Homologous Superfamily

Transcriptional repressor, C-terminal (IPR008988)

Short name: Transcriptional_repressor_C

Overlapping entries


The C-terminal domain of several bacterial transcriptional repressors show structural homology to one another. These domains are characterised by an SH3-like structure consisting of a partly opened beta-barrel, where the last strand is interrupted by a 3-10 helical turn. The C-terminal domain displays a metal-binding function in DTXR and IDER and may act to stabilising the dimeric form of the Escherichia coli KorB repressor, thereby enhancing specific operator binding by the repressor. The N-terminal region of these proteins is responsible for binding DNA.

Proteins containing this C-terminal domain include: the E. coli biotin repressor BirA, which has the dual role of a transcriptional repressor of the biotin operator and a biotin-activating enzyme [PMID: 1409631, PMID: 11353844]; the E. coli RP4 plasmid regulatory protein KorB, which regulates the expression of plasmid genes whose products are involved in the replication, transfer, and inheritance of RP4 [PMID: 11711548]; and the diphtheria toxin repressor (DTXR), along with its homologues in the pathogenic bacteria causing tuberculosis (IDER), leprosy, syphilis, and staphylococcal infections, which play important roles in regulating virulence-associated genes [PMID: 11320302, PMID: 11053439].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.