| Type |
Details |
Score |
| Publication |
| First Author: |
Meadow ND |
| Year: |
1990 |
| Journal: |
Annu Rev Biochem |
| Title: |
The bacterial phosphoenolpyruvate: glycose phosphotransferase system. |
| Volume: |
59 |
|
| Pages: |
497-542 |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
mutant strain, coisogenic, transgenic |
|
•
•
•
•
•
|
| GO Term |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains.The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range ofsugars, rather than being specific for just one or a few sugars.The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities.The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This group is specific for the IIC domain of the mannitol PTS transporters. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [, ]is a major carbohydrate transport system in bacteria. The PTS catalyzes thephosphorylation of incoming sugar substrates concomitant with theirtranslocation across the cell membrane. The general mechanism of the PTS isthe following: a phosphoryl group from phosphoenolpyruvate (PEP) istransferred to enzyme I (EI) of PTS which in turn transfers it to a phosphorylcarrier protein (HPr). Phospho-HPr then transfers thephosphoryl group to a sugar-specific permease which consists of at least threestructurally distinct domains (IIA, IIB, and IIC), []which can either be fused together in a single polypeptide chain or exist as two or threeinteractive chains, formerly called enzymes II (EII) and III (EIII).The first domain (IIA), carries the first permease-specificphosphorylation site, an histidine which is phosphorylated by phospho-HPr. Thesecond domain (IIB) is phosphorylated by phospho-IIA on acysteinyl or histidyl residue, depending on the sugar transported. Finally,the phosphoryl group is transferred from the IIB domain to the sugar substrateconcomitantly with the sugar uptake processed by the IIC domain. The IICdomain forms the translocation channel and the specific substrate-bindingsite. An additional transmembrane domain IID, homologous toIIC, can be found in some PTSs, e.g. for mannose [, , , , ].According to sequence analyses [, , , ], the PTS EIIC domain can be dividedin five groups.The PTS EIIC type 1 domain is found in the Glucose class of PTS and has anaverage length of about 80 amino acids.The PTS EIIC type 2 domain is found in the Mannitol class of PTS and has anaverage length of about 90 amino acids.The PTS EIIC type 3 domain is found in the Lactose class of PTS and has anaverage length of about 100 amino acids.The PTS EIIC type 4 domain is found in the Mannose class of PTS and has anaverage length of about 160 amino acids.The PTS EIIC type 5 domain is found in the Sorbitol class of PTS and has anaverage length of about 190 amino acids. |
|
•
•
•
•
•
|
| Allele |
| Name: |
transgene insertion 6, Chiho Sumi-Ichinose |
| Allele Type: |
Transgenic |
| Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rogers MJ |
| Year: |
1988 |
| Journal: |
Gene |
| Title: |
Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. |
| Volume: |
62 |
| Issue: |
2 |
| Pages: |
197-207 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Luesink EJ |
| Year: |
1999 |
| Journal: |
J Bacteriol |
| Title: |
Molecular characterization of the Lactococcus lactis ptsHI operon and analysis of the regulatory role of HPr. |
| Volume: |
181 |
| Issue: |
3 |
| Pages: |
764-71 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active-transport system, catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.This family includes the IIC component of the ascorbate-specific PTS system, UlaA, []and the IIC component of the galactitol-specific PTS system. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active-transport system, catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane.This family represents the IIC component of the PTS galactitol-specific family. Gat family PTS systems typically have 3 components: IIA, IIB and IIC []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents phosphoenolpyruvate-protein phosphotransferase, also known as PTS enzyme I, which is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS).PTS catalyses the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. PTS enzyme I transfers the phosphoryl group from phosphoenolpyruvate to the phosphoryl carrier protein HPr []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the combined B and C domains of the PTS transport system enzyme II specific for N-acetylglucosamine transport []. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name 'PTS system, N-acetylglucosamine-specific IIABC component'. This family is most closely related to the glucose-specific PTS enzymes. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| 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 sequence analyses [, , ], the PTS EIIC domain can be divided in five groups:The PTS EIIC type 1 domain is found in the Glucose class of PTS and has an average length of about 80 amino acids. The PTS EIIC type 2 domain is found in the Mannitol class of PTS and has an average length of about 90 amino acids.The PTS EIIC type 3 domain is found in the Lactose class of PTS and has an average length of about 100 amino acids. The PTS EIIC type 4 domain is found in the Mannose class of PTS and has an average length of about 160 amino acids. The PTS EIIC type 5 domain is found in the Sorbitol class of PTS and has an average length of about 190 amino acids. This entry represents the type 1 domain. