P0A6Y8
SS
Gene name |
dnaK (groP, grpF, seg, b0014, JW0013) |
Protein name |
Chaperone protein DnaK |
Names |
HSP70 , Heat shock 70 kDa protein , Heat shock protein 70 |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
ecj:JW0013, eco:b0014, |
EC number |
|
Protein Class |
|
Descriptions
HSPA8 (or hsc70) is a heat shock cognate protein involved in many cellular processes. During recovery from stress, HSPA8, initially accumulating in the nucleoplasm for folding/refolding of proteins, transiently concentrates in nucleoli for nucleolar morphology and function restoration. The inhibitory region is positioned at one of the three domains of HSPA8 protein, which is the N-terminal ATPase domain, specifically in residues 263-287 of domain IIB. Under normal growth conditions, the constitutive nucleolar targeting function that is provided by residues 225-262 is diminished by the autoinhibitory element located in residues 263-287. When cells recover from stress, the autoinhibitory element is inactivated, and the constitutive nucleolar targeting function restores.
Autoinhibitory domains (AIDs)
Target domain |
224-261 (Nucleolar targeting region) |
Relief mechanism |
Others |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
63 structures for P0A6Y8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1BPR | NMR | - | A | 384-561 | PDB |
| 1DG4 | NMR | - | A | 393-507 | PDB |
| 1DKG | X-ray | 280 A | D | 1-383 | PDB |
| 1DKX | X-ray | 200 A | A | 389-607 | PDB |
| 1DKY | X-ray | 280 A | A/B | 389-607 | PDB |
| 1DKZ | X-ray | 200 A | A | 389-607 | PDB |
| 1Q5L | NMR | - | A | 393-507 | PDB |
| 2BPR | NMR | - | A | 384-561 | PDB |
| 2KHO | NMR | - | A | 1-605 | PDB |
| 3DPO | X-ray | 210 A | A/B | 389-607 | PDB |
| 3DPP | X-ray | 250 A | A/B | 389-607 | PDB |
| 3DPQ | X-ray | 260 A | A/B/E/F | 389-601 | PDB |
| 3QNJ | X-ray | 228 A | A/B | 389-607 | PDB |
| 4B9Q | X-ray | 240 A | A/B/C/D | 1-605 | PDB |
| 4E81 | X-ray | 190 A | A/B | 389-607 | PDB |
| 4EZN | X-ray | 180 A | A/B | 389-607 | PDB |
| 4EZO | X-ray | 190 A | A/B | 389-607 | PDB |
| 4EZP | X-ray | 165 A | A/B | 389-607 | PDB |
| 4EZQ | X-ray | 200 A | A | 389-607 | PDB |
| 4EZR | X-ray | 190 A | A | 389-607 | PDB |
| 4EZS | X-ray | 190 A | A | 389-607 | PDB |
| 4EZT | X-ray | 200 A | A | 389-607 | PDB |
| 4EZU | X-ray | 190 A | A | 389-607 | PDB |
| 4EZV | X-ray | 210 A | A/B | 389-607 | PDB |
| 4EZW | X-ray | 180 A | A/B/C/D | 389-607 | PDB |
| 4EZX | X-ray | 170 A | A/B | 389-607 | PDB |
| 4EZY | X-ray | 185 A | A | 389-607 | PDB |
| 4EZZ | X-ray | 205 A | A | 389-607 | PDB |
| 4F00 | X-ray | 195 A | A | 389-607 | PDB |
| 4F01 | X-ray | 140 A | A/B | 389-607 | PDB |
| 4HY9 | X-ray | 155 A | A/B | 389-607 | PDB |
| 4HYB | X-ray | 170 A | A/B | 389-607 | PDB |
| 4JN4 | X-ray | 230 A | A/B | 2-610 | PDB |
| 4JNE | X-ray | 196 A | A/B | 2-610 | PDB |
| 4JNF | X-ray | 162 A | A | 389-610 | PDB |
| 4JWC | X-ray | 180 A | A/B | 389-607 | PDB |
| 4JWD | X-ray | 195 A | A/B | 389-607 | PDB |
| 4JWE | X-ray | 195 A | A/B | 389-607 | PDB |
| 4JWI | X-ray | 190 A | A/B | 389-607 | PDB |
| 4R5G | X-ray | 345 A | A/B | 389-607 | PDB |
| 4R5I | X-ray | 197 A | A | 389-607 | PDB |
| 4R5J | X-ray | 236 A | A/B/C/D | 389-607 | PDB |
| 4R5K | X-ray | 175 A | A/B | 389-607 | PDB |
| 4R5L | X-ray | 297 A | A/B/C/D | 389-607 | PDB |
