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Protein

Phosphocarrier protein HPr

Gene

ptsH

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 4 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).
P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Phosphorylation on Ser-46 inhibits the phosphoryl transfer from enzyme I to HPr.

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Phosphotransferase system, Sugar transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-697-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphocarrier protein HPr (EC:2.7.11.-)
Alternative name(s):
Histidine-containing protein
Gene namesi
Name:ptsH
Ordered Locus Names:EF_0709
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8888Phosphocarrier protein HPrPRO_0000107853Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by HPrK/PPROSITE-ProRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi226185.EF0709.

Structurei

Secondary structure

1
88
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi16 – 2611Combined sources
Beta strandi30 – 378Combined sources
Beta strandi40 – 434Combined sources
Helixi47 – 537Combined sources
Beta strandi60 – 678Combined sources
Helixi70 – 8314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU0X-ray1.90A/B1-87[»]
1PTFX-ray1.60A1-88[»]
1QFRNMR-A1-88[»]
ProteinModelPortaliP07515.
SMRiP07515. Positions 1-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8888HPrPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105KRI. Bacteria.
COG1925. LUCA.
KOiK11189.
OMAiYQGKDVN.
OrthoDBiEOG6XDGX2.

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.

P07515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKKEFHIVA ETGIHARPAT LLVQTASKFN SDINLEYKGK SVNLKSIMGV
60 70 80
MSLGVGQGSD VTITVDGADE AEGMAAIVET LQKEGLAE
Length:88
Mass (Da):9,321
Last modified:November 1, 1995 - v2
Checksum:iD01E27D6CEE6DA06
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 881E → EQ AA sequence (PubMed:3098288).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19137 Genomic DNA. Translation: CAA79533.1.
AE016830 Genomic DNA. Translation: AAO80530.1.
PIRiA25053. WQSOHP.
RefSeqiNP_814460.1. NC_004668.1.
WP_002355551.1. NZ_KE136527.1.

Genome annotation databases

EnsemblBacteriaiAAO80530; AAO80530; EF_0709.
GeneIDi1199609.
KEGGiefa:EF0709.
PATRICi21851810. VBIEntFae7065_0655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19137 Genomic DNA. Translation: CAA79533.1.
AE016830 Genomic DNA. Translation: AAO80530.1.
PIRiA25053. WQSOHP.
RefSeqiNP_814460.1. NC_004668.1.
WP_002355551.1. NZ_KE136527.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FU0X-ray1.90A/B1-87[»]
1PTFX-ray1.60A1-88[»]
1QFRNMR-A1-88[»]
ProteinModelPortaliP07515.
SMRiP07515. Positions 1-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF0709.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO80530; AAO80530; EF_0709.
GeneIDi1199609.
KEGGiefa:EF0709.
PATRICi21851810. VBIEntFae7065_0655.

Phylogenomic databases

eggNOGiENOG4105KRI. Bacteria.
COG1925. LUCA.
KOiK11189.
OMAiYQGKDVN.
OrthoDBiEOG6XDGX2.

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-697-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07515.

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. Reizer J., Mitchell W.J., Romano A.H., Mirkov E.T., Saier M.H. Jr.
    Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr."
    Deutscher J., Pevec B., Beyreuther K., Kiltz H.H., Hengstenberg W.
    Biochemistry 25:6543-6551(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700802 / V583.
  4. "Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein."
    Jia Z., Vandonselaar M., Quail J.W., Delbaere L.T.J.
    Nature 361:94-97(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  5. "The 1.9-A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis."
    Audette G.F., Engelmann R., Hengstenberg W., Deutscher J., Hayakawa K., Quail J.W., Delbaere L.T.
    J. Mol. Biol. 303:545-553(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  6. "Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis."
    Hahmann M., Maurer T., Lorenz M., Hengstenberg W., Glaser S., Kalbitzer H.R.
    Eur. J. Biochem. 252:51-58(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution."
    Maurer T., Doeker R., Goerler A., Hengstenberg W., Kalbitzer H.R.
    Eur. J. Biochem. 268:635-644(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiPTHP_ENTFA
AccessioniPrimary (citable) accession number: P07515
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1995
Last modified: November 11, 2015
This is version 143 of the entry and version 2 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.