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MalT-like TPR region
This entry contains a series of TPR repeats. [1]. 11709169. Crystal structure of transcription factor MalT domain III: a. novel helix repeat fold implicated in regulated oligomerization.. Steegborn C, Danot O, Huber R, Clausen T;. Structure. 2001;9:1051-1060.. [2]. 22171003. Inscuteable and NuMA proteins bind competitively to Leu-Gly-Asn. repeat-enriched protein (LGN) during asymmetric cell divisions.. Culurgioni S, Alfieri A, Pendolino V, Laddomada F, Mapelli M;. Proc Natl Acad Sci U S A. 2011;108:20998-21003.. [3]. 22215984. Structural basis of response regulator inhibition by a bacterial. anti-activator protein.. Baker MD, Neiditch MB;. PLoS Biol. 2011;9:e1001226.. [4]. 23526880. Structural basis of Rap phosphatase inhibition by Phr peptides.. Gallego del Sol F, Marina A;. PLoS Biol. 2013;11:e1001511.. [5]. 23519214. Structural basis for kinesin-1:cargo recognition.. Pernigo S, Lamprecht A, Steiner RA, Dodding MP;. Science. 2013;340:356-359.. [6]. 23526881. Conformational change-induced repeat domain expansion regulates. Rap phosphatase quorum-sensing signal receptors.. Parashar V, Jeffrey PD, Neiditch MB;. PLoS Biol. 2013;11:e1001512. (from Pfam)
LuxR C-terminal-related transcriptional regulator
HTH-type transcriptional regulator MalT
HTH-type transcriptional regulator MalT regulates transcription of the maltose regulon and thus the uptake and catabolism of malto-oligosaccharides
Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides
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