Protein Family Models

The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The sugar-specific permease of the PTS consists of three domains (IIA, IIB and IIC). The IIC domain catalyses the transfer of a phosphoryl group from IIB to the sugar substrate. [1]. 9689210. Novel phosphotransferase system genes revealed by bacterial. genome analysis: the complete complement of pts genes in. mycoplasma genitalium.. Reizer J, Paulsen IT, Reizer A, Titgemeyer F, Saier MH Jr;. Microb Comp Genomics 1996;1:151-164. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

Date:

2024-08-14

This HMM represents a family of PTS enzyme II proteins in which all three domains are found in the same polypeptide chain and which appear to have a broad specificity for beta-glucosides including salicin (beta-D-glucose-1-salicylate) and arbutin (Hydroquinone-O-beta-D-glucopyranoside) [1]. These are distinct from the closely related sucrose-specific and trehalose-specific PTS transporters.

Date:

2024-05-29

PTS beta-glucoside transporter subunit IIBCA catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane

Date:

2017-03-21

These are part of the The PTS Glucose-Glucoside (Glc) SuperFamily. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). The IIA, IIB and IIC domains of all of the permeases listed below are demonstrably homologous. These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. The three-dimensional structures of the IIA and IIB domains of the E. coli glucose permease have been elucidated. IIAglchas a complex b-sandwich structure while IIBglc is a split ab-sandwich with a topology unrelated to the split ab-sandwich structure of HPr.

Date:

2021-08-24