| Accession | TIGR00390 |
| Name | hslU |
| Function | ATP-dependent protease HslVU, ATPase subunit |
| Gene Symbol | hslU |
| Trusted Cutoff | 362.45 |
| Domain Trusted Cutoff | 362.45 |
| Noise Cutoff | 225.25 |
| Domain Noise Cutoff | 225.25 |
| Isology Type | equivalog |
| HMM Length | 441 |
| Mainrole Category | Protein fate |
| Subrole Category | Protein folding and stabilization |
| Gene Ontology Term | GO:0004176: ATP-dependent peptidase activity molecular_function |
| | GO:0005524: ATP binding molecular_function |
| | GO:0006508: proteolysis biological_process |
| | GO:0009376: HslUV protease complex cellular_component |
| Author | Loftus BJ |
| Entry Date | Apr 20 1999 2:08PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model represents the ATPase subunit of HslVU, while the proteasome-related peptidase subunit is HslV. Residues 54-61 of the model contain a P-loop ATP-binding motif. Cys-287 of E. coli (position 308 in the seed alignment), studied in MEDLINE:98389714, is Ser in other members of the seed alignment. |
| References | DR ECOCYC; EG11881; hslU;
RN [1]
RM 98389714
RT The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase.
RA Seol JH, Yoo SJ, Shin DH, Shim YK, Kang MS, Goldberg AL, Chung CH
RL Eur J Biochem 1997 Aug 1;247(3):1143-50
RN [2]
RM 98389714
RT Effects of the Cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis.
RA Yoo SJ, Kim HH, Shin DH, Lee CS, Seong IS, Seol JH, Shimbara N, Tanaka K, Chung CH
RL J Biol Chem 1998 Sep 4;273(36):22929-35
SE TIGR
GA hmmls
DR HAMAP; MF_00249; 280 of 286 |
| Genome Property | GenProp0835: ATP-dependent protease HslVU (HMM) |
