Tryptophan-rich sensory protein
| TspO_MBR | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | TspO_MBR | ||||||||
| Pfam | PF03073 | ||||||||
| InterPro | IPR004307 | ||||||||
| TCDB | Manning Peyton Manning | ||||||||
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| Available protein structures: | |
|---|---|
| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
Tryptophan-rich sensory proteins (TspO) are a family of proteins that are involved in transmembrane signalling. In either prokaryotes or they are localized to the , and have been shown to bind and transport dicarboxylic tetrapyrrole intermediates of the haem biosynthetic pathway. They are associated with the major porins (in prokaryotes) and with the voltage-dependent anion channel (in mitochondria).
TspO of Rhodobacter sphaeroides is involved in signal transduction, functioning as a negative regulator of the expression of some photosynthesis genes (PpsR/AppA repressor/antirepressor regulon). This down-regulation is believed to be in response to oxygen levels. TspO works through (or modulates) the PpsR/AppA system and acts upstream of the site of action of these regulatory proteins. It has been suggested that the TspO regulatory pathway works by regulating the efflux of certain tetrapyrrole intermediates of the haem/bacteriochlorophyll biosynthetic pathways in response to the availability of molecular oxygen, thereby causing the accumulation of a biosynthetic intermediate that serves as a corepressor for the regulated genes. A homologue of the TspO protein in Rhizobium meliloti is involved in regulating expression of the ndi locus in response to stress conditions.
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