PF18431

Bacterial CdiA-CT RNAse A domain

Pfam entry
Member databasePfam
Pfam typedomain
Short nameRNAse_A_bac
Author El-Gebali S;0000-0003-1378-5495
Sequence Ontology0000417

Description

Contact-dependent growth inhibition (CDI) is an important mechanism of inter-bacterial competition found in many Gram-negative pathogens. CDI+ cells express cell-surface CdiA proteins that bind neighboring bacteria and deliver C-terminal toxin domains (CdiA-CT) to inhibit target-cell growth. Structure analysis of CdiA-CT shows that it adopts the same fold (with two beta-sheets forming an overall kidney shape) as angiogenin and other RNase A paralogs, but the toxin does not share sequence similarity with these nucleases and lacks the characteristic disulfide bonds of the superfamily. Furthermore, structural comparison analysis identified human angiogenin, Rana pipiens protein P-30 (onconase) and mouse pancreatic ribonuclease (RNase 1) as the closest structural homologs of CdiA-CT
[1]
.

References

1.The CDI toxin of Yersinia kristensenii is a novel bacterial member of the RNase A superfamily. Batot G, Michalska K, Ekberg G, Irimpan EM, Joachimiak G, Jedrzejczak R, Babnigg G, Hayes CS, Joachimiak A, Goulding CW. Nucleic Acids Res. 45, 5013-5025, (2017). View articlePMID: 28398546

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