Accession | TIGR00493 |
Name | clpP |
Function | ATP-dependent Clp endopeptidase, proteolytic subunit ClpP |
Gene Symbol | clpP |
Trusted Cutoff | 308.60 |
Domain Trusted Cutoff | 308.60 |
Noise Cutoff | 59.20 |
Domain Noise Cutoff | 59.20 |
Isology Type | equivalog |
EC Number | 3.4.21.92 |
HMM Length | 192 |
Mainrole Category | Protein fate |
Subrole Category | Degradation of proteins, peptides, and glycopeptides |
Gene Ontology Term | GO:0004176: ATP-dependent peptidase activity molecular_function |
| GO:0004252: serine-type endopeptidase activity molecular_function |
| GO:0006508: proteolysis biological_process |
| GO:0009368: endopeptidase Clp complex cellular_component |
Author | Anolik RT, Haft DH |
Entry Date | Apr 20 1999 2:06PM |
Last Modified | Feb 2 2012 11:16AM |
Comment | This model for the proteolytic subunit ClpP has been rebuilt to a higher stringency. In every bacterial genome with the ClpXP machine, a ClpP protein will be found that scores at least 370 by this HMM. In general, this ClpP member will be encoded adjacent to the clpX gene, as were all examples used in the seed alignment. A large fraction of genomes have one or more additional ClpP paralogs, sometimes encoded nearby and sometimes elsewhere. The stringency of the trusted cutoff used here excludes the more divergent ClpP paralogs from being called authentic ClpP by this model. |
References | DR PROSITE; PDOC00358;
SE TIGR
GA hmmls
DR HAMAP; MF_00444; 354 of 624 |
Genome Property | GenProp0251: clpXP degradation machine (HMM) |