PROSITE documentation PDOC51108 [for PROSITE entry PS51108]PTS EIID domain profile
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [1,2] is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr) (see <PDOC00318>). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains (IIA, IIB, and IIC), [3] which 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).
The first domain (IIA) (see <PDOC00528>), carries the first permease-specific phosphorylation site, an histidine which is phosphorylated by phospho-HPr. The second domain (IIB) (see <PDOC00795>) is phosphorylated by phospho-IIA on a cysteinyl or histidyl residue, depending on the sugar transported. Finally, the phosphoryl group is transferred from the IIB domain to the sugar substrate concomitantly with the sugar uptake processed by the IIC domain. The IIC (see <PDOC51103>) domain forms the translocation channel and the specific substrate-binding site. An additional transmembrane domain IID, homologous to IIC, can be found in some PTSs, e.g. for mannose [1,3,4,5,6].
We have developed a profile for this domain, which cover the entire PTS EIID domain.
Last update:April 2005 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Postma P.W. Lengeler J.W. Jacobson G.R. |
| Title | Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. | |
| Source | Microbiol. Rev. 57:543-594(1993). | |
| PubMed ID | 8246840 |
| 2 | Authors | Meadow N.D. Fox D.K. Roseman S. |
| Title | The bacterial phosphoenolpyruvate: glycose phosphotransferase system. | |
| Source | Annu. Rev. Biochem. 59:497-542(1990). | |
| PubMed ID | 2197982 | |
| DOI | 10.1146/annurev.bi.59.070190.002433 |
| 3 | Authors | Saier M.H. Jr. Reizer J. |
| Title | Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. | |
| Source | J. Bacteriol. 174:1433-1438(1992). | |
| PubMed ID | 1537788 |
| 4 | Authors | Saier M.H. Jr. Reizer J. |
| Title | The bacterial phosphotransferase system: new frontiers 30 years later. | |
| Source | Mol. Microbiol. 13:755-764(1994). | |
| PubMed ID | 7815935 |
| 5 | Authors | Tchieu J.H. Norris V. Edwards J.S. Saier M.H. Jr. |
| Title | The complete phosphotranferase system in Escherichia coli. | |
| Source | J. Mol. Microbiol. Biotechnol. 3:329-346(2001). | |
| PubMed ID | 11361063 |
| 6 | Authors | Saier M.H. Hvorup R.N. Barabote R.D. |
| Title | Evolution of the bacterial phosphotransferase system: from carriers and enzymes to group translocators. | |
| Source | Biochem. Soc. Trans. 33:220-224(2005). | |
| PubMed ID | 15667312 | |
| DOI | 10.1042/BST0330220 |
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