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DNA gyrase C-terminal beta-propeller domain-containing protein
This repeat is found as 6 tandem copies at the C-termini of GyrA and ParC DNA gyrases. It is predicted to form 4 beta strands and to probably form a beta-propeller structure [1]. This region has been shown to bind DNA non-specifically and may stabilise the DNA-topoisomerase complex [2]. [1]. 11948780. C-terminal domain of gyrase A is predicted to have a beta-propeller structure. Qi Y, Pei J, Grishin NV;. Proteins 2002;47:258-264. [2]. 1657531. DNA gyrase: structure and function. Reece RJ, Maxwell A;. Crit Rev Biochem Mol Biol 1991;26:335-375. (from Pfam)
DNA gyrase subunit A
DNA gyrase subunit A (GyrA) forms a 2:2 heterotetrameric complex with GyrB to form gyrase, a type II topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state
Negatively supercoils closed circular double-stranded DNA
DNA topoisomerase (ATP-hydrolyzing)
This HMM identifies type II DNA topoisomerases such as ParC (DNA topoisomerase IV subunit A) and GyrA (DNA gyrase subunit A).
DNA topoisomerase (ATP-hydrolyzing) subunit A
This model describes the common type II DNA topoisomerase (DNA gyrase). Two apparently independently arising families, one in the Proteobacteria and one in Gram-positive lineages, are both designated toposisomerase IV.
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