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| Accession Number: | P0AA04 |
| Protein Name: | Phosphocarrier protein aka PTHP aka HPr aka PTSH aka B2415 |
| Length: | 85 |
| Molecular Weight: | 9119.00 |
| Species: | Escherichia coli [83333] |
| Location1 / Topology2 / Orientation3: | Cytoplasm1 |
| Substrate | |
Cross database links:
| DIP: | DIP-35731N |
|---|---|
| RefSeq: | AP_003009.1 NP_416910.1 |
| Entrez Gene ID: | 946886 |
| Pfam: | PF00381 |
| BioCyc: | EcoCyc:PTSH-MONOMER ECOL168927:B2415-MONOMER |
| KEGG: | ecj:JW2408 eco:b2415 |
Gene Ontology
GO:0005737
C:cytoplasm
GO:0008047
F:enzyme activator activity
GO:0016301
F:kinase activity
GO:0005515
F:protein binding
GO:0005351
F:sugar:hydrogen symporter activity
GO:0009401
P:phosphoenolpyruvate-dependent sugar phospho...
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References (19)[1] “The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription.” de Reuse H.et.al. 2457575 [2] “Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide sequence of the ptsH gene.” de Reuse H.et.al. 2411636 [3] “Sugar transport by the bacterial phosphotransferase system. Molecular cloning and structural analysis of the Escherichia coli ptsH, ptsI, and crr genes.” Saffen D.W.et.al. 2960675 [4] “DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH.” Byrne C.R.et.al. 3290198 [5] “Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.” Yamamoto Y.et.al. 9205837 [6] “The complete genome sequence of Escherichia coli K-12.” Blattner F.R.et.al. 9278503 [7] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.” Hayashi K.et.al. 16738553 [8] “Small genes/gene-products in Escherichia coli K-12.” Wasinger V.C.et.al. 9868784 [9] “Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.” Link A.J.et.al. 9298646 [10] “Effect of phosphorylation on hydrogen-bonding interactions of the active site histidine of the phosphocarrier protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system determined by 15N NMR spectroscopy.” van Dijk A.A.et.al. 2261470 [11] “The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination.” Jia Z.et.al. 8226757 [12] “Mutation of serine-46 to aspartate in the histidine-containing protein of Escherichia coli mimics the inactivation by phosphorylation of serine-46 in HPrs from Gram-positive bacteria.” Napper S.et.al. 8784179 [13] “Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR.” Klevit R.E.et.al. 3542036 [14] “Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy.” Hammen P.K.et.al. 1751501 [15] “Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.” van Nuland N.A.J.et.al. 1483471 [16] “The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data.” van Nuland N.A.J.et.al. 8158637 [17] “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.” van Nuland N.A.J.et.al. 7853396 [18] “Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement.” van Nuland N.A.J.et.al. 8868480 [19] “Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.” Garrett D.S.et.al. 10048929
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1: MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV 61: VTISAEGEDE QKAVEHLVKL MAELE