Penicillin-Binding Protein

A Penicillin-Binding Proteins (PBPs) are a group of Proteins that are characterized by their affinity for and binding of Penicillin.

Example(s):
- Beta-lactamase precursor (EC:3.5.2.6, penicillinase)
- Peptidoglycan synthetase ftsI (EC:2.4.1.129, peptidoglycan glycosyltransferase 3)
- Methicillin resistance mecR1 protein.
- Methicillin resistance blaR1 protein.
- Escherichia coli (strain K12) http://www.uniprot.org/uniprot/P0AD65
- Bacillus subtilis) http://www.uniprot.org/uniprot/P38050
- PMID 8109929: “The penicillin-binding protein (PBP) patterns of six strains of Bilophila wadsworthia were investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis and subsequent fluorography of membrane preparations labelled with [3H]benzylpenicillin”
Counter-Example(s):
- Penicillin-Binding Protein 2 (PBP-2).
See: DD-Transpeptidase, Protein, Penicillin, Bacteria, Beta-Lactam Antibiotic, Tabtoxinine-β-Lactam, Glutamine Synthetase, Cell Wall.

References

(Wikipedia, 2019) ⇒ https://en.wikipedia.org/wiki/Penicillin_binding_proteins Retrieved:2019-5-23.
- Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases.

The large number of penicillin binding proteins, which are represented in this group of sequences, are responsible for the final stages of peptidoglycan biosynthesis for cell wall formation. The proteins synthesise cross-linked peptidoglycan from lipid intermediates, and contain a penicillin-sensitive transpeptidase carboxy-terminal domain. The active site serine (residue 337 in P14677) is conserved in all members of this family PMID: 8605631.

MecR1 and BlaR1 are metallopeptidases belonging to MEROPS peptidase family M56, clan M-. BlaR1 and MecR1 cleave their cognate transcriptional repressors BlaI and MecI, respectively, activating the synthesis of MecA.

(Pfam, 2019) ⇒ http://pfam.xfam.org/family/PF00905 Retrieved:2019-5-23.
- QUOTE: Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases.

(InterPro, 2019) ⇒ http://www.ebi.ac.uk/interpro/entry/IPR017790 Retrieved:2019-5-23.
- QUOTE: This entry represents penicillin-binding protein 2 (PBP-2, also known as peptidoglycan D, D-transpeptidase MrdA), a protein whose gene (designated either pbpA or mrdA) is generally found next to the gene for RodA, a protein required for the rod (bacillus) shape in many bacteria PMID: 2644207. PBP-2 acts as a transpeptidase for cell elongation, hence it is involved in formation of the rod shape.