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P08877

- PTHP_BACSU

UniProt

P08877 - PTHP_BACSU

Protein

Phosphocarrier protein HPr

Gene

ptsH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 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.

    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; alternate1 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. phosphoenolpyruvate-dependent sugar phosphotransferase system Source: UniProtKB-KW
    2. regulation of carbohydrate utilization Source: CACAO
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. 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

    Enzyme and pathway databases

    BioCyciBSUB:BSU13900-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:BSU13900
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU13900. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461S → A: No phosphorylation by HPrK/P; abolishes the catabolite repressive effects of glucose on gluconate kinase, glucitol dehydrogenase, and the mannitol-specific catabolic enzymes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 8887Phosphocarrier protein HPrPRO_0000107842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine1 Publication
    Modified residuei15 – 151Tele-phosphohistidine; alternate1 Publication
    Modified residuei46 – 461Phosphoserine; by HPrK/P1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP08877.

    PTM databases

    PhosSiteiP0802234.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ccpAP251443EBI-1034482,EBI-5247535

    Protein-protein interaction databases

    IntActiP08877. 5 interactions.
    MINTiMINT-8366889.
    STRINGi224308.BSU13900.

    Structurei

    Secondary structure

    1
    88
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Beta strandi10 – 123
    Helixi16 – 2611
    Beta strandi29 – 379
    Beta strandi40 – 434
    Helixi47 – 537
    Beta strandi60 – 678
    Helixi70 – 8314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEMNMR-A2-88[»]
    1KKLX-ray2.80H/I/J1-88[»]
    1KKMX-ray2.80H/I/J1-88[»]
    1SPHX-ray2.00A/B1-88[»]
    2FEPX-ray2.45S2-88[»]
    2HIDNMR-A2-88[»]
    2HPRX-ray2.00A2-88[»]
    3OQMX-ray2.96D/S2-88[»]
    3OQNX-ray3.30D/S2-88[»]
    3OQOX-ray2.97D/S2-88[»]
    ProteinModelPortaliP08877.
    SMRiP08877. Positions 2-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08877.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8887HPrPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1925.
    HOGENOMiHOG000278399.
    KOiK11189.
    OMAiVRINISI.
    OrthoDBiEOG6XDGX2.
    PhylomeDBiP08877.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08877-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQKTFKVTA DSGIHARPAT VLVQTASKYD ADVNLEYNGK TVNLKSIMGV   50
    MSLGIAKGAE ITISASGADE NDALNALEET MKSEGLGE 88
    Length:88
    Mass (Da):9,189
    Last modified:January 23, 2007 - v3
    Checksum:i2B13DBD63DD636A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12832 Genomic DNA. Translation: CAA31317.1.
    AL009126 Genomic DNA. Translation: CAB13263.1.
    PIRiS04177. WQBSPH.
    RefSeqiNP_389273.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB13263; CAB13263; BSU13900.
    GeneIDi939259.
    KEGGibsu:BSU13900.
    PATRICi18974563. VBIBacSub10457_1473.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12832 Genomic DNA. Translation: CAA31317.1 .
    AL009126 Genomic DNA. Translation: CAB13263.1 .
    PIRi S04177. WQBSPH.
    RefSeqi NP_389273.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JEM NMR - A 2-88 [» ]
    1KKL X-ray 2.80 H/I/J 1-88 [» ]
    1KKM X-ray 2.80 H/I/J 1-88 [» ]
    1SPH X-ray 2.00 A/B 1-88 [» ]
    2FEP X-ray 2.45 S 2-88 [» ]
    2HID NMR - A 2-88 [» ]
    2HPR X-ray 2.00 A 2-88 [» ]
    3OQM X-ray 2.96 D/S 2-88 [» ]
    3OQN X-ray 3.30 D/S 2-88 [» ]
    3OQO X-ray 2.97 D/S 2-88 [» ]
    ProteinModelPortali P08877.
    SMRi P08877. Positions 2-88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08877. 5 interactions.
    MINTi MINT-8366889.
    STRINGi 224308.BSU13900.

    PTM databases

    PhosSitei P0802234.

    Proteomic databases

    PaxDbi P08877.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13263 ; CAB13263 ; BSU13900 .
    GeneIDi 939259.
    KEGGi bsu:BSU13900.
    PATRICi 18974563. VBIBacSub10457_1473.

    Organism-specific databases

    GenoListi BSU13900. [Micado ]

    Phylogenomic databases

    eggNOGi COG1925.
    HOGENOMi HOG000278399.
    KOi K11189.
    OMAi VRINISI.
    OrthoDBi EOG6XDGX2.
    PhylomeDBi P08877.

    Enzyme and pathway databases

    BioCyci BSUB:BSU13900-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P08877.
    PROi P08877.

    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. "Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: nucleotide sequence of ptsX, ptsH and the 5'-end of ptsI and evidence for a ptsHI operon."
      Gonzy-Treboul G., Zagorec M., Rain-Guion M.-C., Steinmetz M.
      Mol. Microbiol. 3:103-112(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Amino acid sequences of several Bacillus subtilis proteins modified by apparent guanylylation."
      Mitchell C., Morris P.W., Vary J.C.
      Mol. Microbiol. 6:1579-1581(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
    4. "Cold shock stress-induced proteins in Bacillus subtilis."
      Graumann P., Schroeder K., Schmid R., Marahiel M.A.
      J. Bacteriol. 178:4611-4619(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-27.
      Strain: 168 / JH642.
    5. "Loss of protein kinase-catalyzed phosphorylation of HPr, a phosphocarrier protein of the phosphotransferase system, by mutation of the ptsH gene confers catabolite repression resistance to several catabolic genes of Bacillus subtilis."
      Deutscher J., Reizer J., Fischer C., Galinier A., Saier M.H. Jr., Steinmetz M.
      J. Bacteriol. 176:3336-3344(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-46.
    6. "Specific recognition of the Bacillus subtilis gnt cis-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr."
      Fujita Y., Miwa Y., Galinier A., Deutscher J.
      Mol. Microbiol. 17:953-960(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.
    8. "Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution."
      Herzberg O., Reddy P., Sutrina S., Saier M.H. Jr., Reizer J., Kapadia G.
      Proc. Natl. Acad. Sci. U.S.A. 89:2499-2503(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), ACTIVE SITE HIS-15, PHOSPHORYLATION AT HIS-15.
    9. "Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins."
      Liao D.-I., Herzberg O.
      Structure 2:1203-1216(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
    10. "Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap."
      Wittekind M., Reizer J., Klevit R.E.
      Biochemistry 29:7191-7200(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    11. "Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy."
      Wittekind M., Rajagopal P., Branchini B.R., Reizer J., Saier M.H. Jr., Klevit R.E.
      Protein Sci. 1:1363-1376(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    12. "Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis."
      Jones B.E., Rajagopal P., Klevit R.E.
      Protein Sci. 6:2107-2119(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    13. "X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr."
      Fieulaine S., Morera S., Poncet S., Mijakovic I., Galinier A., Janin J., Deutscher J., Nessler S.
      Proc. Natl. Acad. Sci. U.S.A. 99:13437-13441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 16-88 IN COMPLEX WITH L.CASEI HPRK/P.

    Entry informationi

    Entry nameiPTHP_BACSU
    AccessioniPrimary (citable) accession number: P08877
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 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. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3