Penicillin-binding protein 2x
Also known as: SP_0336, pbpX
Function
A transpeptidase that forms peptide cross-links between adjacent glycan strands in cell wall peptidoglycan (PG). Part of the divisome machinery that synthesizes the septal cross wall. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.
Classification
- Family (Pfam)
- PF03793 PASTA, PF03717 PBP_dimer, PF00905 Transpeptidase
- InterPro
- Beta-lactam/transpept, Beta-lactam/transpept-like, PASTA_dom, PBP_dimer, PBP_dimer_sf, PbpX, PCN-bd_Tpept
- Functional cluster
- Cell-Surface & Secreted Bacterial Proteins
Experimental structures · PDB · 8
- 1PMD X-ray 3.50A
- 1QME X-ray 2.40A
- 1QMF X-ray 2.80A
- 1RP5 X-ray 3.00A
- 2Z2L X-ray 2.85A
- 2Z2M X-ray 2.60A
- 2ZC3 X-ray 2.50A
- 2ZC4 X-ray 2.80A
A predicted model is available from AlphaFold.
Gene Ontology · 7
Drugs targeting this protein · 1
- CEFTAROLINE FOSAMIL inhibitor
Related proteins · sequence + function similarity
- Penicillin-binding protein 2B 0.92
- Penicillin-binding protein 2B 0.92
- Penicillin-binding protein 2B 0.92
- Penicillin-binding protein 2B 0.92
- Penicillin-binding protein H 0.88
- Penicillin-binding protein 2A 0.88
- Penicillin-binding protein 2a 0.84
- Penicillin-binding protein 2a 0.84
- Penicillin-binding protein 1A 0.83
- Penicillin-binding protein 1A 0.82
- Penicillin-binding protein 1A 0.82
- Penicillin-binding protein 1A 0.79
Literature · 2 cited papers
- Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science · 2001
- X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. · 1996
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