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. 2002 Dec;184(23):6465–6471. doi: 10.1128/JB.184.23.6465-6471.2002

FIG. 1.

FIG. 1.

PilT sequence and purification. (A) Conservation of PilT and putative type II secretion ATPase family members. A. aeolicus, P. aeruginosa, and N. gonorrhoeae PilT, A. aeolicus and P. aeruginosa PilU, P. aeruginosa PilB (putative NTPase required for pilus assembly), and P. aeruginosa XcpR (type II secretion putative nucleotide-binding protein) were aligned with the GCG package program PILEUP. The sequence of amino acids 83 to 348 of A. aeolicus PilT is shown. Identities or conservative changes among at least six of these seven are in bold uppercase letters, while identities or conservative changes among all three PilT proteins are in uppercase. The Walker A motif, ASP box, Walker B motif, and HIS boxes (shaded, in that order) identify the putative type II and type IV secretion ATPase families (26). The K149Q mutation is noted with an asterisk (see text). An N-terminal extension of approximately 200 amino acids is not shown for PilB and XcpR. Pair wise amino acid identity for PilT is 68% for the P. aeruginosa and N. gonorrhoeae proteins and 51% for the P. aeruginosa and A. aeolicus proteins. (B) Purification of A. aeolicus PilT. TL, total cell lysate from E. coli BL21(DE3)/pet23a(+)AaPilTHis6 after IPTG induction; WT, purified PilT-His6; K149Q, purified PilT K149Q. The positions of molecular size markers (lane M) are indicated.