Summary: phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1
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phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1 Provide feedback
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Internal database links
|SCOOP:||DUF1154 Peptidase_M23 QRPTase_N|
|Similarity to PfamA using HHSearch:||Peptidase_M23 Biotin_lipoyl_2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001127
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [PUBMED:8246840, PUBMED:2197982] 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 [PUBMED:1537788]. 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.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||membrane (GO:0016020)|
|Molecular function||sugar:hydrogen symporter activity (GO:0005351)|
|Biological process||transport (GO:0006810)|
|phosphoenolpyruvate-dependent sugar phosphotransferase system (GO:0009401)|
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This superfamily contains proteins with a hybrid motif . This motif is embedded in structurally diverse proteins.
The clan contains the following 17 members:Apocytochr_F_C Biotin_lipoyl Biotin_lipoyl_2 Complex1_51K DUF2118 DUF2254 GCV_H HlyD HlyD_2 HlyD_3 NQRA OEP Peptidase_M23 PTS_EIIA_1 PYNP_C QRPTase_N RnfC_N
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Curation and family details
|Number in seed:||14|
|Number in full:||7674|
|Average length of the domain:||132.00 aa|
|Average identity of full alignment:||41 %|
|Average coverage of the sequence by the domain:||27.04 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PTS_EIIA_1 domain has been found. There are 18 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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