| 5NRO | X-ray | 325 A | A | 1-605 | PDB |
| 5OOW | X-ray | 290 A | A/B | 183-383 | PDB |
| 7JMM | X-ray | 256 A | A | 389-607 | PDB |
| 7JN8 | X-ray | 309 A | A | 389-607 | PDB |
| 7JN9 | X-ray | 240 A | A | 389-607 | PDB |
| 7JNE | X-ray | 254 A | A | 389-607 | PDB |
| 7KO2 | X-ray | 264 A | A/B/C/D | 1-609 | PDB |
| 7KRT | X-ray | 279 A | A/B/C/D | 1-600 | PDB |
| 7KRU | X-ray | 182 A | A/B | 1-540 | PDB |
| 7KRV | X-ray | 192 A | A/B | 1-540 | PDB |
| 7KRW | X-ray | 770 A | A/B/C/D | 1-614 | PDB |
| 7KZI | X-ray | 282 A | A/B | 1-609 | PDB |
| 7KZU | X-ray | 215 A | A | 2-540 | PDB |
| 7N6J | X-ray | 200 A | A | 389-607 | PDB |
| 7N6K | X-ray | 255 A | A | 389-607 | PDB |
| 7N6L | X-ray | 240 A | A | 389-607 | PDB |
| 7N6M | X-ray | 182 A | A | 389-607 | PDB |
| 7RAX | X-ray | 141 A | A | 2-393 | PDB |
| AF-P0A6Y8-F1 | Predicted | AlphaFoldDB |
No variants for P0A6Y8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0A6Y8 | |||||
No associated diseases with P0A6Y8
3 regional properties for P0A6Y8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Heat shock protein 70, conserved site | 7 - 14 | IPR018181-1 |
| conserved_site | Heat shock protein 70, conserved site | 192 - 205 | IPR018181-2 |
| conserved_site | Heat shock protein 70, conserved site | 337 - 351 | IPR018181-3 |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| inclusion body | A discrete intracellular part formed of aggregated molecules such as proteins or other biopolymers. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
10 GO annotations of molecular function
| Name | Definition |
|---|---|
| ADP binding | Binding to ADP, adenosine 5'-diphosphate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction |
| ATP-dependent protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. |
| heat shock protein binding | Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. |
| protein folding chaperone | Binding to a protein or a protein-containing complex to assist the protein folding process. |
| protein-folding chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
| sigma factor antagonist activity | The function of binding to a sigma factor and stopping, preventing or reducing the rate of its transcriptional activity. |
| unfolded protein binding | Binding to an unfolded protein. |
| zinc ion binding | Binding to a zinc ion (Zn). |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to unfolded protein | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus. |
| chaperone cofactor-dependent protein refolding | The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. |
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by the origin recognition complex, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
| protein refolding | The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. |
| protein unfolding | The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state. |
| protein-containing complex assembly | The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex. |
| response to heat | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| stress response to copper ion | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis caused by a copper ion stimulus. |
