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Protein

Phosphocarrier protein HPr

Gene

ptsH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).

Catalytic activityi

Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei15 – 151Pros-phosphohistidine intermediatePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • enzyme activator activity Source: EcoliWiki
  • kinase activity Source: EcoCyc
  • phosphoenolpyruvate-protein phosphotransferase activity Source: EcoCyc
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • phosphoenolpyruvate-dependent sugar phosphotransferase system Source: EcoCyc
  • positive regulation of catalytic activity Source: GOC
  • positive regulation of glycogen catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:PTSH-MONOMER.
ECOL316407:JW2408-MONOMER.
MetaCyc:PTSH-MONOMER.

Protein family/group databases

TCDBi8.A.8.1.1. the phosphotransferase system hpr (hpr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphocarrier protein HPr (EC:2.7.11.-)
Alternative name(s):
Histidine-containing protein
Gene namesi
Name:ptsH
Synonyms:hpr
Ordered Locus Names:b2415, JW2408
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10788. ptsH.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • phosphoenolpyruvate-dependent sugar phosphotransferase complex Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8585Phosphocarrier protein HPrPRO_0000107850Add
BLAST

Proteomic databases

EPDiP0AA04.
PaxDbiP0AA04.
PRIDEiP0AA04.

2D gel databases

SWISS-2DPAGEP0AA04.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
bglGP119895EBI-902853,EBI-545674
ptsIP088392EBI-902853,EBI-551533

Protein-protein interaction databases

BioGridi4259700. 557 interactions.
DIPiDIP-35731N.
IntActiP0AA04. 7 interactions.
MINTiMINT-8085981.
STRINGi511145.b2415.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi10 – 123Combined sources
Helixi16 – 2611Combined sources
Beta strandi31 – 377Combined sources
Beta strandi40 – 434Combined sources
Helixi47 – 504Combined sources
Beta strandi60 – 678Combined sources
Helixi70 – 8112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM2X-ray1.80A1-85[»]
1CM3X-ray1.60A1-85[»]
1GGRNMR-B1-85[»]
1HDNNMR-A1-85[»]
1J6TNMR-B1-85[»]
1OPDX-ray1.50A1-85[»]
1PFHNMR-A1-85[»]
1POHX-ray2.00A1-85[»]
1VRCNMR-C/D1-85[»]
2JELX-ray2.50P1-85[»]
2LRKNMR-D1-85[»]
2LRLNMR-D1-85[»]
2XDFNMR-C/D1-85[»]
3CCDX-ray1.00A/B1-85[»]
3EZANMR-B1-85[»]
3EZBNMR-B1-85[»]
3EZENMR-B1-85[»]
4XWJX-ray2.10B1-85[»]
ProteinModelPortaliP0AA04.
SMRiP0AA04. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AA04.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585HPrPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the HPr family.Curated
Contains 1 HPr domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1925. LUCA.
HOGENOMiHOG000278399.
InParanoidiP0AA04.
KOiK02784.
OMAiYQGKDVN.
OrthoDBiEOG6XDGX2.
PhylomeDBiP0AA04.

Family and domain databases

Gene3Di3.30.1340.10. 1 hit.
InterProiIPR000032. HPr_prot-like.
IPR001020. PTS_HPr_His_P_site.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]
PfamiPF00381. PTS-HPr. 1 hit.
[Graphical view]
PRINTSiPR00107. PHOSPHOCPHPR.
SUPFAMiSSF55594. SSF55594. 1 hit.
TIGRFAMsiTIGR01003. PTS_HPr_family. 1 hit.
PROSITEiPS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AA04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL
60 70 80
QTLGLTQGTV VTISAEGEDE QKAVEHLVKL MAELE
Length:85
Mass (Da):9,119
Last modified:April 1, 1988 - v1
Checksum:iE5C8879C0A95AD41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10425 Genomic DNA. Translation: AAA24438.1.
J02796 Genomic DNA. Translation: AAA24440.1.
M21994 Genomic DNA. Translation: AAA24384.1.
M21451 Genomic DNA. Translation: AAA23655.1.
U00096 Genomic DNA. Translation: AAC75468.1.
AP009048 Genomic DNA. Translation: BAA16289.1.
PIRiA29785. WQECPH.
RefSeqiNP_416910.1. NC_000913.3.
WP_000487600.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75468; AAC75468; b2415.
BAA16289; BAA16289; BAA16289.
GeneIDi5550362.
946886.
KEGGiecj:JW2408.
eco:b2415.
PATRICi32120213. VBIEscCol129921_2509.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10425 Genomic DNA. Translation: AAA24438.1.
J02796 Genomic DNA. Translation: AAA24440.1.
M21994 Genomic DNA. Translation: AAA24384.1.
M21451 Genomic DNA. Translation: AAA23655.1.
U00096 Genomic DNA. Translation: AAC75468.1.
AP009048 Genomic DNA. Translation: BAA16289.1.
PIRiA29785. WQECPH.
RefSeqiNP_416910.1. NC_000913.3.
WP_000487600.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CM2X-ray1.80A1-85[»]
1CM3X-ray1.60A1-85[»]
1GGRNMR-B1-85[»]
1HDNNMR-A1-85[»]
1J6TNMR-B1-85[»]
1OPDX-ray1.50A1-85[»]
1PFHNMR-A1-85[»]
1POHX-ray2.00A1-85[»]
1VRCNMR-C/D1-85[»]
2JELX-ray2.50P1-85[»]
2LRKNMR-D1-85[»]
2LRLNMR-D1-85[»]
2XDFNMR-C/D1-85[»]
3CCDX-ray1.00A/B1-85[»]
3EZANMR-B1-85[»]
3EZBNMR-B1-85[»]
3EZENMR-B1-85[»]
4XWJX-ray2.10B1-85[»]
ProteinModelPortaliP0AA04.
SMRiP0AA04. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259700. 557 interactions.
DIPiDIP-35731N.
IntActiP0AA04. 7 interactions.
MINTiMINT-8085981.
STRINGi511145.b2415.

