Accession | TIGR03692 |
Name | ATP_dep_HslV |
Function | ATP-dependent protease HslVU, peptidase subunit |
Gene Symbol | hslV |
Trusted Cutoff | 157.75 |
Domain Trusted Cutoff | 157.75 |
Noise Cutoff | 94.90 |
Domain Noise Cutoff | 94.90 |
Isology Type | equivalog |
EC Number | 3.4.25.2 |
HMM Length | 171 |
Mainrole Category | Protein fate |
Subrole Category | Degradation of proteins, peptides, and glycopeptides |
Gene Ontology Term | GO:0004176: ATP-dependent peptidase activity molecular_function |
| GO:0004298: threonine-type endopeptidase activity molecular_function |
| GO:0006508: proteolysis biological_process |
| GO:0009376: HslUV protease complex cellular_component |
Author | Haft DH |
Entry Date | Nov 6 2008 2:43PM |
Last Modified | Dec 12 2011 10:41PM |
Comment | The ATP-dependent protease HslVU, a complex of hexameric HslU active as a protein-unfolding ATPase and dodecameric HslV, the catalytic threonine protease. |
References | RN [1]
RM PMID:15849200
RT Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase.
RA Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, Song JJ, Bang O, Seol JH, Wang J, Eom SH, Chung CH
RL J Biol Chem. 2005 Jun 17;280(24):22892-8. Epub 2005 Apr 22.
RN [2]
RM PMID:12446803
RT Eubacterial HslV and HslU subunits homologs in primordial eukaryotes.
RA Couvreur B, Wattiez R, Bollen A, Falmagne P, Le Ray D, Dujardin JC
RL Mol Biol Evol. 2002 Dec;19(12):2110-7. |
Genome Property | GenProp0835: ATP-dependent protease HslVU (HMM) |