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P0A0E3 (PTHP_STAAU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphocarrier protein HPr

EC=2.7.11.-
Alternative name(s):
Histidine-containing protein
Gene names
Name:ptsH
OrganismStaphylococcus aureus
Taxonomic identifier1280 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length88 AA.
Sequence statusComplete.
Protein existenceEvidence 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).

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.

Catalytic activity

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

Enzyme regulation

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the HPr family.

Contains 1 HPr domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8888Phosphocarrier protein HPr
PRO_0000107878

Regions

Domain1 – 8888HPr

Sites

Active site151Pros-phosphohistidine intermediate

Amino acid modifications

Modified residue461Phosphoserine; by HPrK/P

Secondary structure

.............. 88
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A0E3 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: B2C6639D53226FF9

FASTA889,496
        10         20         30         40         50         60 
MEQNSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV MSLGVGKDAE 

        70         80 
ITIYADGSDE SDAIQAISDV LSKEGLTK 

« Hide

References

[1]Kravanja M., Engelmann R., Christiansen I., Hengstenberg W.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 305A.
[2]"The phosphoenolpyruvate-dependent phosphotransferase system of Staphylococcus aureus. 1. Amino-acid sequence of the phosphocarrier protein HPr."
Beyreuther K., Raufuss H., Schrecker O., Hengstenberg W.
Eur. J. Biochem. 75:275-286(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE.
[3]"The phosphoenolpyruvate:sugar phosphotransferase system in Gram-positive bacteria: properties, mechanism, and regulation."
Reizer J., Saier M.H. Jr., Deutscher J., Grenier F., Thompson J., Hengstenberg W.
Crit. Rev. Microbiol. 15:297-338(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Two-dimensional 1H NMR studies on HPr protein from Staphylococcus aureus: complete sequential assignments and secondary structure."
Kalbitzer H.R., Neidig K.-P., Hengstenberg W.
Biochemistry 30:11186-11192(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"The solution structure of the histidine-containing protein (HPr) from Staphylococcus aureus as determined by two-dimensional 1H-NMR spectroscopy."
Kalbitzer H.R., Hengstenberg W.
Eur. J. Biochem. 216:205-214(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X93205 Genomic DNA. Translation: CAA63688.1.
PIRWPSAHP. A03404.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KA5NMR-A1-88[»]
ProteinModelPortalP0A0E3.
SMRP0A0E3. Positions 1-88.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1925.

Family and domain databases

Gene3D3.30.1340.10. 1 hit.
InterProIPR000032. HPr_prot-like.
IPR001020. PTS_HPr_His_P_site.
IPR002114. PTS_HPr_Ser_P_site.
[Graphical view]
PfamPF00381. PTS-HPr. 1 hit.
[Graphical view]
PRINTSPR00107. PHOSPHOCPHPR.
SUPFAMSSF55594. SSF55594. 1 hit.
TIGRFAMsTIGR01003. PTS_HPr_family. 1 hit.
PROSITEPS51350. PTS_HPR_DOM. 1 hit.
PS00369. PTS_HPR_HIS. 1 hit.
PS00589. PTS_HPR_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A0E3.

Entry information

Entry namePTHP_STAAU
AccessionPrimary (citable) accession number: P0A0E3
Secondary accession number(s): P02907
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 2005
Last modified: July 9, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references