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Protein Domain : MtfA, N-terminal

Primary Identifier  IPR042252 Type  Homologous_superfamily
Short Name  MtfA_N
description  Mlc titration factor A (MtfA, previously known as YeeI) is a transcription factor A that binds Mlc (make large colonies), itself a repressor of glucose and hence a protein important in regulation of the phosphoenolpyruvate:glucose-phosphotransferase (ptsG) system, the major glucose transporter in E. coli. Mlc is a repressor of ptsG, and MtfA is found to bind and inactivate Mlc with high affinity []. The membrane-bound protein EIICBGlc encoded by the ptsG gene is the major glucose transporter in Escherichia coli. MtfA is found to be a glucose-regulated peptidase [], whose activity is regulated by binding to Mlc available in the cytoplasm, which in turn has been released from EIICBGlc during times when no glucose is taken up. A physiologically relevant target for this peptidase is not yet known.The N-terminal domain of MtfA adopts a mixed alpha/beta structure, with four α-helices, three 310-helices, and three parallel β-strands. The C-terminal domain has an all-helical structure [].This superfamily represents the N-terminal domain found in MtfA.

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