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Article

Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.

The Journal of biological chemistry - 25 Jul 1990

Maurizi M R, Clark W P, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S

Abstract excerpt

The ATP-dependent Clp protease of Escherichia coli contains two dissimilar components: the Clp A regulatory polypeptide, with two ATP binding sites and intrinsic ATPase activity, and the Clp P subunit, which contains the proteolytic active site. The DNA sequence of the clpP gene predicts a protein of 207 amino acids (Mr 21,679), which is in close agreement with the size determined by sodium dodecyl sulfate-gel...

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PMID: 2197275

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli.PMID 2197275Read ↗

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