Bacillus cereus ATP-dependent protease ATPase subunit HslU (hslU)

Product name : Bacillus cereus ATP-dependent protease ATPase subunit HslU (hslU)

Catalog number : GEN1019718.E.coli

Supplier : MBS Recombinant

Price : 2288 EUR

Size : 1000ug

More about:

Classification : VPS9 domain containing

Discovery year : 2000-09-20

Entrez Gene : caseinolytic mitochondrial matrix peptidase proteolytic subunit  (CLPP)

Entrez gene record : 9605

GenBank acession : AB018551

Gene : VPS9D1

Gene ontology - Biological process : protein homooligomerization proteolysis involved in cellular protein catabolic process

Gene ontology - Cellular component : mitochondrion mitochondrial matrix endopeptidase Clp complex

Gene ontology - Molecular function : serine-type endopeptidase activity protein binding identical protein binding peptidase activity

Havana BLAST/BLAT : OTTHUMG00000173219

Identity : 13526

InterPro : ClpP/crotonase-like domain ATP-dependent Clp protease proteolytic subunit  (VPS9D1) ClpP, histidine active site ClpP, Ser active site Clp protease proteolytic subunit /Translocation-enhancing protein TepA

Locus : 16q24.3

Long gene name : VPS9 domain containing 1

PubMed : Observational study of gene-disease association. (HuGE Navigator) the N-terminal peptide of ClpP is a structural component of the substrate translocation channel and may play an important functional role as well hClpX can regulate the appearance of hClpP peptidase activity in mitochondria and might affect the nature of the degradation products released during ATP-dependent proteolytic cycles We propose that decreased levels of mitochondrial proteases Lon and ClpP may allow heat shock protein 60 substrate proteins to go through more folding attempts Perrault syndrome is caused by recessive mutations in CLPP. Optical trapping to assay single-molecule ClpXP unfolding and translocation of substrates consisting of domains with varying stabilities and sequences; find that ClpXP unfolds most domains by a single pathway, with kinetics that depend on the native fold and structural stability. ClpP proteases from E. coli, S. aureus, and human mitochondria exhibit preferences for certain amino acids in the P1, P2, and P3 positions . ere we present eight families affected by Perrault syndrome. In five families we identified novel or previously reported variants in HSD17B4, LARS2, CLPP and C10orf2 Data indicate endopeptidase Clp (ClpP) mutation identified in two patients with Perrault syndrome type 3 in a Turkish family. Data suggest that tumors exploit ClpXP-directed proteostasis to maintain mitochondrial bioenergetics, buffer oxidative stress, and enable metastatic competence.

Pubmed identfication : 10231027

RefSeq identity : NM_004913

Synonyms : ATP-BL

Synonyms gene : C16orf7

Synonyms gene name : chromosome 16 open reading frame 7