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Protein

Phosphocarrier protein HPr

Gene

ptsH

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

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; alternatePROSITE-ProRule annotation1 Publication

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

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 Componenti: Chromosome

Organism-specific databases

GenoListiBSU13900. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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/PPROSITE-ProRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08877.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

IntActiP08877. 5 interactions.
MINTiMINT-8366889.
STRINGi224308.Bsubs1_010100007716.

Structurei

Secondary structure

1
88
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Beta strandi10 – 123Combined sources
Helixi16 – 2611Combined sources
Beta strandi29 – 379Combined 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
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.
InParanoidiP08877.
KOiK11189.
OMAiTSESGIH.
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

        10         20         30         40         50
MAQKTFKVTA DSGIHARPAT VLVQTASKYD ADVNLEYNGK TVNLKSIMGV
60 70 80
MSLGIAKGAE ITISASGADE NDALNALEET MKSEGLGE
Length:88
Mass (Da):9,189
Last modified:January 23, 2007 - v3
Checksum:i2B13DBD63DD636A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12832 Genomic DNA. Translation: CAA31317.1.
AL009126 Genomic DNA. Translation: CAB13263.1.
PIRiS04177. WQBSPH.
RefSeqiNP_389273.1. NC_000964.3.
WP_003154654.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13263; CAB13263; BSU13900.
GeneIDi939259.
9779573.
KEGGibsu:BSU13900.
PATRICi18974563. VBIBacSub10457_1473.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12832 Genomic DNA. Translation: CAA31317.1.
AL009126 Genomic DNA. Translation: CAB13263.1.
PIRiS04177. WQBSPH.
RefSeqiNP_389273.1. NC_000964.3.
WP_003154654.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

IntActiP08877. 5 interactions.
MINTiMINT-8366889.
STRINGi224308.Bsubs1_010100007716.

Proteomic databases

PaxDbiP08877.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13263; CAB13263; BSU13900.
GeneIDi939259.
9779573.
KEGGibsu:BSU13900.
PATRICi18974563. VBIBacSub10457_1473.

Organism-specific databases

GenoListiBSU13900. [Micado]

Phylogenomic databases

eggNOGiCOG1925.
HOGENOMiHOG000278399.
InParanoidiP08877.
KOiK11189.
OMAiTSESGIH.
OrthoDBiEOG6XDGX2.
PhylomeDBiP08877.

Enzyme and pathway databases

BioCyciBSUB:BSU13900-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP08877.
PROiP08877.

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. "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: June 24, 2015
This is version 158 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

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.