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| 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 sequence analyses [, , ], the PTS EIIC domain can be divided in five groups:The PTS EIIC type 1 domain is found in the Glucose class of PTS and has an average length of about 80 amino acids. The PTS EIIC type 2 domain is found in the Mannitol class of PTS and has an average length of about 90 amino acids.The PTS EIIC type 3 domain is found in the Lactose class of PTS and has an average length of about 100 amino acids. The PTS EIIC type 4 domain is found in the Mannose class of PTS and has an average length of about 160 amino acids. The PTS EIIC type 5 domain is found in the Sorbitol class of PTS and has an average length of about 190 amino acids. This entry represents the type 2 domain. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Mannose (Man) family is unique in several respects among PTS permease families [].It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The mannose permease of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. This entry represents the IIC subunits of this family of PTS transporters. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The mannose permease of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this family can transport sorbose, fructose and N-acetylglucosamine. This domain is specific for the IIA component of the PTS mannose family []. |
|
•
•
•
•
•
|
| GO Term |
|
•
•
•
•
•
|
| Strain |
| Attribute String: |
mutant strain, coisogenic, transgenic |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains []. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The mannose permease of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. The active site histidine receives a phosphate group from the IIA subunit and transfers it to the substrate []. This entry is specific for the IIB components of this family of PTS transporters []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains []. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The mannose permease of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. The active site histidine receives a phosphate group from the IIA subunit and transfers it to the substrate []. This entry is specific for the IIB components of this family of PTS transporters []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The Gut family consists only of glucitol-specific permeases, but these occur both in Gram-negative and Gram-positive bacteria. Escherichia coli consists of IIA protein, a IIC protein and a IIBC protein.This family is specific for the IIBC component. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains.The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The Gut family consists only of glucitol-specific transporters, but these occur both in Gram-negative and Gram-positive bacteria. Escherichia coli consists of IIA protein, a IIC protein and a IIBC protein. This family is specific for the IIC component. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The Gut family consists only of glucitol-specific permeases, but these occur both in Gram-negative and Gram-positive bacteria. Escherichia coli consists of IIA protein, a IIC protein and a IIBC protein.This entry represents the N-terminal conserved region of the IIBC component. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| 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 [, , , ]. The Man family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The PTS Fructose-Mannitol (Fru) family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This family is specific for the IIA domain of the fructose PTS transporters. Alsosimilar to the Enzyme IIA Fru subunits of the PTS is Enzyme IIA Ntr (nitrogen) found in Escherichia coli and other organisms, which may play a solely regulatory role. |
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•
•
•
•
•
|
| Publication |
| First Author: |
Barabote RD |
| Year: |
2005 |
| Journal: |
Microbiol Mol Biol Rev |
| Title: |
Comparative genomic analyses of the bacterial phosphotransferase system. |
| Volume: |
69 |
| Issue: |
4 |
| Pages: |
608-34 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
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 alpha- and beta-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) beta-glucoside PTS permease is in the Lac family.Several of the Escherichia 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 entry is specific for the IIC domain of this type of Glc family PTS transporters. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [, ]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) []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.Several PTS permease families are currently recognised, namely, the (i) glucose (including glucoside), (ii) fructose (including mannitol), (iii) lactose (including N,N-diacetylchitobiose), (iv) galactitol, (v) glucitol, (vi) mannose, and (vii) l-ascorbate families [].This entry represents the component IIB of the glucose family of PTS systems (type 1). The structure of this domain has a homing endonuclease-like fold, which is composed of an α-β(2)-α-β(2)-alpha fold arranged into two layers (alpha/beta) with antiparallel sheet. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
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 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) []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). IIB () is is phosphorylated by phospho-IIA, before the phosphoryl group is transferred to the sugar substrate.Several PTS permease families are currently recognised, namely, the (i) glucose (including glucoside), (ii) fructose (including mannitol), (iii) lactose (including N,N-diacetylchitobiose), (iv) galactitol, (v) glucitol, (vi) mannose, and (vii) l-ascorbate families [].This entry represents the component EIIB of fructose-specific PTS systems. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [, ]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) []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.Several PTS permease families are currently recognised, namely, the (i) glucose (including glucoside), (ii) fructose (including mannitol), (iii) lactose (including N,N-diacetylchitobiose), (iv) galactitol, (v) glucitol, (vi) mannose, and (vii) l-ascorbate families [].This entry represents the component IIB of the glucose family of PTS systems (type 1). |
