Chaperone protein HtpG

<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

Sites

<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

• ATPase activity Source: CACAO <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity."
    Motojima-Miyazaki Y., Yoshida M., Motojima F.
    Biochem Biophys Res Commun 400:241-245(2010) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: UniProtKB-UniRule
• chaperone binding Source: EcoCyc <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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling."
    Genest O., Hoskins J.R., Camberg J.L., Doyle S.M., Wickner S.
    Proc Natl Acad Sci U S A 108:8206-8211(2011) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.13

    "Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding."
    Huai Q., Wang H., Liu Y., Kim H.Y., Toft D., Ke H.
    Structure 13:579-590(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-559 IN COMPLEX WITH ATP, CATALYTIC ACTIVITY.
  • "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]
  • "Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90."
    Krukenberg K.A., Forster F., Rice L.M., Sali A., Agard D.A.
    Structure 16:755-765(2008) [PubMed] [Europe PMC] [Abstract]
  • "The binary protein-protein interaction landscape of Escherichia coli."
    Rajagopala S.V., Sikorski P., Kumar A., Mosca R., Vlasblom J., Arnold R., Franca-Koh J., Pakala S.B., Phanse S., Ceol A., Hauser R., Siszler G., Wuchty S., Emili A., Babu M., Aloy P., Pieper R., Uetz P.
    Nat Biotechnol 32:285-290(2014) [PubMed] [Europe PMC] [Abstract]
• protein folding chaperone Source: EcoCycInferred from direct assayⁱ
  • "Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling."
    Genest O., Hoskins J.R., Camberg J.L., Doyle S.M., Wickner S.
    Proc Natl Acad Sci U S A 108:8206-8211(2011) [PubMed] [Europe PMC] [Abstract]
• unfolded protein binding 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%2Dgo%2Devidence%2Dcodes#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 Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• ATP-dependent chaperone mediated protein folding Source: EcoCycInferred from direct assayⁱ
  • "Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling."
    Genest O., Hoskins J.R., Camberg J.L., Doyle S.M., Wickner S.
    Proc Natl Acad Sci U S A 108:8206-8211(2011) [PubMed] [Europe PMC] [Abstract]
• cellular response to DNA damage stimulus Source: EcoliWiki <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Over 1000 genes are involved in the DNA damage response of Escherichia coli."
    Khil P.P., Camerini-Otero R.D.
    Mol Microbiol 44:89-105(2002) [PubMed] [Europe PMC] [Abstract]
• FtsZ-dependent cytokinesis Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Hsp90 of <i>E. coli</i> modulates assembly of FtsZ, the bacterial tubulin homolog."
    Balasubramanian A., Markovski M., Hoskins J.R., Doyle S.M., Wickner S.
    Proc Natl Acad Sci U S A 116:12285-12294(2019) [PubMed] [Europe PMC] [Abstract]
• protein folding Source: EcoCycInferred from mutant phenotypeⁱ
  • "ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells."
    Thomas J.G., Baneyx F.
    Mol Microbiol 36:1360-1370(2000) [PubMed] [Europe PMC] [Abstract]
• response to heat Source: EcoliWikiInferred from expression patternⁱ
  • "Characterization of twenty-six new heat shock genes of Escherichia coli."
    Chuang S.E., Blattner F.R.
    J. Bacteriol. 175:5242-5252(1993) [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

<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

• UniProt annotation
• GO - Cellular component

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

Miscellaneous databases

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• chaperone binding Source: EcoCycInferred from physical interactionⁱ
  • "Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling."
    Genest O., Hoskins J.R., Camberg J.L., Doyle S.M., Wickner S.
    Proc Natl Acad Sci U S A 108:8206-8211(2011) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.13

    "Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding."
    Huai Q., Wang H., Liu Y., Kim H.Y., Toft D., Ke H.
    Structure 13:579-590(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-559 IN COMPLEX WITH ATP, CATALYTIC ACTIVITY.
  • "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]
  • "Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90."
    Krukenberg K.A., Forster F., Rice L.M., Sali A., Agard D.A.
    Structure 16:755-765(2008) [PubMed] [Europe PMC] [Abstract]
  • "The binary protein-protein interaction landscape of Escherichia coli."
    Rajagopala S.V., Sikorski P., Kumar A., Mosca R., Vlasblom J., Arnold R., Franca-Koh J., Pakala S.B., Phanse S., Ceol A., Hauser R., Siszler G., Wuchty S., Emili A., Babu M., Aloy P., Pieper R., Uetz P.
    Nat Biotechnol 32:285-290(2014) [PubMed] [Europe PMC] [Abstract]
• unfolded 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 Bioinform 12:449-462(2011) [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

Region

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

        10         20         30         40         50
MKGQETRGFQ SEVKQLLHLM IHSLYSNKEI FLRELISNAS DAADKLRFRA 
        60         70         80         90        100
LSNPDLYEGD GELRVRVSFD KDKRTLTISD NGVGMTRDEV IDHLGTIAKS 
       110        120        130        140        150
GTKSFLESLG SDQAKDSQLI GQFGVGFYSA FIVADKVTVR TRAAGEKPEN 
       160        170        180        190        200
GVFWESAGEG EYTVADITKE DRGTEITLHL REGEDEFLDD WRVRSIISKY 
       210        220        230        240        250
SDHIALPVEI EKREEKDGET VISWEKINKA QALWTRNKSE ITDEEYKEFY 
       260        270        280        290        300
KHIAHDFNDP LTWSHNRVEG KQEYTSLLYI PSQAPWDMWN RDHKHGLKLY 
       310        320        330        340        350
VQRVFIMDDA EQFMPNYLRF VRGLIDSSDL PLNVSREILQ DSTVTRNLRN 
       360        370        380        390        400
ALTKRVLQML EKLAKDDAEK YQTFWQQFGL VLKEGPAEDF ANQEAIAKLL 
       410        420        430        440        450
RFASTHTDSS AQTVSLEDYV SRMKEGQEKI YYITADSYAA AKSSPHLELL 
       460        470        480        490        500
RKKGIEVLLL SDRIDEWMMN YLTEFDGKPF QSVSKVDESL EKLADEVDES 
       510        520        530        540        550
AKEAEKALTP FIDRVKALLG ERVKDVRLTH RLTDTPAIVS TDADEMSTQM 
       560        570        580        590        600
AKLFAAAGQK VPEVKYIFEL NPDHVLVKRA ADTEDEAKFS EWVELLLDQA 
       610        620 
LLAERGTLED PNLFIRRMNQ LLVS                             

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

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