61 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P11484 | SSB1 | Ribosome-associated molecular chaperone SSB1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P40150 | SSB2 | Ribosome-associated molecular chaperone SSB2 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P22202 | SSA4 | Heat shock protein SSA4 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P09435 | SSA3 | Heat shock protein SSA3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P10592 | SSA2 | Heat shock protein SSA2 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P10591 | SSA1 | Heat shock protein SSA1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | SS |
| P19120 | HSPA8 | Heat shock cognate 71 kDa protein | Bos taurus (Bovine) | SS |
| Q2YDD0 | HSPA14 | Heat shock 70 kDa protein 14 | Bos taurus (Bovine) | SS |
| P0CB32 | HSPA1L | Heat shock 70 kDa protein 1-like | Bos taurus (Bovine) | SS |
| Q27975 | HSPA1A | Heat shock 70 kDa protein 1A | Bos taurus (Bovine) | SS |
| O73885 | HSPA8 | Heat shock cognate 71 kDa protein | Gallus gallus (Chicken) | SS |
| E1C2P3 | HSPA14 | Heat shock 70 kDa protein 14 | Gallus gallus (Chicken) | SS |
| P08106 | Heat shock 70 kDa protein | Gallus gallus (Chicken) | SS | |
| P77319 | hscC | Chaperone protein HscC | Escherichia coli (strain K12) | PR |
| P29843 | Hsc70-1 | Heat shock 70 kDa protein cognate 1 | Drosophila melanogaster (Fruit fly) | SS |
| P11147 | Hsc70-4 | Heat shock 70 kDa protein cognate 4 | Drosophila melanogaster (Fruit fly) | SS |
| P11146 | Hsc70-2 | Heat shock 70 kDa protein cognate 2 | Drosophila melanogaster (Fruit fly) | SS |
| Q8INI8 | Hsp70Ba | Major heat shock 70 kDa protein Ba | Drosophila melanogaster (Fruit fly) | SS |
| Q9VG58 | Hsp70Bbb | Major heat shock 70 kDa protein Bbb | Drosophila melanogaster (Fruit fly) | SS |
| P02825 | Hsp70Ab | Major heat shock 70 kDa protein Ab | Drosophila melanogaster (Fruit fly) | SS |
| Q9BIR7 | Hsp70Bc | Major heat shock 70 kDa protein Bc | Drosophila melanogaster (Fruit fly) | SS |
| P82910 | Hsp70Aa | Major heat shock 70 kDa protein Aa | Drosophila melanogaster (Fruit fly) | SS |
| Q9BIS2 | Hsp70Bb | Major heat shock 70 kDa protein Bb | Drosophila melanogaster (Fruit fly) | SS |
| O97125 | Hsp68 | Heat shock protein 68 | Drosophila melanogaster (Fruit fly) | SS |
| A2Q0Z1 | HSPA8 | Heat shock cognate 71 kDa protein | Equus caballus (Horse) | SS |
| P11142 | HSPA8 | Heat shock cognate 71 kDa protein | Homo sapiens (Human) | EV |
| Q0VDF9 | HSPA14 | Heat shock 70 kDa protein 14 | Homo sapiens (Human) | SS |
| P11021 | HSPA5 | Endoplasmic reticulum chaperone BiP | Homo sapiens (Human) | SS |
| P54652 | HSPA2 | Heat shock-related 70 kDa protein 2 | Homo sapiens (Human) | SS |
| P34931 | HSPA1L | Heat shock 70 kDa protein 1-like | Homo sapiens (Human) | SS |
| P48741 | HSPA7 | Putative heat shock 70 kDa protein 7 | Homo sapiens (Human) | SS |
| P17066 | HSPA6 | Heat shock 70 kDa protein 6 | Homo sapiens (Human) | SS |
| P0DMV8 | HSPA1A | Heat shock 70 kDa protein 1A | Homo sapiens (Human) | SS |
| P0DMV9 | HSPA1B | Heat shock 70 kDa protein 1B | Homo sapiens (Human) | SS |
| P38646 | HSPA9 | Stress-70 protein, mitochondrial | Homo sapiens (Human) | SS |
| P11143 | HSP70 | Heat shock 70 kDa protein | Zea mays (Maize) | SS |
| P63017 | Hspa8 | Heat shock cognate 71 kDa protein | Mus musculus (Mouse) | SS |
| Q99M31 | Hspa14 | Heat shock 70 kDa protein 14 | Mus musculus (Mouse) | SS |
| P17156 | Hspa2 | Heat shock-related 70 kDa protein 2 | Mus musculus (Mouse) | SS |
