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Protein

Ribosome hibernation promoting factor

Gene

hpf

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

During stationary phase, promotes and stabilizes dimerization of 70S ribosomes by the ribosome modulation factor (RMF), leading to the formation of inactive 100S ribosomes. May convert immature 90S particles formed by RMF into 100S ribosomes. May also function as a potential translational inhibitor.4 Publications

GO - Molecular functioni

  • ribosomal small subunit binding Source: EcoCyc
  • ribosome binding Source: EcoCyc

GO - Biological processi

  • negative regulation of translation Source: EcoCyc
  • primary metabolic process Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Enzyme and pathway databases

BioCyciEcoCyc:EG11681-MONOMER.
ECOL316407:JW3170-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome hibernation promoting factor
Gene namesi
Name:hpf
Synonyms:yhbH
Ordered Locus Names:b3203, JW3170
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11681. hpf.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9595Ribosome hibernation promoting factorPRO_0000097417Add
BLAST

Proteomic databases

EPDiP0AFX0.
PaxDbiP0AFX0.
PRIDEiP0AFX0.

Expressioni

Inductioni

Induced during stationary growth phase and by the signal autoinducer AI-2.2 Publications

Interactioni

Subunit structurei

Associates exclusively with 100S ribosomes.

Protein-protein interaction databases

BioGridi4259283. 8 interactions.
DIPiDIP-48273N.
IntActiP0AFX0. 4 interactions.
MINTiMINT-1249576.
STRINGi511145.b3203.

Structurei

Secondary structure

1
95
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi14 – 2815Combined sources
Beta strandi35 – 439Combined sources
Beta strandi48 – 569Combined sources
Beta strandi59 – 6911Combined sources
Helixi70 – 9223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQLNMR-A1-95[»]
4V8HX-ray3.10AX/CX1-95[»]
ProteinModelPortaliP0AFX0.
SMRiP0AFX0. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AFX0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41080QH. Bacteria.
COG1544. LUCA.
HOGENOMiHOG000264773.
InParanoidiP0AFX0.
KOiK05808.
OMAiNLTGHHI.
OrthoDBiEOG618R0J.
PhylomeDBiP0AFX0.

Family and domain databases

Gene3Di3.30.160.100. 1 hit.
InterProiIPR003489. Ribosomal_S30Ae/sigma54_mod.
[Graphical view]
PfamiPF02482. Ribosomal_S30AE. 1 hit.
[Graphical view]
SUPFAMiSSF69754. SSF69754. 1 hit.
TIGRFAMsiTIGR00741. yfiA. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AFX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLNITGNNV EITEALREFV TAKFAKLEQY FDRINQVYVV LKVEKVTHTS
60 70 80 90
DATLHVNGGE IHASAEGQDM YAAIDGLIDK LARQLTKHKD KLKQH
Length:95
Mass (Da):10,750
Last modified:December 20, 2005 - v1
Checksum:i5B8F737E6E3A91AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12938 Genomic DNA. Translation: BAA02316.1.
Z27094 Genomic DNA. Translation: CAA81618.1.
U12684 Genomic DNA. Translation: AAB60164.1.
U18997 Genomic DNA. Translation: AAA58005.1.
U00096 Genomic DNA. Translation: AAC76235.1.
AP009048 Genomic DNA. Translation: BAE77247.1.
PIRiI76719.
RefSeqiNP_417670.1. NC_000913.3.
WP_001176599.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76235; AAC76235; b3203.
BAE77247; BAE77247; BAE77247.
GeneIDi947718.
KEGGiecj:JW3170.
eco:b3203.
PATRICi32121826. VBIEscCol129921_3297.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12938 Genomic DNA. Translation: BAA02316.1.
Z27094 Genomic DNA. Translation: CAA81618.1.
U12684 Genomic DNA. Translation: AAB60164.1.
U18997 Genomic DNA. Translation: AAA58005.1.
U00096 Genomic DNA. Translation: AAC76235.1.
AP009048 Genomic DNA. Translation: BAE77247.1.
PIRiI76719.
RefSeqiNP_417670.1. NC_000913.3.
WP_001176599.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQLNMR-A1-95[»]
4V8HX-ray3.10AX/CX1-95[»]
ProteinModelPortaliP0AFX0.
SMRiP0AFX0. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259283. 8 interactions.
DIPiDIP-48273N.
IntActiP0AFX0. 4 interactions.
MINTiMINT-1249576.
STRINGi511145.b3203.

