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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Lon protease belongs to the S16 peptidase family and is an ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins, as well as certain short-lived regulatory proteins. It is required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress [ ]. In pathogenic bacteria, it is required for the expression of virulence genes that promote cell infection [].Lon (La) protease was the first ATP-dependent protease to be purified from E. coli [, , , ]. The enzyme is a homotetramer of 87kDa subunits, with one proteolytic and one ATP-binding site per monomer, making it structurally less complex than other known ATP-dependent proteases []. Despite this relative structural simplicity, Lon recognises its substrates directly, without delegating the task of substrate recognition to other enzymes [].This signature defines the bacterial and eukaryotic lon proteases. This family of sequences does not include the archaeal lon homologues, . In the eukaryotes the majority of the proteins are located in the mitochondrial matrix [ , ]. The yeast homologue, Pim1, is required for mitochondrial function and is constitutively expressed, but is increased after thermal stress, suggesting that Pim1 may play a role in the heat shock response []. | Name | Lon protease, bacterial/eukaryotic-type |
| Short Name | Lon_bac/euk-typ | Type | Family |
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