EC Number   |
General Information |
Reference |
|---|
   3.4.23.52 | evolution |
FlaK can only process archaellins and EppA only pilins |
-, 754570 |
| 3.4.23.52 | evolution |
in Methanococcus maripaludis, the pilins have their own dedicated prepilin peptidase, EppA, which cleaves the signal peptide from pilins but not archaellins. This is in contrast to other studied Archaea which have a single prepilin peptidase-like enzyme, PibD, that cleaves all type IV pilin-like proteins, including archaellins, pilins and sugar binding proteins. Pilins in the organism are encoded by five genes, epdA-E. FlaK can only process archaellins and EppA only pilins |
-, 754570 |
| 3.4.23.52 | more |
in Methanococcus maripaludis, the archaella are composed of three structural glycoproteins (the archaellins, FlaB1, FlaB2 and FlaB3) that are all modified at multiple positions with an N-linked tetrasaccharide |
-, 754570 |
| 3.4.23.52 | physiological function |
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. Both archaella and archaeal type IV pili are assembled from structural proteins synthesized initially as preproteins with a class III (type IV pilin-like) signal peptide which is subsequently cleaved by a dedicated prepilin peptidase-like enzyme (signal peptidase III) |
-, 754570 |
| 3.4.23.52 | physiological function |
Methanococcus maripaludis has two different surface appendages: type IV-like pili and archaella. Both structures are believed to be assembled using a bacterial type IV pilus mechanism. Each structure is composed of multiple subunits, either pilins or archaellins. Both pilins and archaellins are made initially as preproteins with type IV pilin-like signal peptides, which must be removed by a prepilin peptidase-like enzyme. This enzyme is FlaK for archaellins and EppA for pilins. The Epd pili of Methanococcus maripaludis are less numerous and thinner than archaella. Prepilin peptidase EppA cleaves the signal peptide from pilins but not archaellins |
-, 754570 |
| 3.4.23.52 | physiological function |
the enzyme plays an essential role in flagellation |
-, 716249 |
| 3.4.23.52 | physiological function |
type IV prepilin peptidase PibD processes flagellin/pilin precursors, that are essential for the biogenesis and function of the archaellum and other cell surface structures in Haloferax volcanii |
-, 753673 |
