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 |
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Active Site |
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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 |
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Pathway |
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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 |
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Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
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 |
22512862;
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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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