HMM Summary Page: TIGR00390

FunctionATP-dependent protease HslVU, ATPase subunit
Gene SymbolhslU
Trusted Cutoff362.45
Domain Trusted Cutoff362.45
Noise Cutoff225.25
Domain Noise Cutoff225.25
Isology Typeequivalog
HMM Length441
Mainrole CategoryProtein fate
Subrole CategoryProtein folding and stabilization
Gene Ontology TermGO: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
AuthorLoftus BJ
Entry DateApr 20 1999 2:08PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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.
ReferencesDR 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 PropertyGenProp0835: ATP-dependent protease HslVU (HMM)