Phosphocarrier protein

Histidine-containing phosphocarrier protein (HPr) is a small cytoplasmic protein that is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS).[1][2]

Phosphotransferase system, phosphocarrier HPr protein
Phosphocarrier protein HPr, E. coli
Identifiers
SymbolPTS_HPr_protein
PfamPF00381
InterProIPR000032
PROSITEPDOC00318
SCOP21ptf / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1cm2​, 1cm3​, 1fu0​, 1ggr​, 1hdn​, 1j6t​, 1jem​, 1k1c​, 1ka5​, 1kkl​

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).[3][4] 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 most Gram-positive bacteria and certain Gram-negative bacteria, is phosphorylated by an ATP-dependent protein kinase, a process which probably plays a regulatory role in sugar transport.[5]

References
  1. Postma PW, Lengeler JW, Jacobson GR (1993). "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria". Microbiol. Rev. 57 (3): 543–594. doi:10.1128/MMBR.57.3.543-594.1993. PMC 372926. PMID 8246840.
  2. 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.
  3. 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.
  4. 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.
  5. Maurer T, Meier S, Kachel N, Munte CE, Hasenbein S, Koch B, Hengstenberg W, Kalbitzer HR (2004). "High-Resolution Structure of the Histidine-Containing Phosphocarrier Protein (HPr) from Staphylococcus aureus and Characterization of Its Interaction with the Bifunctional HPr Kinase/Phosphorylase". Journal of Bacteriology. 186 (17): 5906–5918. doi:10.1128/JB.186.17.5906-5918.2004. PMC 516805. PMID 15317796.
This article incorporates text from the public domain Pfam and InterPro: IPR000032
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