Caseinolytic proteases
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موضوع
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رقم النظام
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معلومات حول الهوية:
الاسم الرئيس (باللاتينية)
Caseinolytic proteases
صِيَغ اسمية أخرى
Caseinlytic proteinases
Clp proteases
ClpPs (Caseinolytic proteases)
Peptidase S14
موضوع ذو صلة
Molecular chaperones
Peptidase
Serine proteinases
MARC
MARC
أرقام تعريفية أخرى
Wikidata:
Q5012788
Library of congress:
sh2015000781
مصادر المعلومات
- Work cat: Li, T. Substrate recognition and translocation catalyzed by AAA+ chaperones, 2013:abstr. (Both E. coli ClpA and E. coli ClpB belong to the Clp/Hsp100 chaperone family. They share many common features, such as the same conserved motifs ..., hexameric ring-shaped structure, and double nu-cleotide binding domains. ClpA and ClpB are closely related to each other. However, they participate in different protein quality control pathways. ClpA regulates cellular functions by either associating with ClpP to form the ClpAP complex (an ATP-dependant protease) to degrade unwanted polypeptides or remodeling inactive proteins to their bio-logical active forms. ... On the other hand, ClpB cannot associate with any known peptidase for protein degradation, but it can catalyze protein disaggregation with or without the assistance of DnaK chaperone system)
- Lactic acid bacteria and bifidobacteria, 2011:p. 148 (Clp family. Within [the] caseinolytic protease (Clp) family, ClpX and ClpY possess one AAA domain (single ring architecture), while ClpA and ClpB possess two AAA domains (double ring architecture). Only a subgroup of the Clp AAA+ ATPases can interact with the protease subunit ClpP. The association of Clp AAA+ ATPases with ClpP is mediated by a conserved I/V/M-G-F/L tripeptide motif located in the surface of the AAA+ domain, which faces the subunit ClpP. In E. coli, this property is found in ClpA and ClpX but not in ClpB)
- NCBI CDD conserved protein domain S14_ClpP, via WWW, Mar. 25, 2015(Caseinolytic protease (ClpP) is an ATP-dependent, highly conserved serine protease. Clp protease (caseinolytic protease; ClpP; Peptidase S14) is a highly conserved serine protease present throughout in bacteria and eukaryota, but seems to be absent in archaea, mollicutes and some fungi. Clp proteases are involved in a number of cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins. Additionally, they are implicated in the control of cell growth, targeting DNA-binding protein from starved cells. ClpP has also been linked to the tight regulation of virulence genes in the pathogens Listeria monocytogenes and Salmonella typhimurium. This enzyme belong[s] to the family of ATP-dependent proteases. ... Conserved features/sites - active site ... Structure:1TYF: E. coli Clp protease (ClpP))
- Journal of biological chemistry, Feb. 20, 2009:p. 5208 (Proteolysis in bacterial cells is a key cellular function. ATPdependent self-compartmentalizing proteases, whose active sites are located in an inner cavity, play a dominant role in this process. Of these proteases, the serine protease caseinolytic protease (Clp) has been extensively studied both mechanistically and functionally. The Clp proteases are a crucial part of the cell's protein quality control system disposing of truncated, misfolded, aggregated, or denatured proteins. In addition, Clp performs regulatory functions controlling the abundance of certain regulatory proteins in the cell)
- Journal of ichthyology, July 2010:p. 489 (In mucosa of fish intestine, the activity of caseinlytic proteinases is higher than the activity of hemoglobinlytic proteinases)
- BMC biochemistry, 2011:v. 12, art. 61, p. 1 (Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2 ... Caseinolytic proteases (ClpPs) are barrel-shaped self-compartmentalized peptidases involved in eliminating damaged or short-lived regulatory proteins)
- Google search, Mar. 25, 2015(Caseinolytic proteases - 1,620 hits; Caseinlytic proteinases - 398 hits; Caseinolytic proteinases - 350 hits; Cpl proteases - 192 hits)