| IED ID |
IndEnz0002016949 |
| Enzyme Type ID |
protease016949 |
| Protein Name |
ATP-dependent Clp protease ATP-binding subunit ClpC
|
| Gene Name |
clpC SAOUHSC_00505 |
| Organism |
Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Terrabacteria group
Firmicutes
Bacilli
Bacillales
Staphylococcaceae
Staphylococcus
Staphylococcus aureus
Staphylococcus aureus (strain NCTC 8325 / PS 47)
|
| Enzyme Sequence |
MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGHGQDHVGTLHYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGNPEMSNKNAQASKSNNTPTLDSLARDLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKDKRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATTLDEYRKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLIDEASSKVRLKSHTTPNNLKEIEQEIEKVKNEKDAAVHAQEFENAANLRDKQTKLEKQYEEAKNEWKNAQNGMSTSLSEEDIAEVIAGWTGIPLTKINETESEKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTIIIMTSNVGAQELQDQRFAGFGGSSDGQDYETIRKTMLKELKNSFRPEFLNRVDDIIVFHKLTKEELKEIVTMMVNKLTNRLSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVTVDHDGKEFKYDIAEQTSETKTPSQA |
| Enzyme Length |
818 |
| Uniprot Accession Number |
Q2G0P5 |
| 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: Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. {ECO:0000269|PubMed:15554981}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
NP_BIND 208..215; /note=ATP; /evidence=ECO:0000255; NP_BIND 545..552; /note=ATP; /evidence=ECO:0000255 |
| Features |
Chain (1); Domain (2); Nucleotide binding (2); Region (4) |
| Keywords |
3D-structure;ATP-binding;Chaperone;Nucleotide-binding;Reference proteome;Repeat;Stress response;Virulence |
| Interact With |
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| Induction |
INDUCTION: By heat shock. Transcriptionally regulated by CtsR (PubMed:15554981). Up-regulated by heavy metals such as Cu(2+) and Cd(2+), but Zn(2+) and Co(2+) have no effect (PubMed:22126623). Forms part of an operon with ctsR, mcsA and mcsB. {ECO:0000269|PubMed:15554981, ECO:0000269|PubMed:22126623}. |
| 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 |
Electron microscopy (1) |
| Cross Reference PDB |
6EM8;
|
| Mapped Pubmed ID |
29165246;
|
| Motif |
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| Gene Encoded By |
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| Mass |
91,037 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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