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•
•
•
•
•
|
| Strain |
| Attribute String: |
congenic, targeted mutation, transgenic |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Pts/Pts Tg(DBH-PTS)6Csic/? |
| Background: |
B6.Cg-Pts Tg(DBH-PTS)6Csic |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Pts/Pts Tg(DBH-PTS)6Csic/? |
| Background: |
involves: 129X1/SvJ * C57BL/6J |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Postma PW |
| Year: |
1986 |
| Journal: |
J Bacteriol |
| Title: |
Transport of trehalose in Salmonella typhimurium. |
| Volume: |
168 |
| Issue: |
3 |
| Pages: |
1107-11 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jensen JB |
| Year: |
2002 |
| Journal: |
J Bacteriol |
| Title: |
Redundancy in periplasmic binding protein-dependent transport systems for trehalose, sucrose, and maltose in Sinorhizobium meliloti. |
| Volume: |
184 |
| Issue: |
11 |
| Pages: |
2978-86 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Elferink MG |
| Year: |
2001 |
| Journal: |
Mol Microbiol |
| Title: |
Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. |
| Volume: |
39 |
| Issue: |
6 |
| Pages: |
1494-503 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Andersson U |
| Year: |
2001 |
| Journal: |
J Biol Chem |
| Title: |
Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. |
| Volume: |
276 |
| Issue: |
46 |
| Pages: |
42707-13 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schiefner A |
| Year: |
2002 |
| Journal: |
Acta Crystallogr D Biol Crystallogr |
| Title: |
Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis. |
| Volume: |
58 |
| Issue: |
Pt 12 |
| Pages: |
2147-9 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
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 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) []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 IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.PTS systems commonly occur in bacteria. An archaeal version has also been discovered []. This entry identifies both the bacterial family members and archaeal homologues. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the fused enzyme II B and C components of the trehalose-specific PTS sugar transporter system []. 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) []. 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 described by the IIB component and the IIC component (), respectively. In Escherichia coli, Bacillus subtilis and Pseudomonas 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 [], or (in Sinorhizobium, Thermococcus and Sulfolobus, for instance) by ABC transporters [, , ]. |
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| Publication |
| First Author: |
Legler PM |
| Year: |
2004 |
| Journal: |
J Biol Chem |
| Title: |
Three-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter IImannitol of the Escherichia coli phosphotransferase system. |
| Volume: |
279 |
| Issue: |
37 |
| Pages: |
39115-21 |
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•
|
| Publication |
| First Author: |
van Montfort BA |
| Year: |
2001 |
| Journal: |
J Biol Chem |
| Title: |
Cysteine cross-linking defines part of the dimer and B/C domain interface of the Escherichia coli mannitol permease. |
| Volume: |
276 |
| Issue: |
16 |
| Pages: |
12756-63 |
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| Publication |
| First Author: |
Jacobson GR |
| Year: |
1993 |
| Journal: |
J Bioenerg Biomembr |
| Title: |
The Escherichia coli mannitol permease as a model for transport via the bacterial phosphotransferase system. |
| Volume: |
25 |
| Issue: |
6 |
| Pages: |
621-6 |
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•
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| Protein Domain |
| Type: |
Domain |
| Description: |
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 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) []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). IIB () is is phosphorylated by phospho-IIA, before the phosphoryl group is transferred to the sugar substrate.Several PTS permease families are currently recognised, namely, the (i) glucose (including glucoside), (ii) fructose (including mannitol), (iii) lactose (including N,N-diacetylchitobiose), (iv) galactitol, (v) glucitol, (vi) mannose, and (vii) l-ascorbate families [].The IIA, IIB, and IIC domains are expressed from the mtlA gene as a single protein, also known as the mannitol PTS permease, the mtl transporter, or MtlA. MtlA is only functional as a dimer with the dimer contacts occuring between the IIC domains []. MtlA takes up exogenous mannitol releasing the phosphate ester into the cytoplasm in preparation for oxidation to fructose-6-phosphate by the NAD-dependent mannitol-P dehydrogenase (MtlD) []. The IIB domain fold includes a central four-stranded parallel open twisted β-sheet flanked by α-helices on both sides [, ]. This entry represents the component EIIB of mannitol-specific PTS systems. |
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| Publication |
| First Author: |
Campos E |
| Year: |
2004 |
| Journal: |
J Bacteriol |
| Title: |
Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in LaAscorbate dissimilation in Escherichia coli. |
| Volume: |
186 |
| Issue: |
6 |
| Pages: |
1720-8 |
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| Protein Domain |
| Type: |
Family |
