Chaperone protein DnaK

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ADP binding Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate."
    Bertelsen E.B., Chang L., Gestwicki J.E., Zuiderweg E.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:8471-8476(2009) [PubMed] [Europe PMC] [Abstract]
  • "The role of ATP in the functional cycle of the DnaK chaperone system."
    McCarty J.S., Buchberger A., Reinstein J., Bukau B.
    J. Mol. Biol. 249:126-137(1995) [PubMed] [Europe PMC] [Abstract]
• ATPase activity Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• ATPase activity, coupled Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• chaperone binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• misfolded protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• protein folding chaperone Source: EcoCycInferred from direct assayⁱ
  • "Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains."
    Teter S.A., Houry W.A., Ang D., Tradler T., Rockabrand D., Fischer G., Blum P., Georgopoulos C., Hartl F.U.
    Cell 97:755-765(1999) [PubMed] [Europe PMC] [Abstract]
• sigma factor antagonist activity Source: EcoCycInferred from direct assayⁱ
  • "A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32."
    Gamer J., Multhaup G., Tomoyasu T., McCarty J.S., Rudiger S., Schonfeld H.J., Schirra C., Bujard H., Bukau B.
    EMBO J. 15:607-617(1996) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• zinc ion binding Source: EcoliWikiInferred from direct assayⁱ
  • "Systematic search for zinc-binding proteins in Escherichia coli."
    Katayama A., Tsujii A., Wada A., Nishino T., Ishihama A.
    Eur. J. Biochem. 269:2403-2413(2002) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cellular response to heat Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cellular response to unfolded protein Source: EcoCycInferred from direct assayⁱ
  • "The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner."
    Skowyra D., Georgopoulos C., Zylicz M.
    Cell 62:939-944(1990) [PubMed] [Europe PMC] [Abstract]
  • "DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage."
    Schroder H., Langer T., Hartl F.U., Bukau B.
    EMBO J. 12:4137-4144(1993) [PubMed] [Europe PMC] [Abstract]
• chaperone cofactor-dependent protein refolding Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• DNA replication Source: UniProtKB-KW
• protein-containing complex assembly Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex disassembly Source: EcoCycInferred from direct assayⁱ
  • "Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda. Protein association and disassociation reactions responsible for localized initiation of replication."
    Dodson M., McMacken R., Echols H.
    J. Biol. Chem. 264:10719-10725(1989) [PubMed] [Europe PMC] [Abstract]
  • "Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage lambda DNA replication."
    Alfano C., McMacken R.
    J. Biol. Chem. 264:10709-10718(1989) [PubMed] [Europe PMC] [Abstract]
• protein refolding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to heat Source: EcoCycInferred from direct assayⁱ
  • "Positive regulatory gene for temperature-controlled proteins in Escherichia coli."
    Neidhardt F.C., VanBogelen R.A.
    Biochem. Biophys. Res. Commun. 100:894-900(1981) [PubMed] [Europe PMC] [Abstract]
  • "DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage."
    Schroder H., Langer T., Hartl F.U., Bukau B.
    EMBO J. 12:4137-4144(1993) [PubMed] [Europe PMC] [Abstract]
• response to unfolded protein Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

GO - Cellular componentⁱ

• cytoplasm Source: UniProtKBInferred from high throughput direct assayⁱ
  • "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
• cytosol Source: EcoCycInferred from direct assayⁱ
  • "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth."
    Lopez-Campistrous A., Semchuk P., Burke L., Palmer-Stone T., Brokx S.J., Broderick G., Bottorff D., Bolch S., Weiner J.H., Ellison M.J.
    Mol. Cell. Proteomics 4:1205-1209(2005) [PubMed] [Europe PMC] [Abstract]
  • "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS."
    Zhang N., Chen R., Young N., Wishart D., Winter P., Weiner J.H., Li L.
    Proteomics 7:484-493(2007) [PubMed] [Europe PMC] [Abstract]
  • "Protein abundance profiling of the Escherichia coli cytosol."
    Ishihama Y., Schmidt T., Rappsilber J., Mann M., Hartl F.U., Kerner M.J., Frishman D.
    BMC Genomics 9:102-102(2008) [PubMed] [Europe PMC] [Abstract]
• membrane Source: UniProtKBInferred from high throughput direct assayⁱ
  • "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
• plasma membrane Source: UniProtKB-SubCell
• protein-containing complex Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypeⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• chaperone binding Source: CAFAInferred from physical interactionⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]
• heat shock protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• misfolded protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding Source: CAFAInferred from direct assayⁱ
  • "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK."
    Harrison C.J., Hayer-Hartl M., di Liberto M., Hartl F.-U., Kuriyan J.
    Science 276:431-435(1997) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV 
        60         70         80         90        100
GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD 
       110        120        130        140        150
AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ 
       160        170        180        190        200
RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF 
       210        220        230        240        250
DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI 
       260        270        280        290        300
DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV 
       310        320        330        340        350
TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ 
       360        370        380        390        400
KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG 
       410        420        430        440        450
IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD 
       460        470        480        490        500
NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT 
       510        520        530        540        550
IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV 
       560        570        580        590        600
EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME 
       610        620        630 
IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK              

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

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