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Information on EC 3.4.21.92 - Endopeptidase Clp

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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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UNIPROT: P9WPC9 not found.
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Word Map
The enzyme appears in 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
ATP-dependent Clp protease
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Caseinolytic protease
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Clp protease
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ClpP
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endopeptidase Clp
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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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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ClpS
adaptor protein ClpS is inhibitory to ClpC1. the unfolding rate of substrates shows a a nearly three-fold for conditions lacking ClpS relative to conditions with ClpS in excess
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
ClpC1-catalyzed unfolding of an SsrA-tagged protein is negatively impacted by association with the ClpS adaptor protein. ClpS-dependent inhibition of ClpC1-catalyzed SsrA-dependent protein unfolding does not require the ClpC1 N-terminal domain but instead requires the presence of an interaction surface located in the ClpC1 middle domain
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CLPC1_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
848
0
93552
Swiss-Prot
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marsee, J.D.; Ridings, A.; Yu, T.; Miller, J.M.
Mycobacterium tuberculosis ClpC1 N-terminal domain is dispensable for adaptor protein-dependent allosteric regulation
Int. J. Mol. Sci.
19
3651
2018
Mycobacterium tuberculosis (P9WPC9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPC9)
Manually annotated by BRENDA team