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P0A0E3

- PTHP_STAAU

UniProt

P0A0E3 - PTHP_STAAU

Protein

Phosphocarrier protein HPr

Gene

ptsH

Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 87
    Helixi16 – 2914
    Beta strandi30 – 378
    Beta strandi40 – 434
    Helixi47 – 515
    Turni52 – 543
    Beta strandi60 – 6910
    Helixi70 – 8415

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X93205 Genomic DNA. Translation: CAA63688.1.
    PIRiA03404. WPSAHP.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X93205 Genomic DNA. Translation: CAA63688.1 .
    PIRi A03404. WPSAHP.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KA5 NMR - A 1-88 [» ]
    ProteinModelPortali P0A0E3.
    SMRi P0A0E3. Positions 1-88.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1925.

    Miscellaneous databases

    EvolutionaryTracei P0A0E3.

    Family and domain databases

    Gene3Di 3.30.1340.10. 1 hit.
    InterProi IPR000032. HPr_prot-like.
    IPR001020. PTS_HPr_His_P_site.
    IPR002114. PTS_HPr_Ser_P_site.
    [Graphical view ]
    Pfami PF00381. PTS-HPr. 1 hit.
    [Graphical view ]
    PRINTSi PR00107. PHOSPHOCPHPR.
    SUPFAMi SSF55594. SSF55594. 1 hit.
    TIGRFAMsi TIGR01003. PTS_HPr_family. 1 hit.
    PROSITEi PS51350. PTS_HPR_DOM. 1 hit.
    PS00369. PTS_HPR_HIS. 1 hit.
    PS00589. PTS_HPR_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 59 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