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Literature summary extracted from

  • Porankiewicz, J.; Wang, J.; Clarke, A.K.
    New insights into the ATP-dependent Clp protease: Escherichia coli and beyond (1999), Mol. Microbiol., 32, 449-458.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.92 Clp sequenced Pseudomonas aeruginosa
3.4.21.92 Clp sequenced Rhodobacter capsulatus
3.4.21.92 Clp sequenced Enterococcus faecalis
3.4.21.92 Clp sequenced Streptococcus pyogenes
3.4.21.92 Clp sequenced Myxococcus xanthus
3.4.21.92 Clp sequenced Streptomyces coelicolor
3.4.21.92 Clp sequenced Helicobacter pylori
3.4.21.92 Clp sequenced Synechococcus sp.
3.4.21.92 Clp sequenced Clostridium acetobutylicum
3.4.21.92 Clp sequenced Porphyromonas gingivalis
3.4.21.92 Clp sequenced Bordetella pertussis
3.4.21.92 Clp sequenced Deinococcus radiodurans
3.4.21.92 Clp sequenced Listeria monocytogenes
3.4.21.92 Clp sequenced Chlorobaculum tepidum
3.4.21.92 Clp sequenced Shewanella putrefaciens
3.4.21.92 Clp sequenced Chlamydomonas reinhardtii
3.4.21.92 Clp sequenced Chlorella vulgaris
3.4.21.92 Clp sequenced Epifagus virginiana
3.4.21.92 Clp sequenced Haemophilus influenzae
3.4.21.92 Clp sequenced Lactococcus lactis
3.4.21.92 Clp sequenced Marchantia polymorpha
3.4.21.92 Clp sequenced Bacillus subtilis
3.4.21.92 Clp sequenced Nicotiana tabacum
3.4.21.92 Clp sequenced Oryza sativa
3.4.21.92 Clp sequenced Paracoccus denitrificans
3.4.21.92 Clp sequenced Pinus contorta
3.4.21.92 Clp sequenced Pinus thunbergii
3.4.21.92 Clp sequenced Streptococcus salivarius
3.4.21.92 Clp sequenced Borreliella burgdorferi
3.4.21.92 Clp sequenced Treponema pallidum
3.4.21.92 Clp sequenced Triticum aestivum
3.4.21.92 Clp sequenced Yersinia enterocolitica
3.4.21.92 Clp sequenced Zea mays
3.4.21.92 Clp sequenced Caulobacter vibrioides
3.4.21.92 Clp sequenced Chlamydia trachomatis
3.4.21.92 Clp sequenced Chlamydomonas moewusii
3.4.21.92 Clp sequenced Aquifex aeolicus
3.4.21.92 Clp sequenced, nuclear encoded gene Arabidopsis thaliana
3.4.21.92 Clp sequenced, nuclear encoded gene Populus tremula
3.4.21.92 Clp sequenced, nuclear encoded gene Fritillaria agrestis
3.4.21.92 Clp sequenced, nuclear encoded gene Homo sapiens
3.4.21.92 Clp sequenced, nuclear encoded gene Solanum lycopersicum
3.4.21.92 Clp sequenced, nuclear encoded gene Mus musculus
3.4.21.92 Clp sequenced, nuclear encoded gene Caenorhabditis elegans
3.4.21.92 Clp sequenced, plastid encoded gene Cyanophora paradoxa
3.4.21.92 clpP gene detected Salmonella enterica subsp. enterica serovar Typhimurium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.92
-
Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.92 mitochondrion
-
Populus tremula 5739
-
3.4.21.92 mitochondrion
-
Homo sapiens 5739
-
3.4.21.92 mitochondrion
-
Mus musculus 5739
-
3.4.21.92 mitochondrion
-
Caenorhabditis elegans 5739
-
3.4.21.92 plastid
-
Chlorella vulgaris 9536
-
3.4.21.92 plastid
-
Epifagus virginiana 9536
-
3.4.21.92 plastid
-
Fritillaria agrestis 9536
-
3.4.21.92 plastid
-
Solanum lycopersicum 9536
-
3.4.21.92 plastid
-
Marchantia polymorpha 9536
-
3.4.21.92 plastid
-
Nicotiana tabacum 9536
-
3.4.21.92 plastid
-
Oryza sativa 9536
-
3.4.21.92 plastid
-
Pinus contorta 9536
-
3.4.21.92 plastid
-
Pinus thunbergii 9536
-
3.4.21.92 plastid
-
Triticum aestivum 9536
-
3.4.21.92 plastid
-
Zea mays 9536
-
3.4.21.92 plastid
-
Chlamydomonas moewusii 9536
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.21.92 Mg2+ ClpA degrades large proteins down to short peptides of 7 to 10 amino acids, the process requires both Mg2+ and ATP hydrolysis Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.21.92 additional information Bacillus subtilis ClpP linked to many activities, including sporulation, cell competence, stress tolerance and regulation of gene expression ?