| P16627 | Hspa1l | Heat shock 70 kDa protein 1-like | Mus musculus (Mouse) | SS |
| P17879 | Hspa1b | Heat shock 70 kDa protein 1B | Mus musculus (Mouse) | SS |
| Q61696 | Hspa1a | Heat shock 70 kDa protein 1A | Mus musculus (Mouse) | SS |
| Q6S4N2 | HSPA1B | Heat shock 70 kDa protein 1B | Sus scrofa (Pig) | SS |
| P63018 | Hspa8 | Heat shock cognate 71 kDa protein | Rattus norvegicus (Rat) | SS |
| P14659 | Hspa2 | Heat shock-related 70 kDa protein 2 | Rattus norvegicus (Rat) | SS |
| P55063 | Hspa1l | Heat shock 70 kDa protein 1-like | Rattus norvegicus (Rat) | SS |
| P0DMW1 | Hspa1b | Heat shock 70 kDa protein 1B | Rattus norvegicus (Rat) | SS |
| P0DMW0 | Hspa1a | Heat shock 70 kDa protein 1A | Rattus norvegicus (Rat) | SS |
| P09446 | hsp-1 | Heat shock protein hsp-1 | Caenorhabditis elegans | SS |
| P11141 | hsp-6 | Heat shock protein hsp-6 | Caenorhabditis elegans | PR |
| P26413 | HSP70 | Heat shock 70 kDa protein | Glycine max (Soybean) (Glycine hispida) | SS |
| Q9S9N1 | HSP70-5 | Heat shock 70 kDa protein 5 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P22954 | HSP70-2 | Heat shock 70 kDa protein 2 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9C7X7 | HSP70-18 | Heat shock 70 kDa protein 18 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P22953 | HSP70-1 | Heat shock 70 kDa protein 1 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| O65719 | HSP70-3 | Heat shock 70 kDa protein 3 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| Q9LHA8 | HSP70-4 | Heat shock 70 kDa protein 4 | Arabidopsis thaliana (Mouse-ear cress) | SS |
| P27322 | HSC-2 | Heat shock cognate 70 kDa protein 2 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| P24629 | HSC-I | Heat shock cognate 70 kDa protein 1 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | SS |
| Q90473 | hspa8 | Heat shock cognate 71 kDa protein | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| Q5RGE6 | hspa14 | Heat shock 70 kDa protein 14 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGKIIGIDLG | TTNSCVAIMD | GTTPRVLENA | EGDRTTPSII | AYTQDGETLV | GQPAKRQAVT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NPQNTLFAIK | RLIGRRFQDE | EVQRDVSIMP | FKIIAADNGD | AWVEVKGQKM | APPQISAEVL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KKMKKTAEDY | LGEPVTEAVI | TVPAYFNDAQ | RQATKDAGRI | AGLEVKRIIN | EPTAAALAYG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LDKGTGNRTI | AVYDLGGGTF | DISIIEIDEV | DGEKTFEVLA | TNGDTHLGGE | DFDSRLINYL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VEEFKKDQGI | DLRNDPLAMQ | RLKEAAEKAK | IELSSAQQTD | VNLPYITADA | TGPKHMNIKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TRAKLESLVE | DLVNRSIEPL | KVALQDAGLS | VSDIDDVILV | GGQTRMPMVQ | KKVAEFFGKE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PRKDVNPDEA | VAIGAAVQGG | VLTGDVKDVL | LLDVTPLSLG | IETMGGVMTT | LIAKNTTIPT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KHSQVFSTAE | DNQSAVTIHV | LQGERKRAAD | NKSLGQFNLD | GINPAPRGMP | QIEVTFDIDA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DGILHVSAKD | KNSGKEQKIT | IKASSGLNED | EIQKMVRDAE | ANAEADRKFE | ELVQTRNQGD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| HLLHSTRKQV | EEAGDKLPAD | DKTAIESALT | ALETALKGED | KAAIEAKMQE | LAQVSQKLME |
| 610 | 620 | 630 | |||
| IAQQQHAQQQ | TAGADASANN | AKDDDVVDAE | FEEVKDKK |