IPR013013
Phosphotransferase system, EIIC component, type 1
InterPro entry
Short name | PTS_EIIC_1 |
domain relationships |
Description
According to sequence analyses
[1, 4, 5], the PTS EIIC domain can be divided in five groups:
* The PTS EIIC type 1 domain is found in the Glucose class of PTS and has an average length of about 80 amino acids.
* The PTS EIIC type 2 domain is found in the Mannitol class of PTS and has an average length of about 90 amino acids.
* The PTS EIIC type 3 domain is found in the Lactose class of PTS and has an average length of about 100 amino acids.
* The PTS EIIC type 4 domain is found in the Mannose class of PTS and has an average length of about 160 amino acids.
* The PTS EIIC type 5 domain is found in the Sorbitol class of PTS and has an average length of about 190 amino acids.
This entry represents the type 1 domain.
* The PTS EIIC type 1 domain is found in the Glucose class of PTS and has an average length of about 80 amino acids.
* The PTS EIIC type 2 domain is found in the Mannitol class of PTS and has an average length of about 90 amino acids.
* The PTS EIIC type 3 domain is found in the Lactose class of PTS and has an average length of about 100 amino acids.
* The PTS EIIC type 4 domain is found in the Mannose class of PTS and has an average length of about 160 amino acids.
* The PTS EIIC type 5 domain is found in the Sorbitol class of PTS and has an average length of about 190 amino acids.
This entry represents the type 1 domain.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS)
[1, 2] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars.
The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred via a signal transduction pathway, to enzyme I (EI) which in turn transfers it to a phosphoryl carrier, the histidine protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease, a membrane-bound complex known as enzyme 2 (EII), which transports the sugar to the cell. EII consists of at least three structurally distinct domains IIA, IIB and IIC
[3]. These can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII).
References
1.Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Postma PW, Lengeler JW, Jacobson GR. Microbiol. Rev. 57, 543-94, (1993). View articlePMID: 8246840
2.The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Meadow ND, Fox DK, Roseman S. Annu. Rev. Biochem. 59, 497-542, (1990). View articlePMID: 2197982
3.Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Saier MH Jr, Reizer J. J. Bacteriol. 174, 1433-8, (1992). View articlePMID: 1537788
4.The bacterial phosphotransferase system: new frontiers 30 years later. Saier MH Jr, Reizer J. Mol. Microbiol. 13, 755-64, (1994). View articlePMID: 7815935
Cross References
Contributing Member Database Entry
- PROSITE profiles:PS51103