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Protein

Phosphocarrier protein HPr

Gene

ptsH

Organism
Bacillus megaterium
Status
Reviewed-Annotation score: Annotation score: 3 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) (By similarity).By similarity
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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei15 – 151Pros-phosphohistidine intermediatePROSITE-ProRule annotation

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

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphocarrier protein HPr (EC:2.7.11.-)
Alternative name(s):
Histidine-containing protein
Gene namesi
Name:ptsH
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8888Phosphocarrier protein HPrPRO_0000107839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei46 – 461Phosphoserine; by HPrK/PPROSITE-ProRule annotation2 Publications

Keywords - PTMi

Phosphoprotein

PTM databases

iPTMnetiO69250.

Interactioni

Protein-protein interaction databases

STRINGi545693.BMQ_1303.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi16 – 2712Combined sources
Beta strandi29 – 379Combined sources
Beta strandi40 – 434Combined sources
Helixi47 – 526Combined sources
Beta strandi60 – 678Combined sources
Helixi70 – 8314Combined sources
Beta strandi86 – 883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZRX-ray2.80L/S/T/Y1-88[»]
2NZUX-ray2.50L1-88[»]
2NZVX-ray3.00L1-88[»]
2OENX-ray3.17L1-88[»]
ProteinModelPortaliO69250.
SMRiO69250. Positions 2-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO69250.

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

eggNOGiENOG4105KRI. Bacteria.
COG1925. LUCA.

Family and domain databases

Gene3Di3.30.1340.10. 1 hit.
InterProiIPR000032. HPr-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.

O69250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQKTFTVTA DSGIHARPAT TLVQAASKFD SDINLEFNGK TVNLKSIMGV
60 70 80
MSLGIQKGAT ITISAEGSDE ADALAALEDT MSKEGLGE
Length:88
Mass (Da):9,119
Last modified:August 1, 1998 - v1
Checksum:i4EDC85C2E0B9AA3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005075 Genomic DNA. Translation: CAA06331.1.
RefSeqiWP_013056011.1. NZ_LUCO01000002.1.

Genome annotation databases

GeneIDi9116674.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005075 Genomic DNA. Translation: CAA06331.1.
RefSeqiWP_013056011.1. NZ_LUCO01000002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RZRX-ray2.80L/S/T/Y1-88[»]
2NZUX-ray2.50L1-88[»]
2NZVX-ray3.00L1-88[»]
2OENX-ray3.17L1-88[»]
ProteinModelPortaliO69250.
SMRiO69250. Positions 2-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi545693.BMQ_1303.

PTM databases

iPTMnetiO69250.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9116674.

Phylogenomic databases

eggNOGiENOG4105KRI. Bacteria.
COG1925. LUCA.

Miscellaneous databases

EvolutionaryTraceiO69250.
PROiO69250.

Family and domain databases

Gene3Di3.30.1340.10. 1 hit.
InterProiIPR000032. HPr-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. "Sequence of ptsH and ptsI of Bacillus megaterium."
    Wagner A., Kuester E., Hillen W.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: WH348.
  2. "Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P."
    Schumacher M.A., Allen G.S., Diel M., Seidel G., Hillen W., Brennan R.G.
    Cell 118:731-741(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), PHOSPHORYLATION AT SER-46.
  3. "Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate."
    Schumacher M.A., Seidel G., Hillen W., Brennan R.G.
    J. Mol. Biol. 368:1042-1050(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), PHOSPHORYLATION AT SER-46.

Entry informationi

Entry nameiPTHP_BACME
AccessioniPrimary (citable) accession number: O69250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: August 1, 1998
Last modified: July 6, 2016
This is version 94 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

Documents

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

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 one 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.