Histidine phosphotransferase ChpT, C-terminal (IPR018762)

Short name: ChpT_C

Overlapping homologous superfamilies

Domain relationships



This entry represents the C-terminal domain of ChpT.

ChpT is a phosphotransferase that controls the activity of the master bacterial cell-cycle regulator CtrA through phosphorylation. It behaves as a homodimer by adopting the domain architecture of the intracellular part of class I histidine kinase (HK). Each subunit consists of two distinct domains: an N-terminal helical hairpin domain and a C-terminal [alpha]/[beta] domain. The two N-terminal domains are adjacent within the dimer, forming a four-helix bundle. The C-terminal domain adopts an atypical Bergerat ATP-binding fold [PMID: 22949187]. However, despite its similarity with HK, the C-terminal domain of ChpT lacks regions required for ATP binding including the D-box, F-Box, and G-Box. ChpT has also been shown to be unable to bind ATP in vitro. Therefore, it has been suggested that ChpT is unable to catalyze ATP hydrolysis and functions solely as a phosphotransferase [PMID: 26124143].

Contributing signatures

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