S
IPR018113

Phosphotransferase system EIIB, cysteine phosphorylation site

InterPro entry
Short namePTrfase_EIIB_Cys

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). 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) carries the first permease-specific phoshorylation site, a histidine, which is phosphorylated by phospho-HPr. The second domain (IIB) is phosphorylated by phospho-IIA on a cysteinyl or histidyl residue, depending on the permease. Finally, the phosphoryl group is transferred from the IIB domain to the sugar substrate in a process catalyzed by the IIC domain; this process is coupled to the transmembrane transport of the sugar.

This entry covers the phosphorylation site of EIIB domains.

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

GO terms

biological process

  • None

cellular component

  • None

Cross References

Contributing Member Database Entries
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.