| 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 [, , , ]. Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Mannose (Man) family is unique in several respects among PTS permease families.It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The mannose permease of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine,N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. This family is specific for the IID subunits of this family of PTS transporters. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents a group of fused B and C components of PTS enzyme II. This clade is a member of a larger family which contains enzyme II's specific for a variety of sugars including glucose () and N-acetylglucosamine (). None of the members of this clade have been experimentally characterised. This clade includes sequences from Streptococcus and Enterococcus which also include a C-terminal A domain as well as Bacillus and Clostridium which do not. In nearly all cases, these species also contain an authentic glucose-specific PTS transporter. |
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| Publication |
| First Author: |
Orriss GL |
| Year: |
2003 |
| Journal: |
J Mol Biol |
| Title: |
Crystal structure of the IIB(Sor) domain of the sorbose permease from Klebsiella pneumoniae solved to 1.75A resolution. |
| Volume: |
327 |
| Issue: |
5 |
| Pages: |
1111-9 |
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•
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| Publication |
| First Author: |
Thompson J |
| Year: |
2001 |
| Journal: |
J Biol Chem |
| Title: |
Metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae. Participation and properties of sucrose-6-phosphate hydrolase and phospho-alpha-glucosidase. |
| Volume: |
276 |
| Issue: |
40 |
| Pages: |
37415-25 |
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•
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| Publication |
| First Author: |
Pikis A |
| Year: |
2002 |
| Journal: |
Microbiology |
| Title: |
Metabolism of sucrose and its five isomers by Fusobacterium mortiferum. |
| Volume: |
148 |
| Issue: |
Pt 3 |
| Pages: |
843-52 |
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•
|
| Publication |
| First Author: |
Tangney M |
| Year: |
2001 |
| Journal: |
J Ind Microbiol Biotechnol |
| Title: |
Characterization of a maltose transport system in Clostridium acetobutylicum ATCC 824. |
| Volume: |
27 |
| Issue: |
5 |
| Pages: |
298-306 |
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•
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains []. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.The mannose permease of Escherichia coli, for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and other sugars. Other members of this can transport sorbose, fructose and N-acetylglucosamine. The active site histidine receives a phosphate group from the IIA subunit and transfers it to the substrate []. This entry represents the IIB components of this family of PTS transporters []. The structure of this component has three layers (alpha/beta/alpha) with parallel β-sheet of six strands. |
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| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents the fused PTS enzyme II B and C domains. A gene from Clostridium []has been partially characterised as a maltose transporter, while genes from Fusobacterium and Klebsiella [, ]have been proposed to transport the five non-standard isomers of sucrose. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
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 lactose/cellobiose-specific family are one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes. The fold of IIB cellobiose shows similarstructure to mammalian tyrosine phosphatases. This signature is often found downstream of . |
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| Publication |
| First Author: |
Le Coq D |
| Year: |
1995 |
| Journal: |
J Bacteriol |
| Title: |
New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog. |
| Volume: |
177 |
| Issue: |
6 |
| Pages: |
1527-35 |
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•
•
•
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| Protein Domain |
| Type: |
Family |
| 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 [, , , ]. This entry 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) []. These are distinct from the closely related sucrose-specific and trehalose-specific PTS transporters. |
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| Publication |
| First Author: |
Eberstadt M |
| Year: |
1996 |
| Journal: |
Biochemistry |
| Title: |
Solution structure of the IIB domain of the glucose transporter of Escherichia coli. |
| Volume: |
35 |
| Issue: |
35 |
| Pages: |
11286-92 |
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| Publication |
| First Author: |
van Montfort RL |
| Year: |
1997 |
| Journal: |
Structure |
| Title: |
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. |
| Volume: |
5 |
| Issue: |
2 |
| Pages: |
217-25 |
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| HT Experiment |
| Series Id: |
GSE24775 |
| Experiment Type: |
transcription profiling by array |
| Study Type: |
Baseline |
| Source: |
ArrayExpress |
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•
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| Protein Domain |
| Type: |
Domain |
| 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-α-β 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 α-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. The EIIB type 3 domain is often found downstream of the EIIC type 3 domain. |
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| Protein Domain |
| Type: |
Family |
| 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 [, , , ]. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.This family consists only of glucitol-specific transporters, and occur both in Gram-negative and Gram-positive bacteria. The system in Escherichia coli consists of a IIA protein, and a IIBC protein. This family is specific for the IIA component. |
