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Table 1 The full set of predicted PBPs in L. monocytogene s

From: Identification of the full set of Listeria monocytogenes penicillin-binding proteins and characterization of PBPD2 (Lmo2812)

PBPa PBPb genec Classd Prototype aa MW (kDa) IP Putative domain structuree
PPBA1 PBP1 lmo1892 A-3 PBP1a (Spn) 827 90.87 9.15 SP-Φ-TG-TP
PBPB2 PBP2 lmo2039 B-4 PBP2x(Spn) 751 81.89 7.77 SP-Φ-D-TP
PBPB1 PBP3 lmo1438 B-5 PBP2b(Spn) 721 79.91 8.26 SP-Φ-D-TP
PBPA2 PBP4 lmo2229 A-4 PBP2a(Spn) 714 77.85 6.75 SP-Φ-TG-TP
PBPB3 ----- lmo0441 B-1 PBP2a(Sau) 678 74.60 6.57 SP-Φ-MecAN-D-TP
PBPD1 PBP5 lmo2754 C-T5 PBP3(Spn) 445 48.08 7.63 SP-CP-CA
PBPC1 ----- lmo0540 C-TH AmpH(Eco) 397 44.53 9.70 SP-BLA
PBPC2 ----- lmo1916 C-TH R61 (SR61) 335 37.84 7.04 BLA
PBPD3 ----- lmo1855 M15B ---- 274 31.08 5.46 SP-CP(VanY)
PBPD2 ----- lmo2812 C-T5 PBP5 (Bsu) 272 29.48 4.59 SP(lipo)-CP
  1. aNomenclature of PBPs as defined in [16]; bNomenclature of PBPs as defined in [7, 10]; cgene names as identified in Listilist web server http://genolist.pasteur.fr/ListiList/; dspecific class of PBP as identified in [19]; edomain structure of PBPs as described in [16]; SP, signal peptide; Φ, hydrophobic region; TG, transglycosylase domain; TP, transpeptidase domain; D, interaction domain; MecAN, homologous to PBP2a S. aureus resistance protein; CP, carboxypeptidase domain; CA, C-terminal anchor domain; BLA, β-lactamase domain; (VanY), homologous to VanY; SP(lipo), lipoprotein signal peptide.