Protein family/group databases

TCDBi8.A.8.1.1. the phosphotransferase system hpr (hpr) family.

2D gel databases

SWISS-2DPAGEP0AA04.

Proteomic databases

EPDiP0AA04.
PaxDbiP0AA04.
PRIDEiP0AA04.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75468; AAC75468; b2415.
BAA16289; BAA16289; BAA16289.
GeneIDi5550362.
946886.
KEGGiecj:JW2408.
eco:b2415.
PATRICi32120213. VBIEscCol129921_2509.

Organism-specific databases

EchoBASEiEB0781.
EcoGeneiEG10788. ptsH.

Phylogenomic databases

eggNOGiCOG1925. LUCA.
HOGENOMiHOG000278399.
InParanoidiP0AA04.
KOiK02784.
OMAiYQGKDVN.
OrthoDBiEOG6XDGX2.
PhylomeDBiP0AA04.

Enzyme and pathway databases

BioCyciEcoCyc:PTSH-MONOMER.
ECOL316407:JW2408-MONOMER.
MetaCyc:PTSH-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AA04.
PROiP0AA04.

Family and domain databases

Gene3Di3.30.1340.10. 1 hit.
InterProiIPR000032. HPr_prot-like.
IPR001020. PTS_HPr_His_P_site.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]
PfamiPF00381. PTS-HPr. 1 hit.
[Graphical view]
PRINTSiPR00107. PHOSPHOCPHPR.
SUPFAMiSSF55594. SSF55594. 1 hit.
TIGRFAMsiTIGR01003. PTS_HPr_family. 1 hit.
PROSITEiPS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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., Danchin A.
    J. Bacteriol. 170:3827-3837(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Analysis of the ptsH-ptsI-crr region in Escherichia coli K-12: nucleotide sequence of the ptsH gene."
    de Reuse H., Roy A., Danchin A.
    Gene 35:199-207(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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., Presper K.A., Doering T.L., Roseman S.
    J. Biol. Chem. 262:16241-16253(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH."
    Byrne C.R., Monroe R.S., Ward K.A., Kredich N.M.
    J. Bacteriol. 170:3150-3157(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  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., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-20.
    Strain: K12.
  9. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  10. Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
    Submitted (FEB-1996) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "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., de Lange L.C., Bachovchin W.W., Robillard G.T.
    Biochemistry 29:8164-8171(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE HIS-15.
  12. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  13. "The 2.0-A resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr. A redetermination."
    Jia Z., Quail J.W., Waygood E.B., Delbaere L.T.J.
    J. Biol. Chem. 268:22490-22501(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  14. "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., Anderson J.W., Georges F., Quail J.W., Delbaere L.T.J., Waygood E.B.
    Biochemistry 35:11260-11267(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  15. "Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR."
    Klevit R.E., Waygood E.B.
    Biochemistry 25:7774-7781(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  16. "Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy."
    Hammen P.K., Waygood E.B., Klevit R.E.
    Biochemistry 30:11842-11850(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  17. "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., Groetzinger J., Dijkstra K., Scheek R.M., Robillard G.T.
    Eur. J. Biochem. 210:881-891(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  18. "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., Hangyi I.W., van Schaik R.C., Berendsen H.J., van Gunsteren W.F., Scheek R.M., Robillard G.T.
    J. Mol. Biol. 237:544-559(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  19. "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., Boelens R., Scheek R.M., Robillard G.T.
    J. Mol. Biol. 246:180-193(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  20. "Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement."
    van Nuland N.A.J., Wiersma J.A., van der Spoel D., de Groot B.L., Scheek R.M., Robillard G.T.
    Protein Sci. 5:442-446(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  21. "Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr."
    Garrett D.S., Seok Y.-J., Peterkofsky A., Gronenborn A.M., Clore G.M.
    Nat. Struct. Biol. 6:166-173(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiPTHP_ECOLI
AccessioniPrimary (citable) accession number: P0AA04
Secondary accession number(s): P05525, P07006
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: March 16, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.