Phosphocarrier protein

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1cm2, 1cm3, 1fu0, 1ggr, 1hdn, 1j6t, 1jem, 1k1c, 1ka5, 1kkl

Phosphotransferase system, phosphocarrier HPr protein
Phosphotransferase system, phosphocarrier HPr protein
	Phosphocarrier protein HPr, E.Coli
Identifiers
Symbol	PTS_HPr_protein
Pfam	PF00381
InterPro	IPR000032
PROSITE	PDOC00318
SCOP2	1ptf / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1cm2, 1cm3, 1fu0, 1ggr, 1hdn, 1j6t, 1jem, 1k1c, 1ka5, 1kkl

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

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 Gram-positive bacteria only, is phosphorylated by an ATP-dependent protein kinase, a process which probably plays a regulatory role in sugar transport.

References[]

^ 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.
^ 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.

This article incorporates text from the public domain Pfam and InterPro: IPR000032

[PUB00003612-1] 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.

[PUB00000073-2] 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.

[PUB00003342-3] 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.

[PUB00005243-4] 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.

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