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Links from Protein

Items: 5

1.

ATP-dependent Clp protease proteolytic subunit

The Clp protease has an active site catalytic triad. In E. coli Clp protease, ser-111, his-136 and asp-185 form the catalytic triad. Swiss:P48254 has lost all of these active site residues and is therefore inactive. Swiss:P42379 contains two large insertions, Swiss:P42380 contains one large insertion. [1]. 9390554. The structure of ClpP at 2.3 angstroms resolution suggests a. model for ATP-dependent proteolysis.. Wang J, Hartling JA, Flanagan JM;. Cell 1997;91:447-456. (from Pfam)

Date:
2024-08-14
Family Accession:
NF012783.5
Method:
HMM
2.

head maturation protease, ClpP-related

Members of this family may be found as free-standing proteins that are phage head maturation proteases, or as the N-terminal domain of phage fusion proteins that include a longer major capsid protein region.

GO Terms:
Molecular Function:
serine-type peptidase activity (GO:0008236)
Biological Process:
viral procapsid maturation (GO:0046797)
Date:
2023-12-08
Family Accession:
NF045542.1
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.

Clp protease ClpP

Clp protease ClpP is a serine protease, involved in several cellular processes such as degradation of misfolded proteins, regulation of short-lived proteins and housekeeping removal of dysfunctional proteins

Date:
2022-11-01
Family Accession:
10161508
Method:
Sparcle
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