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. 2003 Jun;185(11):3361–3372. doi: 10.1128/JB.185.11.3361-3372.2003

FIG. 5.

FIG. 5.

Alignment of R. capsulatus CrgA (Rc CrgA) with R. capsulatus CcdA (Rc CcdA) and E. coli DsbD (Ec DsbD). Amino acid alignment shows similarities between R. capsulatus CrgA and DsbD polypeptides from Haemophilus influenzae (hiDsbD), Pseudomonas aeruginosa (paDsbD), and E. coli, as well as between R. capsulatus CrgA and R. capsulatus CcdA. Predicted or experimentally confirmed membrane topologies of R. capsulatus CrgA, R. capsulatus CcdA, and E. coli DsbD are also aligned, showing the location of the transmembrane helices (TM). Amino acid sequences of TM7 and TM8 of R. capsulatus CrgA and E. coli DsbD are nonhomologous and are thus indicated in different shades of grey. The conserved cysteine and proline residues are indicated with filled circles and asterisks, respectively, and the numbers indicate the amino acid residues in each protein shown. Black and grey boxes correspond to completely and partially conserved residues, respectively. C, C terminus; N, N terminus.