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P33416

- HSP78_YEAST

UniProt

P33416 - HSP78_YEAST

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP33416.
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

        10         20         30         40         50
MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL
60 70 80 90 100
LSDIKTNALN EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ
110 120 130 140 150
FGTNLTKLAR DGKLDPVIGR DEEIARAIQI LSRRTKNNPC LIGRAGVGKT
160 170 180 190 200
ALIDGLAQRI VAGEVPDSLK DKDLVALDLG SLIAGAKYRG EFEERLKKVL
210 220 230 240 250
EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL ARGLRCISAT
260 270 280 290 300
TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI
310 320 330 340 350
TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL
360 370 380 390 400
DRAIMKIQIE LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE
410 420 430 440 450
RAEIESIKNA KANLEQARIE LEKCQREGDY TKASELRYSR IPDLEKKVAL
460 470 480 490 500
SEKSKDGDKV NLLHDSVTSD DISKVVAKMT GIPTETVMKG DKDRLLYMEN
510 520 530 540 550
SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL GPTGTGKTEL
560 570 580 590 600
TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE
610 620 630 640 650
AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII
660 670 680 690 700
VMTSNIGQDI LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI
710 720 730 740 750
LVFNRLSKKV LRSIVDIRIA EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ
760 770 780 790 800
LYGARPLNRL IHRQILNSMA TFLLKGQIRN GETVRVVVKD TKLVVLPNHE
810
EGEVVEEEAE K
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.
InParanoidi P33416.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 136 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