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Information on EC 3.4.21.92 - Endopeptidase Clp and Organism(s) Pinus thunbergii and UniProt Accession P41609

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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:
Pinus thunbergii
UNIPROT: P41609 not found.
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Word Map
The taxonomic range for the selected organisms is: Pinus thunbergii
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
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ATP-dependent Clp protease
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-
-
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Caseinolytic protease
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-
-
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Clp protease
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-
-
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ClpP
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-
-
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endopeptidase Clp
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-
-
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endopeptidase Ti
-
-
-
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Heat shock protein F21.5
-
-
-
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Protease Ti
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-
-
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stress protein G7
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
110910-59-3
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131017-00-0
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131017-01-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CLPP_PINTH
196
0
21771
Swiss-Prot
other Location (Reliability: 3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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