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PROSITE documentation PDOC50930 [for PROSITE entry PS50930] |
The LytTR ('litter') HTH domain is a DNA-binding, potential winged helix-turn-helix (wHTH) domain of about 100 amino acids, present in bacterial transcriptional regulators of the algR/agrA/lytR family. It is named after Bacillus subtilis LytT and Staphylococcus aureus lytR response regulators, involved in the regulation of cell autolysis [1]. The LytTR domain is found in several bacterial cytoplasmic proteins that regulate the production of important virulence factors, like extracellular polysaccharides, toxins and bacteriocins. These response regulators of the microbial two-component signal transduction systems contain N-terminal cheY-like domains (see <PDOC50110>) and the LytTR domain in the C-terminal part is expected to bind to specific DNA sequences in the upstream regions of target genes [2]. Other domains found N-terminally of LytTR are an ATP-binding domain of ABC-type transporter family (see <PDOC00185>) and a PAS domain (see <PDOC50112>). Besides these cytoplasmic proteins, LytTR also occurs in membrane-bound bacterial proteins. The N-terminal parts of these proteins contain three to eight predicted transmembrane segments or the transmembrane MHYT domain (see <PDOC50924>).
According to secondary structure predictions the LytTR domain consists of four β-strands and three α-helices. The structure is predicted to form a novel type of DNA-binding domain, showing similarity to the 'winged HTH' or 'winged helix' proteins [1,2].
Some cytoplasmic proteins known to contain a LytTR domain:
Some membrane-bound proteins known to contain a LytTR domain:
The profile we developed covers the entire LytTR domain.
Last update:October 2003 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Nikolskaya A.N. Galperin M.Y. |
Title | A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family. | |
Source | Nucleic Acids Res. 30:2453-2459(2002). | |
PubMed ID | 12034833 |
2 | Authors | McGowan S. Lucet I.S. Cheung J.K. Awad M.M. Whisstock J.C. Rood J.I. |
Title | The FxRxHrS motif: a conserved region essential for DNA binding of the VirR response regulator from Clostridium perfringens. | |
Source | J. Mol. Biol. 322:997-1011(2002). | |
PubMed ID | 12367524 |