InterPro : IPR024187

Name  Signal transduction response regulator, citrate/malate metabolism Short Name  Sig_transdc_resp-reg_cit/mal
Type  Family Description  Members of this group are response regulators containing CheY-like receiver and HTH (helix-turn-helix) DNA-binding domains (cognate sensor kinases are in ). Several members of this group have been characterised as response regulators controlling the genes involved in metabolism of citrate or C4-dicarboxylates (aspartate, fumarate, malate, and succinate). In Klebsiella pneumoniae, the phosphorylation of CitB, subsequent conformational changes and increase of apparent DNA-binding affinity (10 to 100-fold), and specific binding to the two sites in the citC-citS intergenic region have been shown experimentally []. The DcuS/R system in Escherichia coliis involved in C4-dicarboxylate-stimulated regulation of the genes encoding the anaerobic fumarate respiratory system []. The DpiB/A system (synonyms: CriR, CitB, but note that the name CitB can also be used for unrelated proteins) is involved in transcriptional regulation of the cit operon (citrate-specific fermentation genes) and of genes involved in plasmid inheritance [].Response regulators of the microbial two-component signal transduction systems typically consist of an N-terminal CheY-like receiver domain and a C-terminal output (usually DNA-binding) domain [, ]. In response to an environmental stimulus, a phosphoryl group is transferred from the His residue of sensor histidine kinase to an Asp residue in the CheY-like receiver domain of the cognate response regulator. Phosphorylation of the CheY-like receiver domain induces conformational changes that activate an associated output domain. Phosphorylation-induced conformational changes in the response regulator molecule have been demonstrated in direct structural studies []. In members of this group, these conformational changes affect the binding of the associated HTH domains to their recognition sites on the chromosomal DNA.HTH domains are very diverse with respect to their sequence, as well as the specific binding sites that they recognise [, , ]. There have been several attempts to classify them [, ]. A detailed sequence analysis of response regulator proteins has been hampered by the remarkable sequence conservation of their N-terminal CheY-like receiver domain, which largely masked (dis)similarities of the DNA-binding domains of various response regulators.For additional information please see [, ].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

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0 Found In

0 Parent Features

10 Publications

First Author Title Year Journal Volume Pages
Stock AM Two-component signal transduction. 2000 Annu Rev Biochem 69 183-215
West AH Histidine kinases and response regulator proteins in two-component signaling systems. 2001 Trends Biochem Sci 26 369-76
Zientz E Fumarate regulation of gene expression in Escherichia coli by the DcuSR (dcuSR genes) two-component regulatory system. 1998 J Bacteriol 180 5421-5
Lewis RJ Dimer formation and transcription activation in the sporulation response regulator Spo0A. 2002 J Mol Biol 316 235-45
Volz K Structural conservation in the CheY superfamily. 1993 Biochemistry 32 11741-53
Meyer M In vitro binding of the response regulator CitB and of its carboxy-terminal domain to A + T-rich DNA target sequences in the control region of the divergent citC and citS operons of Klebsiella pneumoniae. 1997 J Mol Biol 269 719-31
Ingmer H Destabilized inheritance of pSC101 and other Escherichia coli plasmids by DpiA, a novel two-component system regulator. 1998 Mol Microbiol 29 49-59
Wintjens R Structural classification of HTH DNA-binding domains and protein-DNA interaction modes. 1996 J Mol Biol 262 294-313
Müller CW Transcription factors: global and detailed views. 2001 Curr Opin Struct Biol 11 26-32
Bott M Anaerobic citrate metabolism and its regulation in enterobacteria. 1997 Arch Microbiol 167 78-88

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)