This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix [].
Dipeptidyl peptidase FAP (also known as prolyl endopeptidase FAP, fibroblast activation protein alpha (FAP-alpha) or Seprase; MEROPS identifier S09.007), is an integral membrane serine protease that participates in extracellular matrix degradation and is involved in many cellular processes including tissue remodelling, fibrosis, wound healing, inflammation and tumour growth [, , , ].
This entry represents the transcription factor FapR, which is involved in the regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism []. FapR controls the expression of many genes involved in fatty acid and phospholipid metabolism (the fap regulon)[].
