Part:BBa_K3819147
sdbA, encoding a protein which specifically binds the dockerin domain of CipA
The fibrinomeric integrin CipA is the scaffold protein of the cellulose-hydrolyzed complex produced by Clostridium thermonium and contains a cooH-terminal replication fragment called the Dockerin domain. Cloning and sequencing of sdbA (Scaffoldin Dockerin Binding), which encodes proteins that specifically bind CipA's Dockerin domain. The sequence contained an open reading frame consisting of 1,893 nucleotides, encoding a 631 amino acid polypeptide, called SdbA, with a calculated molecular weight of 68577 kDa. SAA consists of a leading peptide at the end of NH2 and three different regions. The NH2 terminal region is similar to the NH2 terminal duplication of C. Thermocellum OlpB and ORF2p. The central region is rich in lysine and contains motifs present in streptococcal M proteins. The COOH terminal region consists of a triplet sequence that is present in the surface proteins of some bacterial cells. The NH2-terminal region of SdbA binds to the DOCkerin domain of CipA with the fusion protein containing the first OlpB NH2-terminal repeats.Western blot and electron microscopy of immunocytochemically labeled cells showed that SdbA was located on the cell surface and was a component of fibrosomes. SdbA can mediate the anchoring of fibrinoid on c. Thermocellum cell surface through interaction with CipA's Dockerin domain.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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