-
?
3.4.21.92 additional information Escherichia coli removing of irreversibly damaged polypeptides ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.92 Aquifex aeolicus O67357
-
-
3.4.21.92 Arabidopsis thaliana P56772
-
-
3.4.21.92 Arabidopsis thaliana Q787X4
-
-
3.4.21.92 Bacillus subtilis P80244
-
-
3.4.21.92 Bordetella pertussis
-
-
-
3.4.21.92 Borreliella burgdorferi O51698
-
-
3.4.21.92 Caenorhabditis elegans Q27539
-
-
3.4.21.92 Caulobacter vibrioides B8GX16
-
-
3.4.21.92 Chlamydia trachomatis P38002
-
-
3.4.21.92 Chlamydomonas moewusii P42379
-
-
3.4.21.92 Chlamydomonas reinhardtii P42380
-
-
3.4.21.92 Chlorella vulgaris P56317
-
-
3.4.21.92 Chlorobaculum tepidum
-
-
-
3.4.21.92 Clostridium acetobutylicum
-
-
-
3.4.21.92 Cyanophora paradoxa Q36863
-
-
3.4.21.92 Deinococcus radiodurans
-
-
-
3.4.21.92 Enterococcus faecalis
-
-
-
3.4.21.92 Epifagus virginiana P30063
-
-
3.4.21.92 Escherichia coli
-
-
-
3.4.21.92 Fritillaria agrestis O49081
-
-
3.4.21.92 Haemophilus influenzae P43867
-
-
3.4.21.92 Helicobacter pylori
-
-
-
3.4.21.92 Homo sapiens Q16740
-
-
3.4.21.92 Lactococcus lactis Q9ZAB0
-
-
3.4.21.92 Listeria monocytogenes
-
-
-
3.4.21.92 Marchantia polymorpha P12208
-
-
3.4.21.92 Mus musculus O88696
-
-
3.4.21.92 Mycobacterium tuberculosis P9WPC5 and P9WPC3
-
-
3.4.21.92 Mycobacterium tuberculosis H37Rv P9WPC5 and P9WPC3
-
-
3.4.21.92 Myxococcus xanthus
-
-
-
3.4.21.92 Nicotiana tabacum P12210 tobacco
-
3.4.21.92 Oryza sativa P0C312 rice
-
3.4.21.92 Paracoccus denitrificans P54414
-
-
3.4.21.92 Pinus contorta P36387
-
-
3.4.21.92 Pinus thunbergii P41609
-
-
3.4.21.92 Populus tremula
-
x tremuloides
-
3.4.21.92 Porphyromonas gingivalis
-
-
-
3.4.21.92 Pseudomonas aeruginosa
-
-
-
3.4.21.92 Rhodobacter capsulatus
-
-
-
3.4.21.92 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
3.4.21.92 Shewanella putrefaciens
-
-
-
3.4.21.92 Solanum lycopersicum Q42886
-
-
3.4.21.92 Streptococcus pyogenes
-
-
-
3.4.21.92 Streptococcus salivarius P36398
-
-
3.4.21.92 Streptomyces coelicolor
-
-
-
3.4.21.92 Synechococcus sp.
-
strain PCC 7942-3
-
3.4.21.92 Synechococcus sp. O34125 strain PCC 7942-2
-
3.4.21.92 Synechococcus sp. P54415 strain PCC 7942-1
-
3.4.21.92 Synechocystis sp. P54416 strain PCC 6803-1
-
3.4.21.92 Synechocystis sp. P74467 strain PCC 6803-3
-
3.4.21.92 Synechocystis sp. Q59993 strain PCC 6803-2
-
3.4.21.92 Treponema pallidum O84003
-
-
3.4.21.92 Triticum aestivum P24064
-
-
3.4.21.92 Yersinia enterocolitica O30612
-
-
3.4.21.92 Yersinia enterocolitica Q60107
-
-
3.4.21.92 Zea mays P12340 corn, maize
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.92 additional information ClpP linked to many activities, including sporulation, cell competence, stress tolerance and regulation of gene expression Bacillus subtilis ?
