILLIN G SODIUM inhibitor
- CEFAMANDOLE inhibitor
- CYCLACILLIN inhibitor
- MOXALACTAM DISODIUM inhibitor
- CEPHALEXIN HYDROCHLORIDE inhibitor
- CEFOPERAZONE SODIUM inhibitor
- CEFAZOLIN SODIUM inhibitor
- CEFOXITIN SODIUM inhibitor
- CEPHALEXIN inhibitor
- LORACARBEF inhibitor
- CEFPIRAMIDE SODIUM inhibitor
- AMPICILLIN SODIUM inhibitor
- CEFTAZIDIME SODIUM inhibitor
- PIPERACILLIN SODIUM inhibitor
- PENICILLIN V POTASSIUM inhibitor
- TICARCILLIN DISODIUM inhibitor
- CEFEPIME HYDROCHLORIDE inhibitor
- BACAMPICILLIN HYDROCHLORIDE inhibitor
- CEPHALOGLYCIN inhibitor
- CEFTIBUTEN DIHYDRATE inhibitor
- CARBENICILLIN INDANYL SODIUM inhibitor
- CEFONICID SODIUM inhibitor
- CEFPODOXIME PROXETIL inhibitor
- CEFACLOR inhibitor
- CEFTIZOXIME SODIUM inhibitor
- CEPHAPIRIN SODIUM inhibitor
- CEFORANIDE inhibitor
- CEFOTETAN DISODIUM inhibitor
- CEFMETAZOLE SODIUM inhibitor
- CEFTOLOZANE SULFATE inhibitor
- PENICILLIN G POTASSIUM inhibitor
- ERTAPENEM SODIUM inhibitor
- RAZUPENEM inhibitor
- FAROPENEM MEDOXOMIL inhibitor
- MEROPENEM inhibitor
- TEMOCILLIN inhibitor
- ERTAPENEM inhibitor
- CEFIXIME inhibitor
- FLOMOXEF inhibitor
- AZTREONAM inhibitor
- CEPHRADINE inhibitor
- CEFTIBUTEN inhibitor
- PHENETHICILLIN inhibitor
- CEFAMANDOLE NAFATE inhibitor
- TALAMPICILLIN inhibitor
- CEPHALOTHIN SODIUM inhibitor
- CEFADROXIL inhibitor
- CEFPODOXIME inhibitor
- MEZLOCILLIN SODIUM inhibitor
- AMPICILLIN inhibitor
- SULOPENEM inhibitor
- PENAMECILLIN inhibitor
- TEBIPENEM PIVOXIL inhibitor
- CEFUROXIME SODIUM inhibitor
- FLOXACILLIN inhibitor
- CEFTIOFUR inhibitor
- CEFODIZIME inhibitor
- PIVAMPICILLIN inhibitor
- CEFMENOXIME HYDROCHLORIDE inhibitor
- CEFSULODIN inhibitor
- CEFTAROLINE FOSAMIL ACETATE inhibitor
- AZTREONAM LYSINE inhibitor
- PENICILLIN G BENZATHINE inhibitor
- CEFIDEROCOL inhibitor
- CEFIDEROCOL SULFATE TOSYLATE inhibitor
- CEFILAVANCIN inhibitor
- CEFOTIAM HYDROCHLORIDE inhibitor
- DORIPENEM MONOHYDRATE inhibitor
- IMIPENEM inhibitor
- CEFTAZIDIME inhibitor
- CEFDITOREN PIVOXIL inhibitor
- SULOPENEM ETZADROXIL inhibitor
- DORIPENEM inhibitor
- CEFTAROLINE FOSAMIL inhibitor
- CEFTOBIPROLE inhibitor
- CEFPROZIL, (E)- inhibitor
- FAROPENEM inhibitor
- CARBENICILLIN DISODIUM inhibitor
- CEFTRIAXONE SODIUM inhibitor
- PENICILLIN V inhibitor
- CEFPIROME inhibitor
- CEFDINIR inhibitor
Related proteins · sequence + function similarity
- Peptidoglycan D,D-transpeptidase FtsI 0.89
- Probable peptidoglycan D,D-transpeptidase PenA 0.85
- Probable peptidoglycan D,D-transpeptidase PenA 0.85
- Probable peptidoglycan D,D-transpeptidase PenA 0.85
- Peptidoglycan D,D-transpeptidase FtsI 0.85
- Probable peptidoglycan D,D-transpeptidase PbpC 0.85
- Penicillin-binding protein 1B 0.81
- Peptidoglycan D,D-transpeptidase MrdA 0.81
- Peptidoglycan D,D-transpeptidase MrdA 0.81
- Peptidoglycan D,D-transpeptidase MrdA 0.81
- Probable peptidoglycan D,D-transpeptidase PenA 0.81
- Penicillin-binding protein 1A 0.77
Co-cited proteins · studied together in the literature
- Probable peptidoglycan glycosyltransferase FtsW 4 shared papers
- Cell division protein FtsL 4 shared papers
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase 1 shared papers
- Peptidoglycan D,D-transpeptidase MrdA 1 shared papers
- Cell division protein FtsN 3 shared papers
- Ribosomal RNA small subunit methyltransferase H 1 shared papers
- Cell division protein FtsA 2 shared papers
- DNA translocase FtsK 2 shared papers
- Cell division protein FtsQ 2 shared papers
Literature · 27 cited papers
- The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli. Microbiology · 2011
- Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins. Microbiology · 2007
- Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol. Syst. Biol. · 2006
- The transmembrane helix of the Escherichia coli division protein FtsI localizes to the septal ring. J. Bacteriol. · 2005
- 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
- The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site. J. Bacteriol. · 2002
- FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol. Microbiol. · 2001
- Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL. J. Bacteriol. · 1999
- The structure and function of Escherichia coli penicillin-binding protein 3. Cell. Mol. Life Sci. · 1998
- FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. · 1998
- Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole. Mol. Microbiol. · 1997
- FtsN, a late recruit to the septum in Escherichia coli. Mol. Microbiol. · 1997
- … and 15 more in the literature graph
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