Skip to main content

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.