PROSITE documentation PDOC51071RpiR-type HTH domain profile
The rpiR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 75-80 amino acids present in prokaryotic regulators of transcription. The domain is named after Escherichia coli rpiR, also known as alsR, a repressor of the rpiB gene and the als operon, which encode proteins involved in sugar metabolism. The DNA-binding rpiR-type HTH domain occurs usually in the N-terminal part; the C-terminal part can contain a phosphosugar-binding SIS domain. Most rpiR-type HTH regulators are involved in sugar metabolism as transcription repressors, but some are activators [1,2,3].
Some proteins known to contain a rpiR-type HTH domain:
- Escherichia coli rpiR, a transcription repressor of ripB, a ribose-phosphate isomerase, and of the als operon, involved in transport and metabolism of allose.
- Pseudomonas aeruginosa hexR, a transcription repressor of the hex regulon, involved in sugar metabolism.
- Bacillus subtilis glvR, a transcription activator of the glv operon, involved in transport and metabolism of maltose [3].
The profile we developed spans the entire rpiR-type HTH DNA-binding domain.
Last update:January 2005 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Sorensen K.I. Hove-Jensen B. |
Title | Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression. | |
Source | J. Bacteriol. 178:1003-1011(1996). | |
PubMed ID | 8576032 |
2 | Authors | Kim C. Song S. Park C. |
Title | The D-allose operon of Escherichia coli K-12. | |
Source | J. Bacteriol. 179:7631-7637(1997). | |
PubMed ID | 9401019 |
3 | Authors | Yamamoto H. Serizawa M. Thompson J. Sekiguchi J. |
Title | Regulation of the glv operon in Bacillus subtilis: YfiA (GlvR) is a positive regulator of the operon that is repressed through CcpA and cre. | |
Source | J. Bacteriol. 183:5110-5121(2001). | |
PubMed ID | 11489864 |
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