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| Protein Domain |
| Type: |
Family |
| 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 [, , , ]. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.This family consists only of glucitol-specific transporters, and occur both in Gram-negative and Gram-positive bacteria. The system in Escherichia coli consists of a IIA protein, and a IIBC protein. This family is specific for the IIA component. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| 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 [, , , ]. The Man family is unique in several respects among PTS permease families:It is the only PTS family in which members possess a IID protein.It is the only PTS family in which the IIB constituent is phosphorylated on a histidyl rather than a cysteyl residue.Its permease members exhibit broad specificity for a range of sugars, rather than being specific for just one or a few sugars.This entry consists only of glucitol-specific transporters, and occur both in Gram-negative and Gram-positive bacteria. The system in Escherichia coli consists of a IIA protein, and a IIBC protein. This superfamily represents specifically the IIA component. The structure of this component is composed of a close barrel fold with mixed sheet; it has two overside connections and consists of two intertwinned structural repeats. |
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| Publication |
| First Author: |
Cases I |
| Year: |
2001 |
| Journal: |
J Bacteriol |
| Title: |
Evidence of multiple regulatory functions for the PtsN (IIA(Ntr)) protein of Pseudomonas putida. |
| Volume: |
183 |
| Issue: |
3 |
| Pages: |
1032-7 |
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•
•
|
| Publication |
| First Author: |
Michiels J |
| Year: |
1998 |
| Journal: |
J Bacteriol |
| Title: |
The Rhizobium etli rpoN locus: DNA sequence analysis and phenotypical characterization of rpoN, ptsN, and ptsA mutants. |
| Volume: |
180 |
| Issue: |
7 |
| Pages: |
1729-40 |
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•
•
•
|
| Publication |
| First Author: |
Tangney M |
| Year: |
2000 |
| Journal: |
J Mol Microbiol Biotechnol |
| Title: |
Analysis of a catabolic operon for sucrose transport and metabolism in Clostridium acetobutylicum ATCC 824. |
| Volume: |
2 |
| Issue: |
1 |
| Pages: |
71-80 |
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•
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| Protein Domain |
| Type: |
Domain |
| Description: |
Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATPas phosphoryl donor and is designated . By contrast, Escherichia coli and many other bacterial species have a multisubunit form () with a phosphoprotein donor related to PTS transport proteins. This entry represents the ADP-binding subunit of the PTS-dependent dihydroxyacetone kinase []. |
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•
•
•
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| Protein Domain |
| Type: |
Domain |
| 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 EIIA domain can be divided in different groups. The mannose class of EIIA consists of a single five-stranded mixed beta sheet, flanked by helices on both sides []. The phosphorylation site (His) is located at the end of the third beta strand, in a shallow crevice lined with hydrophobic residues.This entry represents the mannose-type EIIA domain. This type of domain can also be found in the multidomain protein dihydroxyacetone kinase DhaM from some bacteria [, ]. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| 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 [, , , ]. The lactose/cellobiose-specific superfamily are one of four structurally and functionally distinct group IIA PTS system enzymes. This superfamily of proteins normally function as a homotrimer, stabilised bya centrally located metal ion []. Separation into subunits is thought to occur after phosphorylation. It has a spectrin repeat-like fold which consists of three helices arranged in a close bundle with left-handed twist going up-and-down. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| 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 EIIA domain can be divided in different groups. The mannose class of EIIA consists of a single five-stranded mixed beta sheet, flanked by helices on both sides []. The phosphorylation site (His) is located at the end of the third beta strand, in a shallow crevice lined with hydrophobic residues.This entry represents the mannose-type EIIA domain superfamily. This type of domain can also be found in the multidomain protein dihydroxyacetone kinase DhaM from some bacteria [, ]. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the fused enzyme II B and C components of the sucrose-specific PTS sugar transporter system []. Sucrose is converted to sucrose-6-phosphate in the process of translocation into the cell. Some of these transporters lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). The exceptions to this rule are Staphylococci, Streptococci, Lactococci, Lactobacilli, etc. which contain their own A domain as a C-terminal fusion. |
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| Protein Domain |
| Type: |
Family |
| 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 [, , , ]. The lactose/cellobiose-specific family are one of four structurally and functionally distinct group IIA PTS system enzymes. This family of proteins normally function as a homotrimer, stabilised by a centrally located metal ion []. Separation into subunits is thought to occur after phosphorylation. |
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| Protein Domain |
| Type: |
Family |
