PROSITE documentation PDOC51482
DegV domain profile


The DegV protein family received its name based on sequence similarity to the DegV protein from Bacillus subtilis. All members of the DegV family are from bacteria, mostly Firmicutes. The function of DegV proteins is not yet completely understood, but structural evidence indicates that they can bind different fatty acids [1,2].

The DegV domain consists of two different α/β folds (see <PDB:3FYS>). The N-terminal domain, which contains seven β-strands and six α-helices, can be further divided into two subdomains: a three-layer α/β core domain and a small peripheral subdomain including a three-stranded antiparallel β-sheet and one α-helix. The C-terminal domain contains six β-strands and five α-helices in a two-layered α/β-arrangement. The two domains mainly interact through hydrophobic contacts and form a ligand-binding pocket at the domain interface [1,2].

The profile we developed covers the entire DegV domain.

Last update:

February 2010 / First entry.


Technical section

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

DEGV, PS51482; DegV domain profile  (MATRIX)


1AuthorsSchulze-Gahmen U. Pelaschier J. Yokota H. Kim R. Kim S.-H.
TitleCrystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein.
SourceProteins 50:526-530(2003).
PubMed ID12577257

2AuthorsNan J. Zhou Y. Yang C. Brostromer E. Kristensen O. Su X.-D.
TitleStructure of a fatty-acid-binding protein from Bacillus subtilis determined by sulfur-SAD phasing using in-house chromium radiation.
SourceActa Crystallogr. D 65:440-448(2009).
PubMed ID19390149

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