| IED ID |
IndEnz0002017398 |
| Enzyme Type ID |
protease017398 |
| Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpX
|
| Gene Name |
clpX CCNA_02039 |
| Organism |
Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Alphaproteobacteria
Caulobacterales
Caulobacteraceae
Caulobacter
Caulobacter vibrioides (Caulobacter crescentus)
Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
|
| Enzyme Sequence |
MTKAASGDTKSTLYCSFCGKSQHEVRKLIAGPTVFICDECVELCMDIIREEHKIAFVKSKDGVPTPREICEVLDDYVIGQGHAKKVLAVAVHNHYKRLNHASKNNDVELAKSNILLVGPTGTGKTLLAQTLARIIDVPFTMADATTLTEAGYVGEDVENIVLKLLQAADYNVERAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKIMEGTVASVPPQGGRKHPQQEFLQVDTTNILFICGGAFAGLEKIISARGAAKSIGFGAKVTDPEERRTGEILRNVEPDDLQRFGLIPEFIGRLPVVATLEDLDEAALVKILTEPKNAFVKQYQRLFEMENIGLTFTEDALHQVAKKAIARKTGARGLRSIMEGILLETMFELPTYEGVEEVVVNAEVVEGRAQPLLIYAEKKGGAASA |
| Enzyme Length |
420 |
| Uniprot Accession Number |
B8GX14 |
| 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 |
|
| 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 (By similarity). It directs the protease to specific substrates (By similarity). Required for degradation of response regulator CtrA, thus contributing to the G1-to-S transition (PubMed:9755166). Required to degrade DNA replication inhibitor toxin SocB, this function is probably the reason why the protease is essential in this organism (PubMed:24239291). Can perform chaperone functions in the absence of ClpP (By similarity). {ECO:0000255|HAMAP-Rule:MF_00175, ECO:0000269|PubMed:24239291, ECO:0000269|PubMed:9755166}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
NP_BIND 119..126; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00175 |
| Features |
Chain (1); Domain (1); Metal binding (4); Mutagenesis (2); Nucleotide binding (1); Region (1) |
| Keywords |
ATP-binding;Chaperone;Metal-binding;Nucleotide-binding;Reference proteome;Zinc |
| Interact With |
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| Induction |
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| 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 |
- |
| Motif |
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| Gene Encoded By |
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| Mass |
45,860 |
| Kinetics |
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| Metal Binding |
METAL 15; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 18; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 37; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 40; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250 |
| Rhea ID |
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| Cross Reference Brenda |
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