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Literature summary for 3.4.21.92 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
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 tobacco
-
Oryza sativa P0C312 rice
-
Paracoccus denitrificans P54414
-
-
Pinus contorta P36387
-
-
Pinus thunbergii P41609
-
-
Populus tremula
-
x tremuloides
-
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.
-
strain PCC 7942-3
-
Synechococcus sp. O34125 strain PCC 7942-2
-
Synechococcus sp. P54415 strain PCC 7942-1
-
Synechocystis sp. P54416 strain PCC 6803-1
-
Synechocystis sp. P74467 strain PCC 6803-3
-
Synechocystis sp. Q59993 strain PCC 6803-2
-
Treponema pallidum O84003
-
-
Triticum aestivum P24064
-
-
Yersinia enterocolitica O30612
-
-
Yersinia enterocolitica Q60107
-
-
Zea mays P12340 corn, maize
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
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
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
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