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P33416 (HSP78_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock protein 78, mitochondrial
Gene names
Name:HSP78
Ordered Locus Names:YDR258C
ORF Names:YD9320A.08C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length811 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.15 Ref.16

Subunit structure

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. Ref.8

Subcellular location

Mitochondrion matrix Ref.1 Ref.7 Ref.11 Ref.13.

Induction

By heat stress. Expressed at a higher level in respiring cells than in fermenting cells (at protein level). Ref.1 Ref.14

Domain

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

Miscellaneous

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

Sequence similarities

Belongs to the ClpA/ClpB family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSA1P105912EBI-8680,EBI-8591

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4444Mitochondrion Potential
Chain45 – 811767Heat shock protein 78, mitochondrial
PRO_0000005500

Regions

Nucleotide binding143 – 1508ATP 1 Potential
Nucleotide binding541 – 5488ATP 2 Potential
Region98 – 344247NBD1
Region467 – 658192NBD2
Coiled coil345 – 43086 Potential

Experimental info

Mutagenesis1491K → T: Abolishes ATPase activity. Ref.8
Mutagenesis5471K → T: Impairs oligomerization. Reduces ATPase activity by 92%. Ref.8
Sequence conflict1061T → K in AAC37362. Ref.1
Sequence conflict2451R → A in AAC37362. Ref.1
Sequence conflict4291D → V in AAC37362. Ref.1
Sequence conflict5491E → K in AAC37362. Ref.1
Sequence conflict6081A → P in AAC37362. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33416 [UniParc].

Last modified May 23, 2003. Version 2.
Checksum: FC080D1874877075

FASTA81191,336
        10         20         30         40         50         60 
MLRQATKAPI QKYLQRTQLL RRSTPRIYTI VQCKRSICSF NARPRVANKL LSDIKTNALN 

        70         80         90        100        110        120 
EVAISTCALK SSYGLPNFKR TYVQMRMDPN QQPEKPALEQ FGTNLTKLAR DGKLDPVIGR 

       130        140        150        160        170        180 
DEEIARAIQI LSRRTKNNPC LIGRAGVGKT ALIDGLAQRI VAGEVPDSLK DKDLVALDLG 

       190        200        210        220        230        240 
SLIAGAKYRG EFEERLKKVL EEIDKANGKV IVFIDEVHML LGLGKTDGSM DASNILKPKL 

       250        260        270        280        290        300 
ARGLRCISAT TLDEFKIIEK DPALSRRFQP ILLNEPSVSD TISILRGLKE RYEVHHGVRI 

       310        320        330        340        350        360 
TDTALVSAAV LSNRYITDRF LPDKAIDLVD EACAVLRLQH ESKPDEIQKL DRAIMKIQIE 

       370        380        390        400        410        420 
LESLKKETDP VSVERREALE KDLEMKNDEL NRLTKIWDAE RAEIESIKNA KANLEQARIE 

       430        440        450        460        470        480 
LEKCQREGDY TKASELRYSR IPDLEKKVAL SEKSKDGDKV NLLHDSVTSD DISKVVAKMT 

       490        500        510        520        530        540 
GIPTETVMKG DKDRLLYMEN SLKERVVGQD EAIAAISDAV RLQRAGLTSE KRPIASFMFL 

       550        560        570        580        590        600 
GPTGTGKTEL TKALAEFLFD DESNVIRFDM SEFQEKHTVS RLIGAPPGYV LSESGGQLTE 

       610        620        630        640        650        660 
AVRRKPYAVV LFDEFEKAHP DVSKLLLQVL DEGKLTDSLG HHVDFRNTII VMTSNIGQDI 

       670        680        690        700        710        720 
LLNDTKLGDD GKIDTATKNK VIEAMKRSYP PEFINRIDDI LVFNRLSKKV LRSIVDIRIA 

       730        740        750        760        770        780 
EIQDRLAEKR MKIDLTDEAK DWLTDKGYDQ LYGARPLNRL IHRQILNSMA TFLLKGQIRN 

       790        800        810 
GETVRVVVKD TKLVVLPNHE EGEVVEEEAE K 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L16533 Unassigned DNA. Translation: AAC37362.1.
Z68329 Genomic DNA. Translation: CAA92715.1.
Z70202 Genomic DNA. Translation: CAA94097.1.
BK006938 Genomic DNA. Translation: DAA12098.1.
PIRS67315.
RefSeqNP_010544.3. NM_001180566.3.

3D structure databases

ProteinModelPortalP33416.
SMRP33416. Positions 6-797.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32308. 52 interactions.
IntActP33416. 2 interactions.
MINTMINT-4481700.
STRING4932.YDR258C.

Proteomic databases

PaxDbP33416.
PeptideAtlasP33416.
PRIDEP33416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR258C; YDR258C; YDR258C.
GeneID851845.
KEGGsce:YDR258C.

Organism-specific databases

CYGDYDR258c.
SGDS000002666. HSP78.

Phylogenomic databases

eggNOGCOG0542.
GeneTreeENSGT00390000012961.
HOGENOMHOG000218211.
OMAQKIMVEP.
OrthoDBEOG7X6M7K.

Enzyme and pathway databases

BioCycYEAST:G3O-29829-MONOMER.

Gene expression databases

GenevestigatorP33416.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
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]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969757.
PROP33416.

Entry information

Entry nameHSP78_YEAST
AccessionPrimary (citable) accession number: P33416
Secondary accession number(s): D6VSN8, Q12137
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 23, 2003
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families