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Information on EC 3.4.21.92 - Endopeptidase Clp and Organism(s) Homo sapiens and UniProt Accession Q16740

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.92 Endopeptidase Clp
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This record set is specific for:
Homo sapiens
UNIPROT: Q16740 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins to small peptides in the presence of ATP and Mg2+. alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolysed (such as succinyl-Leu-Tyr-/-NHMec, and Leu-Tyr-Leu-/-Tyr-Trp, in which cleavage of the -Tyr-/-Leu- and -Tyr-/-Trp bonds also occurs)
Synonyms
clp protease, clpap, clpxp protease, clpc1, clpp1, caseinolytic protease, clpp protease, clpp2, clpp1p2, atp-dependent clp protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Clp protease
-
ATP-dependent Clp protease
-
-
-
-
Caseinolytic protease
-
-
-
-
Clp protease
ClpP
-
-
-
-
endopeptidase Clp
-
-
-
-
endopeptidase Ti
-
-
-
-
Heat shock protein F21.5
-
-
-
-
Protease Ti
-
-
-
-
stress protein G7
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
110910-59-3
-
131017-00-0
-
131017-01-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
reduced level of the Lon and ClpP proteins in SPG13 patient cells as compared with controls
Manually annotated by BRENDA team
reduced level of the Lon and ClpP proteins in SPG13 patient cells as compared with controls
Manually annotated by BRENDA team
additional information
decreased expression of the mitochondrial protein quality control proteases Lon and ClpP, both at the RNA and protein level, in patients with an autosomal dominant form of hereditary spastic paraplegia (SPG13)
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
reducing the levels of mitochondrial ClpP or ClpX renders human cancer cells more sensitive to cisplatin. Overexpression of ClpP desensitizes cells to cisplatin. Cisplatin resistance correlates with decreased cellular accumulation of cisplatin and decreased levels of diguanosine-cisplatin adducts in both mitochondrial and genomic DNA. Higher levels of cisplatin-DNA adducts are found in cells in which ClpP has been depleted. Changes in the levels of ClpP have no effect on the levels of copper transporter CTR1. The levels of copper efflux pumps ATP7A and ATP7B are increased when ClpPwas overexpressed
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CLPP_HUMAN
277
0
30180
Swiss-Prot
Mitochondrion (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heptamer
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ClpP structures have been solved from five different organisms, human ClpP can form a complex with Escherichia coli ClpX in vitro
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S97A
inactive. Overexpression has no effect on sensitivity of cells to cisplatin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Clp sequenced, nuclear encoded gene
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
reducing the levels of mitochondrial ClpP or ClpX renders human cancer cells more sensitive to cisplatin. ClpP levels are elevated in cervical carcinoma cells (KB-CP20) and hepatoma cells (BEL-7404-CP20) independently selected for cisplatin resistance
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Porankiewicz, J.; Wang, J.; Clarke, A.K.
New insights into the ATP-dependent Clp protease: Escherichia coli and beyond
Mol. Microbiol.
32
449-458
1999
Aquifex aeolicus (O67357), Arabidopsis thaliana (P56772), Arabidopsis thaliana (Q787X4), Bacillus subtilis (P80244), Bordetella pertussis, Borreliella burgdorferi (O51698), Caenorhabditis elegans (Q27539), Caulobacter vibrioides (B8GX16), Chlamydia trachomatis (P38002), Chlamydomonas moewusii (P42379), Chlamydomonas reinhardtii (P42380), Chlorella vulgaris (P56317), Chlorobaculum tepidum, Clostridium acetobutylicum, Cyanophora paradoxa (Q36863), Deinococcus radiodurans, Enterococcus faecalis, Epifagus virginiana (P30063), Escherichia coli, Fritillaria agrestis (O49081), Haemophilus influenzae (P43867), Helicobacter pylori, Homo sapiens (Q16740), Lactococcus lactis (Q9ZAB0), Listeria monocytogenes, Marchantia polymorpha (P12208), Mus musculus (O88696), Mycobacterium tuberculosis (P9WPC5 and P9WPC3), Mycobacterium tuberculosis H37Rv (P9WPC5 and P9WPC3), Myxococcus xanthus, Nicotiana tabacum (P12210), Oryza sativa (P0C312), Paracoccus denitrificans (P54414), Pinus contorta (P36387), Pinus thunbergii (P41609), Populus tremula, Porphyromonas gingivalis, Pseudomonas aeruginosa, Rhodobacter capsulatus, Salmonella enterica subsp. enterica serovar Typhimurium, Shewanella putrefaciens, Solanum lycopersicum (Q42886), Streptococcus pyogenes, Streptococcus salivarius (P36398), Streptomyces coelicolor, Synechococcus sp., Synechococcus sp. (O34125), Synechococcus sp. (P54415), Synechocystis sp. (P54416), Synechocystis sp. (P74467), Synechocystis sp. (Q59993), Treponema pallidum (O84003), Triticum aestivum (P24064), Yersinia enterocolitica (O30612), Yersinia enterocolitica (Q60107), Zea mays (P12340)
Manually annotated by BRENDA team
Yu, A.Y.; Houry, W.A.
ClpP: a distinctive family of cylindrical energy-dependent serine proteases
FEBS Lett.
581
3749-3757
2007
Streptococcus pneumoniae, Escherichia coli, Homo sapiens, Mycobacterium tuberculosis, Plasmodium falciparum
Manually annotated by BRENDA team
Hansen, J.; Corydon, T.J.; Palmfeldt, J.; Duerr, A.; Fontaine, B.; Nielsen, M.N.; Christensen, J.H.; Gregersen, N.; Bross, P.
Decreased expression of the mitochondrial matrix proteases Lon and ClpP in cells from a patient with hereditary spastic paraplegia (SPG13)
Neuroscience
153
474-482
2008
Homo sapiens (Q16740)
Manually annotated by BRENDA team
Zhang, Y.; Maurizi, M.R.
Mitochondrial ClpP activity is required for cisplatin resistance in human cells
Biochim. Biophys. Acta
1862
252-264
2016
Homo sapiens (Q16740)
Manually annotated by BRENDA team