Category:Complex:EIIABCFrv
About
Description (originally from EcoCyc[1][2]) EIIABCFrv
Comments (originally from EcoCyc[1]) FrvAB, a PTS permease of unknown specificity, belongs to the functional superfamily of the phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The PTS transports and simultaneously phosphorylates its sugar substrates in a process called group translocation. FrvAB presumably takes up an exogenous PTS sugar, releasing the phosphate ester into the cell cytoplasm in preparation for metabolism [3][4][3][4].
FrvAB, the Enzyme IIFrv complex, possesses
two domains in a single polypeptide chain (FrvB) with the domain
order IIB-IIC and one domain in FrvA which corresponds to a IIA
protein. It is homologous to the fructose- and mannitol-specific
PTS Enzymes II. The latter has been reported to possess 6 transmembrane
α-helical segments in its IIC domain.
The IIB and IIA domains are localized to the cytoplasmic side
of the membrane. The overall PTS-mediated phosphoryl transfer
reaction, requiring the two general energy coupling proteins of
the PTS, Enzyme I and HPr, as well as the three domains of the
Enzyme II complex is presumably:
--> HPr(his~~P) --> IIA(his~~P) -->
IIB(cys~~P) -(IIC)-> sugar-P.
The frv operon (frvABXR) encodes, in addition to FrvAB, a probable hydrolase (FrvX) and a transcriptional regulatory protein (FrvR). It is presumably cryptic, but nothing is known regarding its expression.
References
- ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 Postma, PW et al. (1993) Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57 543-94 PubMed
- ↑ 4.0 4.1 Reizer, J et al. (1994) Novel phosphotransferase system genes revealed by bacterial genome analysis: unique, putative fructose- and glucoside-specific systems. Protein Sci. 3 440-50 PubMed
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