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P33416

- HSP78_YEAST

UniProt

P33416 - HSP78_YEAST

Protein

Heat shock protein 78, mitochondrial

Gene

HSP78

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (23 May 2003)
      Previous versions | rss
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    Functioni

    Required, in concert with mitochondrial Hsp70 (SSC1), for the dissociation, resolubilization and refolding of aggregates of damaged proteins in the mitochondrial matrix after heat stress. May extract proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by the Hsp70 chaperone system. Required for resumption of mitochondrial respiratory function, DNA synthesis and morphology after heat stress. Its main role may be maintaining the molecular chaperone SSC1 in a soluble and functional state. Also required for the efficient degradation of proteins by matrix protease PIM1, independent on its protein remodeling activity.9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi143 – 1508ATP 1Sequence Analysis
    Nucleotide bindingi541 – 5488ATP 2Sequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. misfolded protein binding Source: SGD
    4. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to heat Source: SGD
    3. mitochondrial genome maintenance Source: SGD
    4. protein refolding Source: SGD
    5. protein stabilization Source: SGD
    6. protein unfolding Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29829-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock protein 78, mitochondrial
    Gene namesi
    Name:HSP78
    Ordered Locus Names:YDR258C
    ORF Names:YD9320A.08C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR258c.
    SGDiS000002666. HSP78.

    Subcellular locationi

    Mitochondrion matrix 4 Publications

    GO - Cellular componenti

    1. mitochondrial matrix Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491K → T: Abolishes ATPase activity. 1 Publication
    Mutagenesisi547 – 5471K → T: Impairs oligomerization. Reduces ATPase activity by 92%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4444MitochondrionSequence AnalysisAdd
    BLAST
    Chaini45 – 811767Heat shock protein 78, mitochondrialPRO_0000005500Add
    BLAST

    Proteomic databases

    MaxQBiP33416.
    PaxDbiP33416.
    PeptideAtlasiP33416.
    PRIDEiP33416.

    Expressioni

    Inductioni

    By heat stress. Expressed at a higher level in respiring cells than in fermenting cells (at protein level).2 Publications

    Gene expression databases

    GenevestigatoriP33416.

    Interactioni

    Subunit structurei

    Homohexamer, forming a ring with a central pore. The hexamer is stabilized by high protein concentrations and by ADP or ATP. Oligomerization influences ATP hydrolysis activity.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SSA1P105912EBI-8680,EBI-8591

    Protein-protein interaction databases

    BioGridi32308. 52 interactions.
    IntActiP33416. 2 interactions.
    MINTiMINT-4481700.
    STRINGi4932.YDR258C.

    Structurei

    3D structure databases

    ProteinModelPortaliP33416.
    SMRiP33416. Positions 97-794.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 344247NBD1Add
    BLAST
    Regioni467 – 658192NBD2Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili345 – 43086Sequence AnalysisAdd
    BLAST

    Domaini

    Has 2 AAA ATPase type nucleotide-binding domains (NBDs) per monomer. NBD1 is primarily responsible for ATP hydrolysis. NBD2 is crucial for oligomerization.

    Sequence similaritiesi

    Belongs to the ClpA/ClpB family.Curated

    Keywords - Domaini

    Coiled coil, Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0542.
    GeneTreeiENSGT00390000012961.
    HOGENOMiHOG000218211.
    OMAiGHHVDFR.
    OrthoDBiEOG7X6M7K.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR019489. Clp_ATPase_C.
    IPR001270. ClpA/B.
    IPR018368. ClpA/B_CS1.
    IPR028299. ClpA/B_CS2.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF07724. AAA_2. 1 hit.
    PF10431. ClpB_D2-small. 1 hit.
    [Graphical view]
    PRINTSiPR00300. CLPPROTEASEA.
    SMARTiSM00382. AAA. 2 hits.
    SM01086. ClpB_D2-small. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00870. CLPAB_1. 1 hit.
    PS00871. CLPAB_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33416-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL    50
    LSDIKTNALN EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ 100
    FGTNLTKLAR DGKLDPVIGR DEEIARAIQI LSRRTKNNPC LIGRAGVGKT 150
    ALIDGLAQRI VAGEVPDSLK DKDLVALDLG SLIAGAKYRG EFEERLKKVL 200
    EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL ARGLRCISAT 250
    TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI 300
    TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL 350
    DRAIMKIQIE LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE 400
    RAEIESIKNA KANLEQARIE LEKCQREGDY TKASELRYSR IPDLEKKVAL 450
    SEKSKDGDKV NLLHDSVTSD DISKVVAKMT GIPTETVMKG DKDRLLYMEN 500
    SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL GPTGTGKTEL 550
    TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE 600
    AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII 650
    VMTSNIGQDI LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI 700
    LVFNRLSKKV LRSIVDIRIA EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ 750
    LYGARPLNRL IHRQILNSMA TFLLKGQIRN GETVRVVVKD TKLVVLPNHE 800
    EGEVVEEEAE K 811
    Length:811
    Mass (Da):91,336
    Last modified:May 23, 2003 - v2
    Checksum:iFC080D1874877075
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061T → K in AAC37362. (PubMed:8413229)Curated
    Sequence conflicti245 – 2451R → A in AAC37362. (PubMed:8413229)Curated
    Sequence conflicti429 – 4291D → V in AAC37362. (PubMed:8413229)Curated
    Sequence conflicti549 – 5491E → K in AAC37362. (PubMed:8413229)Curated
    Sequence conflicti608 – 6081A → P in AAC37362. (PubMed:8413229)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16533 Unassigned DNA. Translation: AAC37362.1.
    Z68329 Genomic DNA. Translation: CAA92715.1.
    Z70202 Genomic DNA. Translation: CAA94097.1.
    BK006938 Genomic DNA. Translation: DAA12098.1.
    PIRiS67315.
    RefSeqiNP_010544.3. NM_001180566.3.

