Summary: PEP-utilising enzyme, N-terminal
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PEP-utilising enzyme, N-terminal Provide feedback
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This tab holds annotation information from the InterPro database.
InterPro entry IPR008731
This sequence identifies proteins which are a component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), a major carbohydrate active transport system. 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 [PUBMED:8246840]. This entry represents the N-terminal domain of enzyme I (EIN) which 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. The N-terminal domain of EI (EIN) extends from residues 1 to 259 and can be phosphorylated in a fully reversible manner by phosphorylated HPr. EIN, however, cannot be autophosphorylated by PEP [PUBMED:1655788, PUBMED:8031118].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||phosphoenolpyruvate-protein phosphotransferase activity (GO:0008965)|
|sugar:hydrogen symporter activity (GO:0005351)|
|Biological process||phosphoenolpyruvate-dependent sugar phosphotransferase system (GO:0009401)|
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Curation and family details
|Seed source:||Pfam-B_69291 (release 8.0)|
|Author:||Finn RD, Studholme DJ|
|Number in seed:||186|
|Number in full:||5872|
|Average length of the domain:||122.50 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||19.06 %|
|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:||8|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
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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 PEP-utilisers_N domain has been found. There are 22 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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