Phosphocarrier protein HPr
Details
- Name
- Phosphocarrier protein HPr
- Synonyms
- 2.7.11.-
- Histidine-containing protein
- Gene Name
- ptsH
- Organism
- Enterococcus faecalis (strain ATCC 700802 / V583)
- Amino acid sequence
>lcl|BSEQ0017058|Phosphocarrier protein HPr MEKKEFHIVAETGIHARPATLLVQTASKFNSDINLEYKGKSVNLKSIMGVMSLGVGQGSD VTITVDGADEAEGMAAIVETLQKEGLAE
- Number of residues
- 88
- Molecular Weight
- 9320.575
- Theoretical pI
- 4.58
- GO Classification
- Functionsprotein serine/threonine kinase activityProcessesphosphoenolpyruvate-dependent sugar phosphotransferase system / regulation of transcription, DNA-templated / transcription, DNA-templatedComponentscytoplasm
- General Function
- Protein serine/threonine kinase activity
- Specific Function
- General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the permease (enzymes II/III).P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).
- Pfam Domain Function
- PTS-HPr (PF00381)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0017059|Phosphocarrier protein HPr (ptsH) ATGGAAAAGAAAGAATTTCACATTGTAGCAGAAACAGGAATTCACGCACGTCCAGCTACT TTATTAGTACAAACTGCAAGCAAATTTAACTCAGATATTAACTTAGAATACAAAGGTAAA TCTGTTAACTTAAAATCAATCATGGGCGTTATGTCTTTAGGCGTTGGTCAAGGTTCTGAC GTAACAATCACTGTTGATGGTGCTGACGAAGCTGAAGGAATGGCAGCAATCGTTGAAACA TTACAAAAAGAAGGATTGGCTGAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P07515 UniProtKB Entry Name PTHP_ENTFA GenBank Gene ID Z19137 - General References
- Deutscher J, Pevec B, Beyreuther K, Kiltz HH, Hengstenberg W: Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr. Biochemistry. 1986 Oct 21;25(21):6543-51. [Article]
- Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [Article]
- Jia Z, Vandonselaar M, Quail JW, Delbaere LT: Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein. Nature. 1993 Jan 7;361(6407):94-7. [Article]
- Audette GF, Engelmann R, Hengstenberg W, Deutscher J, Hayakawa K, Quail JW, Delbaere LT: The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis. J Mol Biol. 2000 Nov 3;303(4):545-53. [Article]
- Hahmann M, Maurer T, Lorenz M, Hengstenberg W, Glaser S, Kalbitzer HR: Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis. Eur J Biochem. 1998 Feb 15;252(1):51-8. [Article]
- Maurer T, Doker R, Gorler A, Hengstenberg W, Kalbitzer HR: Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution. Eur J Biochem. 2001 Feb;268(3):635-44. [Article]