IED ID |
IndEnz0002017398 |
Enzyme Type ID |
protease017398 |
Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpX
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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)
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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 |
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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 (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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