| IED ID |
IndEnz0002015104 |
| Enzyme Type ID |
protease015104 |
| Protein Name |
Heat shock protein 78, mitochondrial
|
| Gene Name |
HSP78 YDR258C YD9320A.08C |
| Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Fungi
Dikarya
Ascomycota
saccharomyceta
Saccharomycotina (true yeasts)
Saccharomycetes
Saccharomycetales
Saccharomycetaceae
Saccharomyces
Saccharomyces cerevisiae (Baker's yeast)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
| Enzyme Sequence |
MLRQATKAPIQKYLQRTQLLRRSTPRIYTIVQCKRSICSFNARPRVANKLLSDIKTNALNEVAISTCALKSSYGLPNFKRTYVQMRMDPNQQPEKPALEQFGTNLTKLARDGKLDPVIGRDEEIARAIQILSRRTKNNPCLIGRAGVGKTALIDGLAQRIVAGEVPDSLKDKDLVALDLGSLIAGAKYRGEFEERLKKVLEEIDKANGKVIVFIDEVHMLLGLGKTDGSMDASNILKPKLARGLRCISATTLDEFKIIEKDPALSRRFQPILLNEPSVSDTISILRGLKERYEVHHGVRITDTALVSAAVLSNRYITDRFLPDKAIDLVDEACAVLRLQHESKPDEIQKLDRAIMKIQIELESLKKETDPVSVERREALEKDLEMKNDELNRLTKIWDAERAEIESIKNAKANLEQARIELEKCQREGDYTKASELRYSRIPDLEKKVALSEKSKDGDKVNLLHDSVTSDDISKVVAKMTGIPTETVMKGDKDRLLYMENSLKERVVGQDEAIAAISDAVRLQRAGLTSEKRPIASFMFLGPTGTGKTELTKALAEFLFDDESNVIRFDMSEFQEKHTVSRLIGAPPGYVLSESGGQLTEAVRRKPYAVVLFDEFEKAHPDVSKLLLQVLDEGKLTDSLGHHVDFRNTIIVMTSNIGQDILLNDTKLGDDGKIDTATKNKVIEAMKRSYPPEFINRIDDILVFNRLSKKVLRSIVDIRIAEIQDRLAEKRMKIDLTDEAKDWLTDKGYDQLYGARPLNRLIHRQILNSMATFLLKGQIRNGETVRVVVKDTKLVVLPNHEEGEVVEEEAEK |
| Enzyme Length |
811 |
| Uniprot Accession Number |
P33416 |
| Absorption |
|
| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
|
| catalytic Activity |
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| DNA Binding |
|
| EC Number |
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| Enzyme Function |
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. {ECO:0000269|PubMed:11231020, ECO:0000269|PubMed:11734006, ECO:0000269|PubMed:12023279, ECO:0000269|PubMed:12237310, ECO:0000269|PubMed:16460754, ECO:0000269|PubMed:16545993, ECO:0000269|PubMed:7500331, ECO:0000269|PubMed:7628444, ECO:0000269|PubMed:8830768}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
NP_BIND 143..150; /note=ATP 1; /evidence=ECO:0000255; NP_BIND 541..548; /note=ATP 2; /evidence=ECO:0000255 |
| Features |
Chain (1); Coiled coil (1); Mutagenesis (2); Nucleotide binding (2); Region (2); Sequence conflict (5); Transit peptide (1) |
| Keywords |
ATP-binding;Chaperone;Coiled coil;Direct protein sequencing;Mitochondrion;Nucleotide-binding;Reference proteome;Repeat;Stress response;Transit peptide |
| Interact With |
P10591 |
| Induction |
INDUCTION: By heat stress. Expressed at a higher level in respiring cells than in fermenting cells (at protein level). {ECO:0000269|PubMed:16339719, ECO:0000269|PubMed:8413229}. |
| Subcellular Location |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:8413229, ECO:0000269|PubMed:8830768}. |
| Modified Residue |
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| Post Translational Modification |
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| Signal Peptide |
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| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
11409176;
12839777;
14690591;
15096560;
16429126;
16438680;
17651441;
19119411;
19536198;
20070446;
20955007;
21827755;
22319614;
22688810;
23007651;
23152898;
23212899;
23217712;
23420633;
23479443;
24240771;
25710177;
26048933;
27502399;
8631298;
9106654;
9149530;
9271106;
|
| Motif |
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| Gene Encoded By |
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| Mass |
91,336 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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