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Article

Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli.

The Journal of biological chemistry - 7 Apr 1995

Seol J H, Baek S H, Kang M S, Ha D B, Chung C H

Abstract excerpt

ClpA is the ATPase component of the ATP-dependent protease Ti (Clp) in Escherichia coli and contains two ATP-binding sites. A ClpA variant (referred to as ClpAT) carrying threonine in place of the 169th methionine has recently been shown to be highly soluble but indistinguishable from the wild-type, 84-kDa ClpA in its ability to hydrolyze ATP and to support the casein-degrading activity of ClpP. Therefore,...

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PMID: 7713911
DOI: 10.1074/jbc.270.14.8087

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

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Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli.PMID 7713911Read ↗

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