Switches.ELM

Switch #:

SWTI000632

Switch type:
Binary

Switch subtype:
Physicochemical compatibility

Description:
Phosphorylation of T22 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Serine/threonine-protein kinase pknB (pknB) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details).

Participants:
(1) Uncharacterized protein Rv1827/MT1875 (Rv1827)

Interactions

Interaction #1 Rv1827 - Rv1827(intramolecular)
intramolecular
Interfaces
(1) LIG_FHA_1 motif (₂₀ETTSVFR₂₆) in Uncharacterized protein Rv1827/MT1875 (Rv1827)
(2) FHA domain_(77-140) in Uncharacterized protein Rv1827/MT1875 (Rv1827)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of T₂₂ on Uncharacterized protein Rv1827/MT1875 (Rv1827)) of the Uncharacterized protein Rv1827/MT1875 (Rv1827) LIG_FHA_1 motif - Uncharacterized protein Rv1827/MT1875 (Rv1827) FHA domain interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: T₂₂: Serine/threonine-protein kinase pknB (pknB)

Additional Information
Structural information: 2KFU

Context

Switch localisation
ELM curated: nucleus

References

(1) An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis.
Nott et al. Sci Signal (2009)