Nature - USA (2020-08-20)

Article

TMD

E.clocacae

K.pneumoniae

S.typhimurium

Y.pestis

V.cholerae

PH.influenz.rustigianiia

S.frigidimarina

V.parahaemolyticus

E.coli

10 20 30 40 50 60 70 80 90 100

110 120 130 140 150 160 170 180 190 200

210 220 230 240 250 260 270 280 290 300 310

320 330 340 350 360 370 380 390 400

410 420 430 440 450 460 470 480 490

500 510 520 530 540 550 560 570 580

E.clocacae

K.pneumoniae

S.typhimurium

Y.pestis

V.cholerae

PH.influenz.rustigianiia

S.frigidimarina

V.parahaemolyticus

E.coli

E.clocacaK.pneumoniaee

S.typhimurium

Y.pestis

V.cholerae

PH.influenz.rustigianiia

S.frigidimarina

V.parahaemolyticus

E.coli

E.clocacae

K.pneumoniae

S.typhimurium

Y.pestis

V.cholerae

P.rustigianii

H.influenzS.frigidimarinaa

V.parahaemolyticus

E.coli

E.clocacae

K.pneumoniae

S.typhimurium

Y. pestis

V.cholerae

P.rustigianiiH.influenza

S.frigidimarina

V. parahaemolyticus

E.coli

E.clocacaeK.pneumoniae

S.typhimurium

Y. pestis

V.choleraeP.rustigianii

H.influenzS.frigidimarinaa

V. parahaemolyticus

E.coli

PD

IFD

lipid A-binding motif

pseudo-hydrolase site residues

Extended Data Fig. 5 | Sequence alignment of then PbgA homologues.
Sequence alignment of ten PbgA sequences from Enterobacteriaceae
Gram-negative bacteria. Domain boundaries are based on E. coli PbgA

structure are indicated, including the lipid A-binding motif (red shade) and

pseudo-hydrolase active site residues (orange triangles).