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Protein

Phosphocarrier protein HPr

Gene

ptsH

Organism
Staphylococcus aureus
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 intermediate

GO - Molecular functioni

  1. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. phosphoenolpyruvate-dependent sugar phosphotransferase system Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphocarrier protein HPr (EC:2.7.11.-)
Alternative name(s):
Histidine-containing protein
Gene namesi
Name:ptsH
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8888Phosphocarrier protein HPrPRO_0000107878Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by HPrK/P

Keywords - PTMi

Phosphoprotein

Structurei

Secondary structure

1
88
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Helixi16 – 2914Combined sources
Beta strandi30 – 378Combined sources
Beta strandi40 – 434Combined sources
Helixi47 – 515Combined sources
Turni52 – 543Combined sources
Beta strandi60 – 6910Combined sources
Helixi70 – 8415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KA5NMR-A1-88[»]
ProteinModelPortaliP0A0E3.
SMRiP0A0E3. Positions 1-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A0E3.

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

eggNOGiCOG1925.

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.

P0A0E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQNSYVIID ETGIHARPAT MLVQTASKFD SDIQLEYNGK KVNLKSIMGV
60 70 80
MSLGVGKDAE ITIYADGSDE SDAIQAISDV LSKEGLTK
Length:88
Mass (Da):9,496
Last modified:March 1, 2005 - v1
Checksum:iB2C6639D53226FF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93205 Genomic DNA. Translation: CAA63688.1.
PIRiA03404. WPSAHP.
RefSeqiWP_000437472.1. NZ_KN050644.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X93205 Genomic DNA. Translation: CAA63688.1.
PIRiA03404. WPSAHP.
RefSeqiWP_000437472.1. NZ_KN050644.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KA5NMR-A1-88[»]
ProteinModelPortaliP0A0E3.
SMRiP0A0E3. Positions 1-88.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1925.

Miscellaneous databases

EvolutionaryTraceiP0A0E3.

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

  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.

Entry informationi

Entry nameiPTHP_STAAU
AccessioniPrimary (citable) accession number: P0A0E3
Secondary accession number(s): P02907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 2005
Last modified: March 4, 2015
This is version 63 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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.