Part:BBa_K4812001
Scl2.28-1
Sequence of collagen-like protein from Streptococcus pyogenes. GenBank: AY069936.1
Usage and Biology
Collagen-like triple helical proteins have been of great interest in the field of synthetic biology due to their myriad applications. Several collagen-like sequences have been identified in bacteria, and among these Scl1 and Scl2 from Streptococcus pyogenes are perhaps the most widely studied (Xu et. al., 2002). Bacterial collagen-like proteins provide a blank canvas onto which modifications can be introduced as desired for specific applications, such as heparin-binding site and the integrin-binding site (Peng et. al., 2014). However, Scl2 forms a two-domain lollipop-like structure in contrast to the fibrillar structure of mammalian collagen. This is due to the lack of enzymes responsible for post-translational modifications in bacteria. Incorporation of non-coding amino acids (ncAA), such as hydroxyproline (Hyp), has been gaining a lot of attention.
Scl2.28 is related to Scl1.1 (Part: BBa_K4812000), but each has a significantly different primary amino acid sequence. Scl2.28 is made of Ss, signal sequence; V, variable region; CL, collagen-like region; and WM, cell wall/membrane region. The collagen-like region in Scl2.28 is made of 79 Gly-Xaa-Yaa (GXY) motifs that lead to the triple helical structure. The N-terminus of the protein is called the variable (V) region, composed of a noncollagenous sequence and consists of 73 amino acids in Scl2.2. Scl2.28 forms a lollipop-like structure with the stalk being made of collagen-like region and globular head made of the V region.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 715
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 502
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