Phosphocarrier protein HPr

Details

Name
Phosphocarrier protein HPr
Synonyms
  • 2.7.11.-
  • Histidine-containing protein
Gene Name
ptsH
Organism
Bacillus subtilis (strain 168)
Amino acid sequence
>lcl|BSEQ0016405|Phosphocarrier protein HPr
MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAE
ITISASGADENDALNALEETMKSEGLGE
Number of residues
88
Molecular Weight
9189.285
Theoretical pI
4.52
GO Classification
Functions
protein serine/threonine kinase activity
Processes
phosphoenolpyruvate-dependent sugar phosphotransferase system / regulation of carbohydrate utilization / regulation of transcription, DNA-templated / transcription, DNA-templated
Components
cytoplasm
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016406|Phosphocarrier protein HPr (ptsH)
ATGGCACAAAAAACATTTAAAGTAACTGCAGATTCTGGAATCCATGCTCGTCCTGCGACA
GTTCTTGTACAAACTGCTAGCAAATACGACGCTGACGTTAATTTAGAATATAACGGCAAA
ACAGTTAACCTTAAATCTATTATGGGTGTTATGTCTTTAGGTATCGCTAAAGGCGCTGAG
ATCACAATCTCTGCTTCCGGAGCTGACGAAAACGATGCTCTTAACGCTTTAGAAGAAACA
ATGAAAAGCGAAGGACTCGGCGAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP08877
UniProtKB Entry NamePTHP_BACSU
GenBank Protein ID580913
GenBank Gene IDX12832
General References
  1. Gonzy-Treboul G, Zagorec M, Rain-Guion MC, Steinmetz M: Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a ptsHI operon. Mol Microbiol. 1989 Jan;3(1):103-12. [Article]
  2. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, Joris B, Karamata D, Kasahara Y, Klaerr-Blanchard M, Klein C, Kobayashi Y, Koetter P, Koningstein G, Krogh S, Kumano M, Kurita K, Lapidus A, Lardinois S, Lauber J, Lazarevic V, Lee SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, Presecan E, Pujic P, Purnelle B, Rapoport G, Rey M, Reynolds S, Rieger M, Rivolta C, Rocha E, Roche B, Rose M, Sadaie Y, Sato T, Scanlan E, Schleich S, Schroeter R, Scoffone F, Sekiguchi J, Sekowska A, Seror SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [Article]
  3. Mitchell C, Morris PW, Vary JC: Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation. Mol Microbiol. 1992 Jun;6(12):1579-81. [Article]
  4. Graumann P, Schroder K, Schmid R, Marahiel MA: Cold shock stress-induced proteins in Bacillus subtilis. J Bacteriol. 1996 Aug;178(15):4611-9. [Article]
  5. Deutscher J, Reizer J, Fischer C, Galinier A, Saier MH Jr, Steinmetz M: Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis. J Bacteriol. 1994 Jun;176(11):3336-44. [Article]
  6. Fujita Y, Miwa Y, Galinier A, Deutscher J: Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol Microbiol. 1995 Sep;17(5):953-60. [Article]
  7. Macek B, Mijakovic I, Olsen JV, Gnad F, Kumar C, Jensen PR, Mann M: The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics. 2007 Apr;6(4):697-707. Epub 2007 Jan 10. [Article]
  8. Herzberg O, Reddy P, Sutrina S, Saier MH Jr, Reizer J, Kapadia G: Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2499-503. [Article]
  9. Liao DI, Herzberg O: Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins. Structure. 1994 Dec 15;2(12):1203-16. [Article]
  10. Wittekind M, Reizer J, Klevit RE: Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap. Biochemistry. 1990 Aug 7;29(31):7191-200. [Article]
  11. Wittekind M, Rajagopal P, Branchini BR, Reizer J, Saier MH Jr, Klevit RE: Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy. Protein Sci. 1992 Oct;1(10):1363-76. [Article]
  12. Jones BE, Rajagopal P, Klevit RE: Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis. Protein Sci. 1997 Oct;6(10):2107-19. [Article]
  13. Fieulaine S, Morera S, Poncet S, Mijakovic I, Galinier A, Janin J, Deutscher J, Nessler S: X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13437-41. Epub 2002 Oct 1. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01899Nd1-PhosphonohistidineexperimentalunknownDetails