Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08877 (PTHP_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Ordered Locus Names:BSU13900
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length88 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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). Ref.5 Ref.6

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. Ref.5 Ref.6

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ccpAP251443EBI-1034482,EBI-5247535

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 8887Phosphocarrier protein HPr
PRO_0000107842

Regions

Domain2 – 8887HPr

Sites

Active site151Pros-phosphohistidine intermediate; alternate Ref.8

Amino acid modifications

Modified residue121Phosphoserine Ref.7
Modified residue151Tele-phosphohistidine; alternate
Modified residue461Phosphoserine; by HPrK/P Ref.7

Experimental info

Mutagenesis461S → A: No phosphorylation by HPrK/P; abolishes the catabolite repressive effects of glucose on gluconate kinase, glucitol dehydrogenase, and the mannitol-specific catabolic enzymes. Ref.5

Secondary structure

................. 88
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08877 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2B13DBD63DD636A9

FASTA889,189
        10         20         30         40         50         60 
MAQKTFKVTA DSGIHARPAT VLVQTASKYD ADVNLEYNGK TVNLKSIMGV MSLGIAKGAE 

        70         80 
ITISASGADE NDALNALEET MKSEGLGE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12832 Genomic DNA. Translation: CAA31317.1.
AL009126 Genomic DNA. Translation: CAB13263.1.
PIRWQBSPH. S04177.
RefSeqNP_389273.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEMNMR-A2-88[»]
1KKLX-ray2.80H/I/J1-88[»]
1KKMX-ray2.80H/I/J1-88[»]
1SPHX-ray2.00A/B1-88[»]
2FEPX-ray2.45S2-87[»]
2HIDNMR-A2-88[»]
2HPRX-ray2.00A2-88[»]
3OQMX-ray2.96D/S2-88[»]
3OQNX-ray3.30D/S2-88[»]
3OQOX-ray2.97D/S2-88[»]
ProteinModelPortalP08877.
SMRP08877. Positions 2-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08877. 5 interactions.
MINTMINT-8366889.
STRING224308.BSU13900.

PTM databases

PhosSiteP0802234.

Proteomic databases

PaxDbP08877.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13263; CAB13263; BSU13900.
GeneID939259.
KEGGbsu:BSU13900.
PATRIC18974563. VBIBacSub10457_1473.

Organism-specific databases

GenoListBSU13900. [Micado]

Phylogenomic databases

eggNOGCOG1925.
HOGENOMHOG000278399.
KOK11189.
OMASEIQLEY.
OrthoDBEOG6XDGX2.
ProtClustDBPRK13780.

Enzyme and pathway databases

BioCycBSUB:BSU13900-MONOMER.

Family and domain databases

Gene3D3.30.1340.10. 1 hit.
InterProIPR001020. PTS_HPr_His_P_site.
IPR005698. PTS_HPr_prot.
IPR000032. PTS_HPr_prot-like.
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

EvolutionaryTraceP08877.
PROP08877.

Entry information

Entry namePTHP_BACSU
AccessionPrimary (citable) accession number: P08877
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 147 of the entry and version 3 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList