| IED ID |
IndEnz0002019185 |
| Enzyme Type ID |
protease019185 |
| Protein Name |
ATP-dependent protease ATPase subunit ClpY
|
| Gene Name |
clpY codX hslU BSU16160 |
| Organism |
Bacillus subtilis (strain 168) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Firmicutes
Bacilli
Bacillales
Bacillaceae
Bacillus
Bacillus subtilis group
Bacillus subtilis
Bacillus subtilis subsp. subtilis
Bacillus subtilis (strain 168)
|
| Enzyme Sequence |
MEKKPLTPRQIVDRLDQYIVGQQNAKKAVAVALRNRYRRSLLDEKLKDEVVPKNILMMGPTGVGKTEIARRIAKLSGAPFIKIEATKFTEVGYVGRDVESMVRDLVETSVRLIKEEKMNEVKEQAEENANKRIVRLLVPGKKKQSGVKNPFEMFFGGSQPNGEDEAESQEEANIEEKRKRMAHQLALGELEDYYVTVEVEEQQPSMFDMLQGSGMEQMGMNMQDALSGLMPKKKKRRKMTVREARKVLTNEEASKLIDMDEVGQEAVQRAEESGIIFIDEIDKIAKNGGASSSADVSREGVQRDILPIVEGSTVVTKYGSVKTDHVLFIAAGAFHMAKPSDLIPELQGRFPIRVELNKLTVDDFVRILVEPDNALLKQYQALLQTEGISLEFSDEAIHKIAEVAYHVNQDTDNIGARRLHTILERLLEDLSFEAPDVTMEKITITPQYVEEKLGTIAKNKDLSQFIL |
| Enzyme Length |
467 |
| Uniprot Accession Number |
P39778 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
ACTIVITY REGULATION: ATPase activity is much induced upon complex formation with ClpQ. {ECO:0000269|PubMed:11179218}. |
| Binding Site |
BINDING 20; /note=ATP; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250; BINDING 279; /note=ATP; /evidence=ECO:0000250; BINDING 345; /note=ATP; /evidence=ECO:0000250; BINDING 417; /note=ATP; /evidence=ECO:0000250 |
| Calcium Binding |
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| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| Enzyme Function |
FUNCTION: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. {ECO:0000269|PubMed:11179218}. |
| Temperature Dependency |
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| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
NP_BIND 62..67; /note=ATP; /evidence=ECO:0000250 |
| Features |
Binding site (4); Chain (1); Nucleotide binding (1) |
| Keywords |
ATP-binding;Chaperone;Cytoplasm;Nucleotide-binding;Reference proteome |
| Interact With |
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| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
| Modified Residue |
|
| Post Translational Modification |
|
| Signal Peptide |
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| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
22512862;
|
| Motif |
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| Gene Encoded By |
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| Mass |
52,586 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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