P0AA04 (PTHP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

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 Serine/threonine-protein 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 direct assay PubMed 5545082. Source: EcoCyc positive regulation of glycogen catabolic process Inferred from direct assay PubMed 9334229. Source: EcoCyc
Cellular_component	phosphoenolpyruvate-dependent sugar phosphotransferase complex Inferred from direct assay PubMed 5545082. Source: EcoCyc
Molecular_function	enzyme activator activity Inferred from direct assay PubMed 9334229. Source: EcoliWiki kinase activity Inferred from direct assay PubMed 4942330. Source: EcoCyc phosphoenolpyruvate-protein phosphotransferase activity Inferred from direct assay PubMed 5545082. Source: EcoCyc protein serine/threonine 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

85

Phosphocarrier protein HPr

PRO_0000107850

Regions

Domain

1 – 85

85

HPr

Sites

Active site

15

1

Pros-phosphohistidine intermediate Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

85

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

10 – 12

3

Helix

16 – 26

11

Beta strand

31 – 37

7

Beta strand

40 – 43

4

Helix

47 – 50

4

Beta strand

60 – 67

8

Helix

70 – 81

12

Sequences

	Sequence		Length	Mass (Da)
	P0AA04 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: E5C8879C0A95AD41	FASTA	85	9,119
	10 20 30 40 50 60 MFQQEVTITA PNGLHTRPAA QFVKEAKGFT SEITVTSNGK SASAKSLFKL QTLGLTQGTV 70 80 VTISAEGEDE QKAVEHLVKL MAELE

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] [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]	"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] [Europe PMC] [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] [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.
+	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.
YP_490651.1. NC_007779.1.

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	[»]
2LRK	NMR	-	D	1-85	[»]
2LRL	NMR	-	D	1-85	[»]
2XDF	NMR	-	C/D	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.

STRING

511145.b2415.

Protein family/group databases

TCDB

8.A.8.1.1. phosphotransferase system HPr family.

PTM databases

PhosSite

P0810427.

2D gel databases

SWISS-2DPAGE

P0AA04.

Proteomic databases

PaxDb

P0AA04.

PRIDE

P0AA04.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75468; AAC75468; b2415.
BAA16289; BAA16289; BAA16289.

GeneID

12930706.
946886.

KEGG

ecj:Y75_p2376.
eco:b2415.

PATRIC

32120213. VBIEscCol129921_2509.

Organism-specific databases

EchoBASE

EB0781.

EcoGene

EG10788. ptsH.

Phylogenomic databases

eggNOG

COG1925.

HOGENOM

HOG000278399.

KO

K02784.

OMA

TAGKFTS.

ProtClustDB

PRK10850.

Enzyme and pathway databases

BioCyc

EcoCyc:PTSH-MONOMER.
ECOL316407:JW2408-MONOMER.

Gene expression databases

Genevestigator

P0AA04.

Family and domain databases

Gene3D

3.30.1340.10. 1 hit.

InterPro

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

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...

Other

EvolutionaryTrace

P0AA04.

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:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program