IPR049870
Sensor-kinase BvgS-like, first periplasmic domain
InterPro entry
Short name | BvgS-like_periplasmic1 |
Description
This entry represents the first of the two tandem periplasmic solute-binding domains of Virulence sensor protein BvgS from Bordetella pertussis and related proteins mainly found in proteobacteria. These domains are homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a histidine-kinase (HK), a receiver and a histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologue from Escherichia coli Sensor protein EvgS appear to be involved in the transcriptional regulation of drug efflux pumps. This domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor
[3, 4, 5].
PBP2 typically comprises two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energised by ATP hydrolysis
[1, 2].
References
1.The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. Felder CB, Graul RC, Lee AY, Merkle HP, Sadee W. AAPS PharmSci 1, E2, (1999). PMID: 11741199
2.Periplasmic binding proteins: a versatile superfamily for protein engineering. Dwyer MA, Hellinga HW. Curr. Opin. Struct. Biol. 14, 495-504, (2004). View articlePMID: 15313245
3.The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier. Bock A, Gross R. Eur J Biochem 269, 3479-84, (2002). PMID: 12135487
Cross References
ENZYME
Contributing Member Database Entry
- CDD:cd13705