Phosphocarrier protein HPr - Escherichia coli (strain K12)

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P0AA04 (PTHP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphocarrier protein HPr
EC=2.7.11.-

Alternative name(s):
Histidine-containing protein

Gene names

Name:	ptsH
Synonyms:	hpr
Ordered Locus Names:	b2415, JW2408

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	85 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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).
Catalytic activity	Protein HPr N(pi)-phospho-L-histidine + protein EIIA = protein HPr + protein EIIA N(tau)-phospho-L-histidine.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the HPr family. Contains 1 HPr domain.

Ontologies

Keywords
Biological process	Phosphotransferase system Sugar transport Transport
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	enzyme activator activity Inferred from direct assay. Source: EcoliWiki kinase activity Inferred from electronic annotation. Source: UniProtKB-KW sugar:hydrogen symporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
crr	P69783	1	EBI-902853,EBI-369856
ptsI	P08839	1	EBI-902853,EBI-551533

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 85

Phosphocarrier protein HPr

PRO_0000107850

Regions

Domain

1 – 85

HPr

Sites

Active site

Pros-phosphohistidine intermediate Ref.11

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AA04 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: E5C8879C0A95AD41
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FASTA

9,119

        10         20         30         40         50         60 
MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV 

        70         80 
VTISAEGEDE QKAVEHLVKL MAELE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2457575] [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: 2411636] [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: 2960675] [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: 3290198] [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. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] 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: 16738553] [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: 9868784] [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: 9298646] [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: 2261470] [Abstract] Cited for: ACTIVE SITE HIS-15.
[12]	"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: 8226757] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[13]	"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: 8784179] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[14]	"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: 3542036] [Abstract] Cited for: STRUCTURE BY NMR.
[15]	"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: 1751501] [Abstract] Cited for: STRUCTURE BY NMR.
[16]	"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: 1483471] [Abstract] Cited for: STRUCTURE BY NMR.
[17]	"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: 8158637] [Abstract] Cited for: STRUCTURE BY NMR.
[18]	"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: 7853396] [Abstract] Cited for: STRUCTURE BY NMR.
[19]	"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: 8868480] [Abstract] Cited for: STRUCTURE BY NMR.
[20]	"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: 10048929] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

WQECPH. A29785.

RefSeq

NP_416910.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CM2	X-ray	1.80	A	1-85	[»]
1CM3	X-ray	1.60	A	1-85	[»]
1GGR	NMR	-	B	1-85	[»]
1HDN	NMR	-	A	1-85	[»]
1J6T	NMR	-	B	1-85	[»]
1OPD	X-ray	1.50	A	1-85	[»]
1PFH	NMR	-	A	1-85	[»]
1POH	X-ray	2.00	A	1-85	[»]
1VRC	NMR	-	C/D	1-85	[»]
2JEL	X-ray	2.50	P	1-85	[»]
3CCD	X-ray	1.00	A/B	1-85	[»]
3EZA	NMR	-	B	1-85	[»]
3EZB	NMR	-	B	1-85	[»]
3EZE	NMR	-	B	1-85	[»]

ProteinModelPortal

P0AA04.

SMR

P0AA04. Positions 1-85.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35731N.

IntAct

P0AA04. 2 interactions.

Protein family/group databases

TCDB

8.A.8.1.1. phosphotransferase system HPr family.

PTM databases

PhosSite

P0AA04.

2D gel databases

SWISS-2DPAGE

P0AA04.

ECO2DBASE

F007.0. 6TH EDITION.

Proteomic databases

PRIDE

P0AA04.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001666; EBESCP00000001666; EBESCG00000001377.
EBESCT00000001667; EBESCP00000001667; EBESCG00000001377.
EBESCT00000001668; EBESCP00000001668; EBESCG00000001377.
EBESCT00000001669; EBESCP00000001669; EBESCG00000001377.
EBESCT00000001670; EBESCP00000001670; EBESCG00000001377.
EBESCT00000015453; EBESCP00000014744; EBESCG00000014513.

GeneID

946886.

GenomeReviews

Gene locus JW2408 in contig AP009048_GR.
Gene locus b2415 in contig U00096_GR.

KEGG

ecj:JW2408.
eco:b2415.

PATRIC

32120213. VBIEscCol129921_2509.

Organism-specific databases

EchoBASE

EB0781.

EcoGene

EG10788. ptsH.

Phylogenomic databases

eggNOG

COG1925.

GeneTree

EBGT00050000008932.

HOGENOM

HBG653254.

OMA

DEQQAVE.

PhylomeDB

P0AA04.

ProtClustDB

PRK10850.

Enzyme and pathway databases

BioCyc

EcoCyc:PTSH-MONOMER.
MetaCyc:PTSH-MONOMER.

Gene expression databases

Genevestigator

P0AA04.

Family and domain databases

InterPro

IPR001020. PTS_HPr_His_P_site.
IPR005698. PTS_HPr_prot.
IPR000032. PTS_HPr_prot-like.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]

Gene3D

G3DSA:3.30.1340.10. PTS_HPr_protein. 1 hit.

K02784.

Pfam

PF00381. PTS-HPr. 1 hit.
[Graphical view]

PRINTS

PR00107. PHOSPHOCPHPR.

SUPFAM

SSF55594. HPr_protein. 1 hit.

TIGRFAMs

TIGR01003. PTS_HPr_family. 1 hit.

PROSITE

PS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PTHP_ECOLI

Accession

Primary (citable) accession number: P0AA04
Secondary accession number(s): P05525, P07006

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents