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:

2024-10-16

Date:

2024-08-14

This HMM represents the fused enzyme II B and C components of the trehalose-specific PTS sugar transporter system [1]. Trehalose is converted to trehalose-6-phosphate in the process of translocation into the cell. These transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr) [2]. The exceptions to this rule are Staphylococci and Streptococci which contain their own A domain as a C-terminal fusion. This family is closely related to the sucrose transporting PTS IIBC enzymes and the B and C domains of each are described by subfamily-domain level TIGRFAMs models (TIGR00826 and TIGR00852, respectively). In E. coli, B. subtilis and P. fluorescens the presence of this gene is associated with the presence of trehalase which degrades T6P to glucose and glucose-6-P. Trehalose may also be transported (in Salmonella) via the mannose PTS or galactose permease systems [3], or (in Sinorhizobium, Thermococcus and Sulfolobus, for instance) by ABC transporters [4,5,6].

Gene:

treP

Date:

2022-10-11

PTS trehalose transporter subunit IIBC is component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, which catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane

Date:

2019-06-07

The PTS Glucose-Glucoside (Glc) Family (TC 4.A.1) Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. 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). These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the E. coli 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. This HMM is specific for the IIB domain of the Glc family PTS transporters.

Date:

2021-11-04

Involved in the phosphorylation and transport of sugars across the cell membrane; protein IIA transfers a phosphoryl group to IIB which then transfers the phosphoryl group to the sugar; IIC forms the translocation channel for the sugar uptake

Gene:

treB

Date:

2022-10-11