Summary: PTS HPr component phosphorylation site
This is the Wikipedia entry entitled "Phosphocarrier protein". More...
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Phosphocarrier protein Edit Wikipedia article
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|Phosphotransferase system, phosphocarrier HPr protein|
Structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis.
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The mechanism involves the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) via enzyme I (EI) to enzyme II (EII) of the PTS system, which in turn transfers it to a phosphocarrier protein (HPr). In some bacteria HPr is a domain in a larger protein that includes an EIII(Fru) (IIA) domain and in some cases also an EI domain.
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 an ATP-dependent protein kinase, a process which probably plays a regulatory role in sugar transport.
- Jia Z, Vandonselaar M, Hengstenberg W, Quail JW, Delbaere LT (March 1994). "The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis". J. Mol. Biol. 236 (5): 1341–55. doi:10.1016/0022-2836(94)90062-0. PMID 8126724.
- Postma PW, Lengeler JW, Jacobson GR (1993). "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria". Microbiol. Rev. 57 (3): 543–594. PMC 372926. PMID 8246840.
- Meadow ND, Fox DK, Roseman S (1990). "The bacterial phosphoenolpyruvate: glycose phosphotransferase system". Annu. Rev. Biochem. 59 (1): 497–542. doi:10.1146/annurev.bi.59.070190.002433. PMID 2197982.
- Boelens R, Scheek RM, Robillard GT, van Nuland NA (1995). "High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data". J. Mol. Biol. 246 (1): 180–193. doi:10.1006/jmbi.1994.0075. PMID 7853396.
- Liao DI, Herzberg O (1994). "Refined structures of the active Ser83→Cys and impaired Ser46→Asp histidine-containing phosphocarrier proteins". Structure 2 (12): 1203–1216. doi:10.1016/S0969-2126(94)00122-7. PMID 7704530.
PTS HPr component phosphorylation site Provide feedback
No Pfam abstract.
Jia Z, Quail JW, Waygood EB, Delbaere LT; , J Biol Chem 1993;268:22490-22501.: The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination. PUBMED:8226757 EPMC:8226757
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005698
The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species [PUBMED:8246840, PUBMED:2197982]. 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 the phosphoryl carrier protein (HPr) [PUBMED:7853396, PUBMED:7704530]. Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease complex (enzymes EII/EIII).
HPr [PUBMED:1549615, PUBMED:7686067] is a small cytoplasmic protein of 70 to 90 amino acid residues. In some bacteria, HPr is a domain in a larger protein that includes a EIII(Fru) (IIA) domain and in some cases also the EI domain. A conserved histidine in the N-terminal section of HPr 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 an ATP-dependent protein kinase; a process which probably play a regulatory role in sugar transport. The overall architecture of the HPr domain has been described as an open faced beta-sandwich in which a beta-sheet is packed against three alpha-helices. Regulatory phosphorylation at the conserved Ser residue does not appear to induce large structural changes to the HPr domain, in particular in the region of the active site [PUBMED:11054290, PUBMED:15713472].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||sugar:hydrogen symporter activity (GO:0005351)|
|Biological process||phosphoenolpyruvate-dependent sugar phosphotransferase system (GO:0009401)|
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Curation and family details
|Author:||Finn RD, Griffiths-Jones SR|
|Number in seed:||168|
|Number in full:||8181|
|Average length of the domain:||83.30 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||35.45 %|
|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:||14|
|Download:||download the raw HMM for this family|
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There are 6 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 PTS-HPr domain has been found. There are 89 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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