Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
helix-turn-helix domain-containing protein
helix-turn-helix domain-containing protein such as an XRE (Xenobiotic Response Element) family transcriptional regulator SinR of Bacillus subtilis, which represses biofilm formation by binding to the respective eps promoter
This is a helix-turn-helix domain that probably binds to DNA. (from Pfam)
Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains. (from Pfam)
This domain is a helix-turn-helix domain that probably binds to DNA. (from Pfam)
DNA-binding anti-repressor SinI
SinR is a pleiotropic regulator of several late growth processes. It is a tetrameric DNA binding protein whose activity is down-regulated thorough the formation of a SinI:SinR protein complex. When complexed with SinI, the SinR tetramer is disrupted such that is no longer able to bind DNA. [1]. 8422983. SinI modulates the activity of SinR, a developmental switch protein of Bacillus subtilis, by protein-protein interaction. Bai U, Mandic-Mulec I, Smith I;. Genes Dev. 1993;7:139-148. [2]. 8549812. Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, SinI. Lewis RJ, Brannigan JA, Smith I, Wilkinson AJ;. FEBS Lett. 1996;378:98-100. (from Pfam)
This large family of DNA binding helix-turn helix proteins includes Cro Swiss:P03036 and CI Swiss:P03034. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteristic of the whole family [1]. [1]. 20196080. The crystal structure of NGO0477 from Neisseria gonorrhoeae reveals a novel protein fold incorporating a helix-turn-helix motif. Ren J, Sainsbury S, Nettleship JE, Saunders NJ, Owens RJ;. Proteins. 2010;78:1798-1802. (from Pfam)
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on