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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51674
4Fe-4S WhiB-like (Wbl)-type iron-sulfur binding domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51674

Description

Members of the WhiB-like (Wbl) family are found exclusively in actinobacteria and are implicated in the regulation of developmental processes. All WhiB-like proteins have four conserved cysteine residues where two of them are in a C-X-X-C motif. The four cysteine residues are proposed to act as the ligands for a [4Fe-4S] cluster. Wbl-mediated transcription regulation is dependent upon the presence or absence and state (nitrosylated or non-nitrosylated) of the [4Fe-4S] cluster [1,2,3].

The profile we developed covers the entire Wbl-type 4Fe-4S domain.

Last update:

May 2013 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

4FE4S_WBL, PS51674; 4Fe-4S WhiB-like (Wbl)-type iron-sulfur binding domain profile  (MATRIX)


References

1AuthorsGarg S.K. Suhail Alam M. Soni V. Radha Kishan K.V. Agrawal P.
TitleCharacterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase.
SourceProtein Expr. Purif. 52:422-432(2007).
PubMed ID17157031
DOI10.1016/j.pep.2006.10.015

2Authorsden Hengst C.D. Buttner M.J.
TitleRedox control in actinobacteria.
SourceBiochim. Biophys. Acta 1780:1201-1216(2008).
PubMed ID18252205
DOI10.1016/j.bbagen.2008.01.008

3AuthorsSmith L.J. Stapleton M.R. Buxton R.S. Green J.
TitleStructure-function relationships of the Mycobacterium tuberculosis transcription factor WhiB1.
SourcePLoS ONE 7:E40407-E40407(2012).
PubMed ID22792304
DOI10.1371/journal.pone.0040407



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