Penicillin-binding protein 1B
Also known as: JW0145, b0149, mrcB, pbpF, ponB
Function
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Classification
- Family (Pfam)
- PF14812 PBP1_TM, PF00912 Transgly, PF00905 Transpeptidase, PF14814 UB2H
- InterPro
- Beta-lactam/transpept-like, Glyco_trans_51, Glycosyltr_51/Transpeptidase, Lysozyme-like_dom_sf, PBP1b_TM, PBP_1b, PBP_transglycosylase, PCN-bd_Tpept, UB2H
- Functional cluster
- Membrane Insertases & Cytochromes
Experimental structures · PDB · 11
- 3FWL X-ray 3.09A
- 3VMA X-ray 2.16A
- 5FGZ X-ray 2.85A
- 5HL9 X-ray 2.70A
- 5HLA X-ray 2.36A
- 5HLB X-ray 2.42A
- 5HLD X-ray 2.31A
- 6FZK NMR
- 6G5R NMR
- 6YN0 X-ray 2.40A
- 7LQ6 EM 3.28A
A predicted model is available from AlphaFold.
Gene Ontology · 13
- GO:0016020 membrane
- GO:0030288 outer membrane-bounded periplasmic space
- GO:0009274 peptidoglycan-based cell wall
- GO:0005886 plasma membrane
- GO:0008658 penicillin binding
- GO:0008955 peptidoglycan glycosyltransferase activity
- GO:0009002 serine-type D-Ala-D-Ala carboxypeptidase activity
- GO:0071433 cell wall repair
- GO:0009252 peptidoglycan biosynthetic process
- GO:0051518 positive regulation of bipolar cell growth
- GO:0006508 proteolysis
- GO:0008360 regulation of cell shape
- GO:0046677 response to antibiotic
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
- Penicillin-binding protein 1B 0.85
- Penicillin-binding protein 1A 0.85
- Penicillin-binding protein 1B 0.84
- Penicillin-binding protein 1A 0.84
- Penicillin-binding protein 1A 0.83
- Peptidoglycan D,D-transpeptidase FtsI 0.81
- Peptidoglycan D,D-transpeptidase FtsI 0.81
- Penicillin-binding protein 1A 0.81
- Penicillin-binding protein 1A 0.79
- Penicillin-binding protein 1A 0.79
- Penicillin-binding protein 1A 0.79
- Penicillin-binding protein 1A 0.79
Co-cited proteins · studied together in the literature
- Penicillin-binding protein 1A 3 shared papers
- Penicillin-binding protein 1C 1 shared papers
- Membrane-bound lytic murein transglycosylase A 1 shared papers
- MltA-interacting protein 1 shared papers
Literature · 14 cited papers
- Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. · 2009
- Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol. Syst. Biol. · 2006
- The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli. Mol. Microbiol. · 1999
- Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. · 1999
- Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. · 1998
- The complete genome sequence of Escherichia coli K-12. Science · 1997
- Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. J. Bacteriol. · 1997
- Localization of a putative second membrane association site in penicillin-binding protein 1B of Escherichia coli. Biochem. J. · 1996
- Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region. Nucleic Acids Res. · 1994
- Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase. J. Biol. Chem. · 1984
- Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12. Proc. Natl. Acad. Sci. U.S.A. · 1985
- The nucleotide sequences of the ponA and ponB genes encoding penicillin-binding protein 1A and 1B of Escherichia coli K12. Eur. J. Biochem. · 1985
- … and 2 more in the literature graph
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