Proteomic databases

EPDiP0AFX0.
PaxDbiP0AFX0.
PRIDEiP0AFX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76235; AAC76235; b3203.
BAE77247; BAE77247; BAE77247.
GeneIDi947718.
KEGGiecj:JW3170.
eco:b3203.
PATRICi32121826. VBIEscCol129921_3297.

Organism-specific databases

EchoBASEiEB1632.
EcoGeneiEG11681. hpf.

Phylogenomic databases

eggNOGiENOG41080QH. Bacteria.
COG1544. LUCA.
HOGENOMiHOG000264773.
InParanoidiP0AFX0.
KOiK05808.
OMAiNLTGHHI.
OrthoDBiEOG618R0J.
PhylomeDBiP0AFX0.

Enzyme and pathway databases

BioCyciEcoCyc:EG11681-MONOMER.
ECOL316407:JW3170-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AFX0.
PROiP0AFX0.

Family and domain databases

Gene3Di3.30.160.100. 1 hit.
InterProiIPR003489. Ribosomal_S30Ae/sigma54_mod.
[Graphical view]
PfamiPF02482. Ribosomal_S30AE. 1 hit.
[Graphical view]
SUPFAMiSSF69754. SSF69754. 1 hit.
TIGRFAMsiTIGR00741. yfiA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Physical map location of the rpoN gene of Escherichia coli."
    Imaishi H., Gomada M., Inouye S., Nakazawa A.
    J. Bacteriol. 175:1550-1551(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Molecular analysis of the operon which encodes the RNA polymerase sigma factor sigma 54 of Escherichia coli."
    Jones D.H.A., Franklin C.F.H., Thomas C.M.
    Microbiology 140:1035-1043(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Novel proteins of the phosphotransferase system encoded within the rpoN operon of Escherichia coli. Enzyme IIANtr affects growth on organic nitrogen and the conditional lethality of an erats mutant."
    Powell B.S., Court D.L., Inada T., Nakamura Y., Michotey V., Cui X., Reizer A., Saier M.H. Jr., Reizer J.
    J. Biol. Chem. 270:4822-4839(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Two proteins, YfiA and YhbH, associated with resting ribosomes in stationary phase Escherichia coli."
    Maki Y., Yoshida H., Wada A.
    Genes Cells 5:965-974(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12, FUNCTION, INTERACTION WITH 100S RIBOSOMES, INDUCTION.
  7. "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography."
    Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.
    Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: B / BL21.
  8. "DNA microarray-based identification of genes controlled by autoinducer 2-stimulated quorum sensing in Escherichia coli."
    DeLisa M.P., Wu C.-F., Wang L., Valdes J.J., Bentley W.E.
    J. Bacteriol. 183:5239-5247(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli."
    Ueta M., Yoshida H., Wada C., Baba T., Mori H., Wada A.
    Genes Cells 10:1103-1112(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GENE NAME.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  10. "Role of HPF (hibernation promoting factor) in translational activity in Escherichia coli."
    Ueta M., Ohniwa R.L., Yoshida H., Maki Y., Wada C., Wada A.
    J. Biochem. 143:425-433(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  11. "Activities of Escherichia coli ribosomes in IF3 and RMF change to prepare 100S ribosome formation on entering the stationary growth phase."
    Yoshida H., Ueta M., Maki Y., Sakai A., Wada A.
    Genes Cells 14:271-280(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Solution structure of the E. coli ribosome hibernation promoting factor HPF: Implications for the relationship between structure and function."
    Sato A., Watanabe T., Maki Y., Ueta M., Yoshida H., Ito Y., Wada A., Mishima M.
    Biochem. Biophys. Res. Commun. 389:580-585(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiHPF_ECOLI
AccessioniPrimary (citable) accession number: P0AFX0
Secondary accession number(s): P31221, Q2M909
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 16, 2016
This is version 82 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.