| 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 [, , , ]. These sequences, which are about 160 residues in length, are closely related to the fructose-specific phosphotransferase (PTS) system IIA component. It is a regulatory protein found only in species with a phosphoenolpyruvate-protein phosphotransferase (enzyme I of PTS systems) and an HPr-like phosphocarrier protein, but not all species have a IIC-like permease. Members of this family are found in Proteobacteria, Chlamydia, and the spirochete Treponema pallidum [, ]. |
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| Protein Domain |
| Type: |
PTM |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyzes thephosphorylation of incoming sugar substrates concomitant with theirtranslocation across the cell membrane. The general mechanism of the PTS isas follows: a phosphoryl group from phosphoenolpyruvate (PEP) is transferredto Enzyme I (EI) of the PTS which in turn transfers it to a phosphoryl carrierprotein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease complex (enzymes EII/EIII).HPr is a small cytoplasmic protein, which in some bacteria is found as a domain in a larger protein that includes a EIII(Fru)(IIA) domain and in some cases also a EI domain . HPr is acomponent of the phosphoenolpyruvate-dependent sugar phosphotransferasesystem (PTS) major carbohydrate transport system in bacteria [, ].There is a conserved histidine in the N terminus of HPr , which serves as an acceptor forthe phosphoryl group of EI. In the central part of HPr there is a conserved serine, which in Gram-positive bacteria only, is phosphorylated by anATP-dependent protein kinase; a process which probably plays a regulatory role in sugartransport.The sequence around both phosphorylation sites are well conserved and can be used as signature patterns for HPr proteins or domains. This signature identifies the serine phosporylation site. |
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| Protein Domain |
| Type: |
PTM |
| 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 concomitant with their translocation across the cell membrane. The general mechanism of the PTS is as follows: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to Enzyme I (EI) of the PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease complex (enzymes EII/EIII).HPr is a small cytoplasmic protein, which in some bacteria is found as a domain in a larger protein that includes a EIII(Fru)(IIA) domain and in some cases also a EI domain . HPr is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) major carbohydrate transport system in bacteria [, ].There is a conserved histidine in the N terminus of HPr which serves as an acceptor for the phosphoryl group of EI. In the central part of HPr there is a conserved serine, which in Gram-positive bacteria only, is phosphorylated by anATP-dependent protein kinase; a process which probably plays a regulatory role in sugar transport ().The sequence around both phosphorylation sites are well conserved and can be used as signature patterns for HPr proteins or domains. This signature identifies the histidine phosphorulation site. |
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| Protein Domain |
| Type: |
Domain |
| 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 [, , , ]. |
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| Protein Domain |
| Type: |
Conserved_site |
| Description: |
A number of enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown to be structurally related [, , , ]. These enzymes are: Pyruvate,orthophosphate dikinase () (PPDK). PPDK catalyzes the reversible phosphorylation of pyruvate and phosphate by ATP to PEP and diphosphate. In plants PPDK function in the direction of the formation of PEP, which is the primary acceptor of carbon dioxide in C4 and crassulacean acid metabolism plants. In some bacteria, such as Bacteroides symbiosus, PPDK functions in the direction of ATP synthesis. Phosphoenolpyruvate synthase () (pyruvate,water dikinase). This enzyme catalyzes the reversible phosphorylation of pyruvate by ATP to form PEP, AMP and phosphate, an essential step in gluconeogenesis when pyruvate and lactate are used as a carbon source. Phosphoenolpyruvate-protein phosphatase (). This is the first enzyme of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), 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 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. The entry signature pattern represents a conserved region in the C-terminal part of the PEP-utilizing enzymes. The biological significance of this region is not yet known. |
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| Protein Domain |
| Type: |
Conserved_site |
| Description: |
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [, ]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) []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. |
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| Publication |
| First Author: |
Ofman R |
| Year: |
2006 |
| Journal: |
Biochem J |
| Title: |
Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity. |
| Volume: |
393 |
| Issue: |
Pt 2 |
| Pages: |
537-43 |
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| Publication |
| First Author: |
Buse M |
| Year: |
2024 |
| Journal: |
iScience |
| Title: |
Lineage tracing reveals transient phenotypic adaptation of tubular cells during acute kidney injury. |
| Volume: |
27 |
| Issue: |
3 |
| Pages: |
109255 |
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| Publication |
| First Author: |
Muraoka H |
| Year: |
2019 |
| Journal: |
Cell Rep |
| Title: |
Role of Nampt-Sirt6 Axis in Renal Proximal Tubules in Extracellular Matrix Deposition in Diabetic Nephropathy. |
| Volume: |
27 |
| Issue: |
1 |
| Pages: |
199-212.e5 |
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| Publication |
| First Author: |
Recktenwald CV |
| Year: |
2024 |