    Genome annotation databases

    EnsemblFungiiYDR258C; YDR258C; YDR258C.
    GeneIDi851845.
    KEGGisce:YDR258C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L16533 Unassigned DNA. Translation: AAC37362.1 .
    Z68329 Genomic DNA. Translation: CAA92715.1 .
    Z70202 Genomic DNA. Translation: CAA94097.1 .
    BK006938 Genomic DNA. Translation: DAA12098.1 .
    PIRi S67315.
    RefSeqi NP_010544.3. NM_001180566.3.

    3D structure databases

    ProteinModelPortali P33416.
    SMRi P33416. Positions 97-794.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32308. 52 interactions.
    IntActi P33416. 2 interactions.
    MINTi MINT-4481700.
    STRINGi 4932.YDR258C.

    Proteomic databases

    MaxQBi P33416.
    PaxDbi P33416.
    PeptideAtlasi P33416.
    PRIDEi P33416.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR258C ; YDR258C ; YDR258C .
    GeneIDi 851845.
    KEGGi sce:YDR258C.

    Organism-specific databases

    CYGDi YDR258c.
    SGDi S000002666. HSP78.

    Phylogenomic databases

    eggNOGi COG0542.
    GeneTreei ENSGT00390000012961.
    HOGENOMi HOG000218211.
    OMAi GHHVDFR.
    OrthoDBi EOG7X6M7K.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29829-MONOMER.

    Miscellaneous databases

    NextBioi 969757.
    PROi P33416.

    Gene expression databases

    Genevestigatori P33416.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR019489. Clp_ATPase_C.
    IPR001270. ClpA/B.
    IPR018368. ClpA/B_CS1.
    IPR028299. ClpA/B_CS2.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF07724. AAA_2. 1 hit.
    PF10431. ClpB_D2-small. 1 hit.
    [Graphical view ]
    PRINTSi PR00300. CLPPROTEASEA.
    SMARTi SM00382. AAA. 2 hits.
    SM01086. ClpB_D2-small. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00870. CLPAB_1. 1 hit.
    PS00871. CLPAB_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases."
      Leonhardt S.A., Fearon K., Danese P.N., Mason T.L.
      Mol. Cell. Biol. 13:6304-6313(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding."
      Krzewska J., Langer T., Liberek K.
      FEBS Lett. 489:92-96(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 85-90, FUNCTION.
    5. "Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70."
      Schmitt M., Neupert W., Langer T.
      EMBO J. 14:3434-3444(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function."
      Moczko M., Schoenfisch B., Voos W., Pfanner N., Rassow J.
      J. Mol. Biol. 254:538-543(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria."
      Schmitt M., Neupert W., Langer T.
      J. Cell Biol. 134:1375-1386(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein."
      Krzewska J., Konopa G., Liberek K.
      J. Mol. Biol. 314:901-910(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, ELECTRON MICROSCOPY, MUTAGENESIS OF LYS-149 AND LYS-547.
    9. "A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase."
      Germaniuk A., Liberek K., Marszalek J.
      J. Biol. Chem. 277:27801-27808(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix."
      Roettgers K., Zufall N., Guiard B., Voos W.
      J. Biol. Chem. 277:45829-45837(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN DEGRADATION.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    14. "Regulation and recovery of functions of Saccharomyces cerevisiae chaperone BiP/Kar2p after thermal insult."
      Seppae L., Makarow M.
      Eukaryot. Cell 4:2008-2016(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    15. "Hsp78 chaperone functions in restoration of mitochondrial network following heat stress."
      Lewandowska A., Gierszewska M., Marszalek J., Liberek K.
      Biochim. Biophys. Acta 1763:141-151(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress."
      von Janowsky B., Major T., Knapp K., Voos W.
      J. Mol. Biol. 357:793-807(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiHSP78_YEAST
    AccessioniPrimary (citable) accession number: P33416
    Secondary accession number(s): D6VSN8, Q12137
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 23, 2003
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2990 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3