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PROSITE documentation PDOC51071

RpiR-type HTH domain profile





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

HTH_RPIR, PS51071; RpiR-type HTH domain profile  (MATRIX)


References

1AuthorsSorensen K.I. Hove-Jensen B.
TitleRibose 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.
SourceJ. Bacteriol. 178:1003-1011(1996).
PubMed ID8576032

2AuthorsKim C. Song S. Park C.
TitleThe D-allose operon of Escherichia coli K-12.
SourceJ. Bacteriol. 179:7631-7637(1997).
PubMed ID9401019

3AuthorsYamamoto H. Serizawa M. Thompson J. Sekiguchi J.
TitleRegulation of the glv operon in Bacillus subtilis: YfiA (GlvR) is a positive regulator of the operon that is repressed through CcpA and cre.
SourceJ. Bacteriol. 183:5110-5121(2001).
PubMed ID11489864



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