| Journal: |
Cell Rep |
| Title: |
The structure of the second CysD domain of MUC2 and role in mucin organization by transglutaminase-based cross-linking. |
| Volume: |
43 |
| Issue: |
5 |
| Pages: |
114207 |
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| Publication |
| First Author: |
Li HS |
| Year: |
1993 |
| Journal: |
Audiology |
| Title: |
Influence of age on noise-induced permanent threshold shifts in CBA/Ca and C57BL/6J mice. |
| Volume: |
32 |
| Issue: |
3 |
| Pages: |
195-204 |
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| Protein Domain |
| Type: |
Domain |
| 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-α-β 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 α-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. |
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| Publication |
| First Author: |
Niersbach M |
| Year: |
1992 |
| Journal: |
Mol Gen Genet |
| Title: |
Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase. |
| Volume: |
231 |
| Issue: |
2 |
| Pages: |
332-6 |
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| Protein Domain |
| Type: |
Active_site |
| Description: |
A number of enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via a phospho-histidine intermediate have been shown to be structurally related [, , , ]. These enzymes are: Pyruvate,orthophosphate dikinase () (PPDK). PPDK catalyzes the reversible phosphorylation of pyruvate and phosphate by ATP to PEP and diphosphate. In plants PPDK function in the direction of the formation of PEP, which is the primary acceptor of carbon dioxide in C4 and crassulacean acid metabolism plants. In some bacteria, such as Bacteroides symbiosus, PPDK functions in the direction of ATP synthesis. Phosphoenolpyruvate synthase () (pyruvate,water dikinase). This enzyme catalyzes the reversible phosphorylation of pyruvate by ATP to form PEP, AMP and phosphate, an essential step in gluconeogenesis when pyruvate and lactate are used as a carbon source. Phosphoenolpyruvate-protein phosphatase (). This is the first enzyme of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), 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 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. All these enzymes share the same catalytic mechanism: they bind PEP and transfer the phosphoryl group from it to a histidine residue. The sequence around that residue is highly conserved and can be used as a signature pattern for these enzymes. The signature pattern for this entry contains the phosphorylated histidine residue. |
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| Publication |
| First Author: |
Honeyman AL |
| Year: |
1992 |
| Journal: |
Infect Immun |
| Title: |
Isolation, characterization, and nucleotide sequence of the Streptococcus mutans mannitol-phosphate dehydrogenase gene and the mannitol-specific factor III gene of the phosphoenolpyruvate phosphotransferase system. |
| Volume: |
60 |
| Issue: |
8 |
| Pages: |
3369-75 |
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| Publication |
| First Author: |
Houman F |
| Year: |
1990 |
| Journal: |
Cell |
| Title: |
Transcriptional antitermination in the bgl operon of E. coli is modulated by a specific RNA binding protein. |
| Volume: |
62 |
| Issue: |
6 |
| Pages: |
1153-63 |
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| Publication |
| First Author: |
Amster-Choder O |
| Year: |
1990 |
| Journal: |
Science |
| Title: |
Regulation of activity of a transcriptional anti-terminator in E. coli by phosphorylation in vivo. |
| Volume: |
249 |
| Issue: |
4968 |
| Pages: |
540-2 |
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| Publication |
| First Author: |
Pickl A |
| Year: |
2012 |
| Journal: |
J Bacteriol |
| Title: |
Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase. |
| Volume: |
194 |
| Issue: |
12 |
| Pages: |
3088-97 |
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| Publication |
| First Author: |
Gutknecht R |
| Year: |
2001 |
| Journal: |
EMBO J |
| Title: |
The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. |
| Volume: |
20 |
| Issue: |
10 |
| Pages: |
2480-6 |
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| Publication |
| First Author: |
Fischer R |
| Year: |
1991 |
| Journal: |
J Bacteriol |
| Title: |
Mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Enterococcus faecalis: molecular cloning and nucleotide sequences of the enzyme IIIMtl gene and the mannitol-1-phosphate dehydrogenase gene, expression in Escherichia coli, and comparison of the gene products with similar enzymes. |
| Volume: |
173 |
| Issue: |
12 |
| Pages: |
3709-15 |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This RNA binding domain is found at the amino terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram-positive and Gram-negative bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer []to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin []. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template []. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
This superfamily describes a domain that can be found in the N terminus of PtsI, a component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). The PTS system is found throughout the bacterial kingdom, and is responsible for the coupled phosphorylation and translocation of numerous sugars across the cytoplasmic membrane []. PtsI transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) which in turn phosphorylates a group of membrane-associated proteins, known as enzyme II [, ].This region contains a SAM domain-like fold. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Mannitol dehydrogenases catalyse the NAD-dependent reduction of mannitol-1-phosphates as part of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates the vectorial translocation of metabolisable carbohydrates to form the corresponding sugar phosphates, which are then converted to glycolytic intermediates []. Mannitol 2-dehydrogenase catalyses the NAD-dependent reduction of mannitol to fructose [].Several dehydrogenases have been shown []to be evolutionary related, including mannitol-1-phosphate 5-dehydrogenase () (gene mtlD), mannitol 2-dehydrogenase () (gene mtlK); mannonate oxidoreductase () (fructuronate reductase) (gene uxuB); Escherichia coli hypothetical proteins ydfI and yeiQ; and yeast hypothetical protein YEL070w. |
