Protein Domain : IPR013011

Type:  Domain Name:  Phosphotransferase system, EIIB component, type 2
Description:  The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [, ] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates and coupled with translocation across the cell membrane, makes the PTS a link between the uptake and metabolism of sugars.The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred via a signal transduction pathway, to enzyme I (EI) which in turn transfers it to a phosphoryl carrier, the histidine protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease, a membrane-bound complex known as enzyme 2 (EII), which transports the sugar to the cell. EII consists of at least three structurally distinct domains IIA, IIB and IIC []. These 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 or EIIA) carries the first permease-specific phosphorylation site, a histidine which is phosphorylated by phospho-HPr. The second domain (IIB or EIIB) 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. This third domain (IIC or EIIC) forms the translocation channel and the specific substrate-binding site. An additional transmembrane domain IID, homologous to IIC, can be found in some PTSs, e.g. for mannose [, , , ]. According to structural and sequence analyses, the PTS EIIB domain () can be divided in five groups [, , ]: The PTS EIIB type 1 domain, which is found in the Glucose class of PTS, has an average length of about 80 amino acids. It forms a split alpha/beta sandwich composed of an antiparallel sheet (beta 1 to beta 4) and three alpha helices superimposed onto one side of the sheet. The phosphorylation site (Cys) is located at the end of the first beta strand on a protrusion formed by the edge of beta 1 and the reverse turn between beta 1 and beta 2 [].The PTS EIIB type 2 domain, which is found in the Mannitol and Fructose class of PTS, has an average length of about 100 amino acids. It consists of a four stranded parallel beta sheet flanked by two alpha helices (alpha 1 and 3) on one face and helix alpha 2 on the opposite face, with a characteristic Rossmann fold comprising two right-handed beta-alpha-beta motifs. The phosphorylation site (Cys) is located at the N terminus of the domain, in the first beta strand. The PTS EIIB type 3 domain, which is found in the Lactose class of PTS, has an average length of about 100 amino acids. It is composed of a central four-stranded parallel open twisted beta sheet, which is flanked by three alpha helices on the concave side and two on the convex side of the beta sheet. The phosphorylation site (Cys) is located in the C-terminal end of the first beta strand [].The PTS EIIB type 4 domain, which is found in the Mannose class of PTS, has an average length of about 160 amino acids. It has a central core of seven parallel beta strands surrounded by a total of six alpha-helices. Three helices cover the front face, one the back face with the remaining two capping the central beta sheet at the top and bottom. The phosphorylation site (His) is located at the suface exposed loop between strand 1 and helix 1 []. The PTS EIIB type 5 domain, which is found in the Sorbitol class of PTS, has an average length of about 190 amino acids. The phosphorylation site (Cys) is located in the N terminus of the domain. An EIIB-like type 2 domain can be found in bacterial transcriptional regulatory proteins []. In these cases, the EIIB-like domain is found in association with other domains like the DeoR-type HTH domain or the PTS regulatory domain (a transcriptional antiterminator). It may possess a regulatory function through its phosphorylation activity, or act as a simple phosphoryl donor. This entry represents the EIIB type 2 domain. Short Name:  PTS_EIIB_2
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2 Child Features

DB identifier Type Name
IPR029503 Domain Phosphotransferase system EIIB component, mannitol-specific
IPR003353 Domain Phosphotransferase system, fructose-specific IIB subunit

0 Contains

1 Cross References

Identifier
PS51099

1 Found In

DB identifier Type Name
IPR017180 Family Phosphotransferase system component IIBC, sugar-specific, predicted

2 GO Annotations

GO Term Gene Name
GO:0008982 IPR013011
GO:0009401 IPR013011

2 Ontology Annotations

GO Term Gene Name
GO:0008982 IPR013011
GO:0009401 IPR013011

1 Parent Features

DB identifier Type Name
IPR003501 Domain Phosphotransferase system, EIIB component, type 2/3

4 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Araha.11756s0242.1.p PAC:28856383 Arabidopsis halleri 564  
Pp3s30_50V3.1.p PAC:32948458 Physcomitrium patens 91  
Brdisv1pangenome1007266m.p PAC:33641287 Brachypodium distachyon Pangenome 970  
Brdisv1BdTR11A1042114m.p PAC:35688106 Brachypodium distachyon BdTR11a 970  

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            2197982
            8246840
            1537788
            7815935
            11361063
            12662934
            8784182
            9032081