Home  |  Contact
PROSITE documentation PDOC51103

PTS EIIC domain profiles





Description

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 domain forms the translocation channel and the specific substrate-binding site. An additional transmembrane domain IID (see <PDOC51108>), homologous to IIC, can be found in some PTSs, e.g. for mannose [1,3,4,5,6].

According to sequence analyses [1,4,5,6], 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.

We have developed five profiles that cover the entire PTS EIIC domains. These profiles are directed respectively against the Glucose class of PTS, the Mannitol class of PTS, the Lactose class of PTS, the Mannose class of PTS, and the Sorbitol class of PTS.

Last update:

May 2005 / Revision to a profile

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PTS_EIIC_TYPE_1, PS51103; PTS_EIIC type-1 domain profile  (MATRIX)

PTS_EIIC_TYPE_2, PS51104; PTS_EIIC type-2 domain profile  (MATRIX)

PTS_EIIC_TYPE_3, PS51105; PTS_EIIC type-3 domain profile  (MATRIX)

PTS_EIIC_TYPE_4, PS51106; PTS_EIIC type-4 domain profile  (MATRIX)

PTS_EIIC_TYPE_5, PS51107; PTS_EIIC type-5 domain profile  (MATRIX)


References

1AuthorsPostma P.W. Lengeler J.W. Jacobson G.R.
TitlePhosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.
SourceMicrobiol. Rev. 57:543-594(1993).
PubMed ID8246840

2AuthorsMeadow N.D. Fox D.K. Roseman S.
TitleThe bacterial phosphoenolpyruvate: glycose phosphotransferase system.
SourceAnnu. Rev. Biochem. 59:497-542(1990).
PubMed ID2197982
DOI10.1146/annurev.bi.59.070190.002433

3AuthorsSaier M.H. Jr. Reizer J.
TitleProposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.
SourceJ. Bacteriol. 174:1433-1438(1992).
PubMed ID1537788

4AuthorsSaier M.H. Jr. Reizer J.
TitleThe bacterial phosphotransferase system: new frontiers 30 years later.
SourceMol. Microbiol. 13:755-764(1994).
PubMed ID7815935

5AuthorsTchieu J.H. Norris V. Edwards J.S. Saier M.H. Jr.
TitleThe complete phosphotranferase system in Escherichia coli.
SourceJ. Mol. Microbiol. Biotechnol. 3:329-346(2001).
PubMed ID11361063

6AuthorsSaier M.H. Hvorup R.N. Barabote R.D.
TitleEvolution of the bacterial phosphotransferase system: from carriers and enzymes to group translocators.
SourceBiochem. Soc. Trans. 33:220-224(2005).
PubMed ID15667312
DOI10.1042/BST0330220



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)