-
?
3.4.21.92 additional information removing of irreversibly damaged polypeptides Escherichia coli ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.21.92 Clp protease
-
Salmonella enterica subsp. enterica serovar Typhimurium
3.4.21.92 Clp protease
-
Escherichia coli
3.4.21.92 Clp protease
-
Pseudomonas aeruginosa
3.4.21.92 Clp protease
-
Rhodobacter capsulatus
3.4.21.92 Clp protease
-
Enterococcus faecalis
3.4.21.92 Clp protease
-
Streptococcus pyogenes
3.4.21.92 Clp protease
-
Myxococcus xanthus
3.4.21.92 Clp protease
-
Streptomyces coelicolor
3.4.21.92 Clp protease
-
Helicobacter pylori
3.4.21.92 Clp protease
-
Clostridium acetobutylicum
3.4.21.92 Clp protease
-
Porphyromonas gingivalis
3.4.21.92 Clp protease
-
Populus tremula
3.4.21.92 Clp protease
-
Bordetella pertussis
3.4.21.92 Clp protease
-
Deinococcus radiodurans
3.4.21.92 Clp protease
-
Listeria monocytogenes
3.4.21.92 Clp protease
-
Chlorobaculum tepidum
3.4.21.92 Clp protease
-
Shewanella putrefaciens
3.4.21.92 Clp protease
-
Chlamydomonas reinhardtii
3.4.21.92 Clp protease
-
Chlorella vulgaris
3.4.21.92 Clp protease
-
Cyanophora paradoxa
3.4.21.92 Clp protease
-
Epifagus virginiana
3.4.21.92 Clp protease
-
Fritillaria agrestis
3.4.21.92 Clp protease
-
Haemophilus influenzae
3.4.21.92 Clp protease
-
Homo sapiens
3.4.21.92 Clp protease
-
Lactococcus lactis
3.4.21.92 Clp protease
-
Solanum lycopersicum
3.4.21.92 Clp protease
-
Marchantia polymorpha
3.4.21.92 Clp protease
-
Mus musculus
3.4.21.92 Clp protease
-
Bacillus subtilis
3.4.21.92 Clp protease
-
Nicotiana tabacum
3.4.21.92 Clp protease
-
Oryza sativa
3.4.21.92 Clp protease
-
Paracoccus denitrificans
3.4.21.92 Clp protease
-
Pinus contorta
3.4.21.92 Clp protease
-
Pinus thunbergii
3.4.21.92 Clp protease
-
Streptococcus salivarius
3.4.21.92 Clp protease
-
Synechococcus sp.
3.4.21.92 Clp protease
-
Synechocystis sp.
3.4.21.92 Clp protease
-
Borreliella burgdorferi
3.4.21.92 Clp protease
-
Treponema pallidum
3.4.21.92 Clp protease
-
Triticum aestivum
3.4.21.92 Clp protease
-
Yersinia enterocolitica
3.4.21.92 Clp protease
-
Zea mays
3.4.21.92 Clp protease
-
Caenorhabditis elegans
3.4.21.92 Clp protease
-
Caulobacter vibrioides
3.4.21.92 Clp protease
-
Chlamydia trachomatis
3.4.21.92 Clp protease
-
Chlamydomonas moewusii
3.4.21.92 Clp protease
-
Arabidopsis thaliana
3.4.21.92 Clp protease
-
Mycobacterium tuberculosis
3.4.21.92 Clp protease
-
Aquifex aeolicus
3.4.21.92 ClpC
-
Listeria monocytogenes
3.4.21.92 ClpQ
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
3.4.21.92 ATP ATP dependent, for full proteolytic activity ClpP must associate with one of two related ATPase subunits, ClpA or ClpX, other nucleoside triphosphates cannot substitute for ATP Escherichia coli
3.4.21.92 ATP ATP dependent, for full proteolytic activity ClpP must associate with one of two related ATPase subunits, ClpA or ClpX, other nucleoside triphosphates cannot substitute for ATP Bacillus subtilis
3.4.21.92 ATP ATP dependent, for full proteolytic activity ClpP must associate with one of two related ATPase subunits, ClpA or ClpX, other nucleoside triphosphates cannot substitute for ATP Yersinia enterocolitica