| Accession | TIGR00382 |
| Name | clpX |
| Function | ATP-dependent Clp protease, ATP-binding subunit ClpX |
| Gene Symbol | clpX |
| Trusted Cutoff | 370.75 |
| Domain Trusted Cutoff | 370.75 |
| Noise Cutoff | 178.75 |
| Domain Noise Cutoff | 178.75 |
| Isology Type | equivalog |
| HMM Length | 414 |
| Mainrole Category | Protein fate |
| Subrole Category | Protein folding and stabilization |
| Gene Ontology Term | GO:0004252: serine-type endopeptidase activity molecular_function |
| | GO:0005524: ATP binding molecular_function |
| | GO:0006508: proteolysis biological_process |
| | GO:0009368: endopeptidase Clp complex cellular_component |
| | GO:0051082: unfolded protein binding molecular_function |
| Author | Loftus BJ |
| Entry Date | Apr 20 1999 2:06PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. |
| References | DR SWISSPROT; P33138;
DR ECOCYC; EG10159; clpX;
DR PROSITE; PDOC00358;
RN [1]
RM 98241620
RT Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP.
RN [2]
RM 98254126
SE TIGR
GA hmmls
AL clustalw, belvu
DR HAMAP; MF_00175; 433 of 438 |
| Genome Property | GenProp0251: clpXP degradation machine (HMM) |
