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Helicobacter pylori  HP0377 is a thiol oxidoreductase, a member of the CcmG family involved in cytochrome biogenesis, as previously shown by  in vitro  experiments. In this report, we document that HP0377 also acts  in vivo  in the cytochrome assembly process in  Bacillus subtilis , where it complements the lack of ResA. However, unlike other characterized proteins in this family, HP0377 is a dithiol reductase and isomerase. We elucidated how the amino acid composition of its active site modulates its functionality. We demonstrated that  cis -proline (P156) is involved in its interaction with the redox partner (CcdA), as a P156T HP0377 variant is inactive  in vivo  and is present in the oxidized form in  B .  subtilis . Furthermore, we showed that engineering the HP0377 active motif by changing CSYC motif into CSYS or SSYC, clearly diminishes two activities (reduction and isomerization) of the protein. Whereas HP0377 CSYA  is inactive in reduction as well as in isomerization, HP0377 CSYS  retains reductive activity. Also, replacement of F95 by Q decreases its ability to regenerate scRNase and does not influence the reductive activity of HP0377 CSYS  towards apocytochrome c. HP0377 is also distinguished from other CcmGs as it forms a 2:1 complex with apocytochrome c. Phylogenetic analyses showed that, although HP0377 is capable of complementing ResA in  Bacillus subtilis , its thioredoxin domain has a different origin, presumably common to DsbC.

plos one

Impact of selected amino acids of HP0377 (Helicobacter pylori thiol oxidoreductase) on its functioning as a CcmG (cytochrome c maturation) protein and Dsb (disulfide bond) isomerase