Difference between revisions of "Part:BBa K3630010"

 
 
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<partinfo>BBa_K3630010 short</partinfo>
 
<partinfo>BBa_K3630010 short</partinfo>
  
Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like.
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"Bacterial adhesins are attached to thin thread-like, one-micron long structures that are called pili or fimbriae. They are rigid structures with a diameter of 2–10 nm. The structure mostly consists of structural protein which acts the scaffold, while the adhesin protein is present at the tip.  
 
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<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 14:56, 26 October 2020


Adhesin

"Bacterial adhesins are attached to thin thread-like, one-micron long structures that are called pili or fimbriae. They are rigid structures with a diameter of 2–10 nm. The structure mostly consists of structural protein which acts the scaffold, while the adhesin protein is present at the tip. "

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]