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| Protein Domain |
| Type: |
Family |
| Description: |
Mannitol dehydrogenases catalyse the NAD-dependent reduction of mannitol-1-phosphates as part of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates the vectorial translocation of metabolisable carbohydrates to form the corresponding sugar phosphates, which are then converted to glycolytic intermediates []. Mannitol 2-dehydrogenase catalyses the NAD-dependent reduction of mannitol to fructose [].Several dehydrogenases have been shown []to be evolutionary related, including mannitol-1-phosphate 5-dehydrogenase () (gene mtlD), mannitol 2-dehydrogenase () (gene mtlK); mannonate oxidoreductase () (fructuronate reductase) (gene uxuB); Escherichia coli hypothetical proteins ydfI and yeiQ; and yeast hypothetical protein YEL070w.This entry represents the mannitol-1-phosphate 5-dehydrogenase family, which catalyses the reactionD-mannitol-1-phosphate + NAD+=>beta-D-fructose-6-phosphate + H++ NADH |
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| Protein Domain |
| Type: |
Conserved_site |
| Description: |
Adenylate cyclase is the enzyme responsible for the synthesis of cAMP from ATP. From sequence data, it has been proposed that there are three different classes of adenylate cyclases [, ]. Class I cyclases are found in enterobacteria and related Gram-negative bacteria. They are proteins of about 850 residues that consist of two functional domains: a N-terminal catalytic domain and a C-terminal regulatory domain.There are two highly conserved regions, the first one is located in the catalytic domain and the second one in the regulatory domain. The second signature includes a conserved histidine which could be phosphorylated by a PTS system IIA enzyme, thus leading to the activation of the cyclase. |
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| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
This RNA binding domain is found at the N terminus of transcriptional antitermination proteins such as BglG, SacY and LicT. These proteins control the expression of sugar metabolising operons in Gram-positive and Gram-negative bacteria. This domain has been called the CAT (Co-AntiTerminator) domain. It binds as a dimer []to short Ribonucleotidic Anti-Terminator (RAT) hairpin, each monomer interacting symmetrically with both strands of the RAT hairpin []. In the full-length protein, CAT is followed by two phosphorylatable PTS regulation domains that modulate the RNA binding activity of CAT. Upon activation, the dimeric proteins bind to RAT targets in the nascent mRNA, thereby preventing abortive dissociation of the RNA polymerase from the DNA template []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry represents the IIC component, or IIC region of a IIABC or IIBC polypeptide of a phosphotransferase system for carbohydrate transport. Members of this family belong to the fructose-specific subfamily of the broader family of PTS EIIC proteins. Members should be found as part of the same chain or in the same operon as fructose family IIA () and IIB () protein regions. A numberof bacterial species have members in two different branches of this subfamily, suggesting some diversity in substrate specificity of its members.PTS systems commonly occur in bacteria. An archaeal version has also been discovered []. This entry identifies both the bacterial family members and archaeal homologues. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
Mannitol-1-phosphate 5-dehydrogenase catalyses the NAD-dependent reduction of mannitol-1-phosphate to fructose-6-phosphate []as part of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates the vectorial translocation of metabolisable carbohydrates to formthe corresponding sugar phosphates, which are then converted to glycolytic intermediates []. Mannitol 2-dehydrogenase catalyses the NAD-dependent reduction of mannitol tofructose [].Several dehydrogenases have been shown []to be evolutionary related, including mannitol-1-phosphate 5-dehydrogenase () (gene mtlD), mannitol 2-dehydrogenase () (gene mtlK); mannonate oxidoreductase () (fructuronate reductase) (gene uxuB); Escherichia coli hypothetical proteins ydfI and yeiQ; and yeast hypothetical protein YEL070w. This domain has a Rossmann-type fold. |
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| Protein Domain |
| Type: |
Conserved_site |
| Description: |
Mannitol dehydrogenases catalyse the NAD-dependent reduction of mannitol-1-phosphates as part of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The PTS facilitates the vectorial translocation of metabolisable carbohydrates to form the corresponding sugar phosphates, which are then converted to glycolytic intermediates []. Mannitol 2-dehydrogenase catalyses the NAD-dependent reduction of mannitol to fructose [].Several dehydrogenases have been shown []to be evolutionary related, including mannitol-1-phosphate 5-dehydrogenase () (gene mtlD), mannitol 2-dehydrogenase () (gene mtlK); mannonate oxidoreductase () (fructuronate reductase) (gene uxuB); Escherichia coli hypothetical proteins ydfI and yeiQ; and yeast hypothetical protein YEL070w.This entry represents a conserved site found in mannitol dehydrogenases. |
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