IED ID |
IndEnz0002017776 |
Enzyme Type ID |
protease017776 |
Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Gene Name |
clpX BSU28220 |
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 |
MFKFNEEKGQLKCSFCGKTQDQVRKLVAGPGVYICDECIELCTEIVEEELGTEEEVEFKDVPKPQEIREILNEYVIGQDQAKKSLAVAVYNHYKRINSNSKVDDVELSKSNISLIGPTGSGKTLLAQTLARILNVPFAIADATSLTEAGYVGEDVENILLKLIQAADYDVEKAEKGIIYIDEIDKVARKSENPSITRDVSGEGVQQALLKILEGTVASVPPQGGRKHPHQEFIQIDTTNILFICGGAFDGIEQIIKRRLGQKVIGFGADNKAADLEKEDLLSKVLPEDLLRFGLIPEFIGRLPVIASLEKLDEEALVAILTKPKNALVKQFKKMLELDNVELEFEEEALSEIAKKAIERKTGARGLRSIIEGIMLDVMFELPSRDDIEKCVITGATVTHGEPPRLLLKDGTEVSQDKTSA |
Enzyme Length |
420 |
Uniprot Accession Number |
P50866 |
Absorption |
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Active Site |
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Activity Regulation |
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Binding Site |
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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: ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP (By similarity). Probably the major protease that degrades proteins tagged by trans-translation (PubMed:11395451). {ECO:0000255|HAMAP-Rule:MF_00175, ECO:0000269|PubMed:11395451}. |
Temperature Dependency |
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PH Dependency |
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Pathway |
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nucleotide Binding |
NP_BIND 117..124; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00175 |
Features |
Chain (1); Domain (1); Metal binding (4); Nucleotide binding (1); Sequence conflict (10) |
Keywords |
ATP-binding;Chaperone;Metal-binding;Nucleotide-binding;Reference proteome;Stress response;Zinc |
Interact With |
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Induction |
INDUCTION: By heat shock. {ECO:0000269|PubMed:8973311}. |
Subcellular Location |
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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 |
46,350 |
Kinetics |
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Metal Binding |
METAL 13; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 16; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 35; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 38; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250 |
Rhea ID |
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Cross Reference Brenda |
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