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8.A.8.1.1
HPr of the PTS

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 NONE

Cross database links:

Genevestigator: P0AA04
EchoBASE: EB0781
EcoGene: EG10788
eggNOG: COG1925
HEGENOM: HBG653254
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...

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
Structure:
1CM2   1CM3   1GGR   1HDN   1J6T   1OPD   1PFH   1POH   1VRC   2JEL   [...more]

External Searches:

  • Search: DB with
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  • 2° Structure (Network Protein Sequence Analysis)

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FASTA formatted sequence
1:	MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV 
61:	VTISAEGEDE QKAVEHLVKL MAELE