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Details on Person UniProt:P0AES6 gyrB
| Class:Id | ReferenceGeneProduct:9761014 |
|---|---|
| _chainChangeLog | initiator methionine:1 for 9761014 added on Wed February 16 2022;chain:2-804 for 9761014 added on Wed February 16 2022;initiator methionine:1 for 9761014 removed on Fri Nov 03 2023;initiator methionine: for 9761014 added on Fri Nov 03 2023;initiator methionine: for 9761014 removed on Fri Aug 15 2025;initiator methionine:1 for 9761014 added on Fri Aug 15 2025 |
| _displayName | UniProt:P0AES6 gyrB |
| _timestamp | 2025-08-15 22:08:25 |
| chain | initiator methionine:1 chain:2-804 |
| checksum | D831B95FFB3A7EE3 |
| comment | FUNCTION DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state (PubMed:12051842, PubMed:12051843, PubMed:1323022, PubMed:18642932, PubMed:186775, PubMed:19060136, PubMed:19965760, PubMed:20356737, PubMed:20675723, PubMed:22457353, PubMed:23294697, PubMed:23352267, PubMed:24386374, PubMed:25202966, PubMed:25849408, PubMed:3031051, PubMed:7811004, PubMed:8248233, PubMed:8621650, PubMed:9657678). This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli (PubMed:9334322). Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes (PubMed:22457352). Relaxes negatively supercoiled DNA in an ATP-independent manner (PubMed:337300). E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli (PubMed:22457352). E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical (PubMed:17400739). The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box (PubMed:16332690, PubMed:8962066).CATALYTIC ACTIVITY ATP-dependent breakage, passage and rejoining of double-stranded DNA.COFACTOR Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+) (PubMed:12051843, PubMed:18642932).COFACTOR Binds one K(+) per subunit which interacts with the alpha-phosphate of ATP analog and stimulates ATPase activity of the N-terminal fragment; Na(+) or water bind less well (PubMed:25849408).COFACTOR Binds one Na(+) per subunit, with 4 ligands provided by water; may be able to bind K(+), the functional significance of this ion is unclear (PubMed:25849408).ACTIVITY REGULATION Gyrase is the target of many classes of inhibitors, including coumarins, cyclothialidines, pyrrolopyrimidines, pyrazolthiazoles and (fluoro)quinolones. Coumarins bind to GyrB and are competitive inhibitors of its ATPase activity (PubMed:7811004). Cyclothialidines also bind GyrB and are ATPase competitive inhibitors; they seem to act differently from coumarins (PubMed:7811004, PubMed:8635474). Pyrrolopyrimidines inhibit both GyrB and its paralog in topoisomerase 4 (parE) (PubMed:23294697, PubMed:23352267, PubMed:24386374). Pyrazolthiazoles also inhibit the ATPase activity of GyrB (PubMed:20356737). Quinolones bind GyrA when the enzyme is complexed with DNA and trap the enzyme in a covalent reaction intermediate with DNA (PubMed:12051842, PubMed:3031051, PubMed:337300). Acriflavine inhibits DNA supercoiling and DNA-stimulated ATPase activity (PubMed:9148951). DNA supercoiling activity is protected from fluoroquinolone inhibition by QnrB4; QnrB4 has no effect on supercoiling activity alone (PubMed:19060136).SUBUNIT Heterotetramer, composed of two GyrA and two GyrB chains (PubMed:12051842, PubMed:9148951). In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with the DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis (PubMed:12051843, PubMed:18642932, PubMed:19965760, PubMed:20675723).INTERACTION Consists of 3 domains; the ATPase domain (residues 1-220), the transducer domain (221-392) and the toprim domain (393-804) (PubMed:10734094, PubMed:1646964). ATP-binding is cooperative, and both subunits must be wild-type at residue 103 for supercoiling to occur (PubMed:8621650). Non-hydrolyzable ATP analogs (and ATP-binding) induce dimerization and enhance ATPase activity (PubMed:10734094, PubMed:9657678). ATP hydrolysis induces domain shifts that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966).MISCELLANEOUS When the enzyme transiently cleaves DNA a phosphotyrosine bond is formed between GyrA and DNA in an ATP-independent manner (PubMed:3031051). In the presence of quinolones this intermediate can be trapped and is used as an indicator of drug toxicity (PubMed:12051842).SIMILARITY Belongs to the type II topoisomerase family. |
| created | [InstanceEdit:9761013] Stephan, Ralf, 2022-01-06 |
| description | recommendedName: fullName evidence="1"DNA gyrase subunit B ecNumber evidence="1 3 4 11 12 14"5.6.2.2 alternativeName: Type IIA topoisomerase subunit GyrB |
| geneName | gyrB acrB cou himB hisU nalC parA pcbA b3699 JW5625 |
| identifier | P0AES6 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing DNA-binding Isomerase Magnesium Metal-binding Nucleotide-binding Potassium Reference proteome Sodium Topoisomerase |
| modified | [InstanceEdit:9765872] Weiser, JD [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | gyrB |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | GYRB_ECOLI O08438 P06982 Q2M811 |
| sequenceLength | 804 |
| species | [Species:159879] Escherichia coli |
| (referenceEntity) | [EntityWithAccessionedSequence:9639503] GyrB [cytosol] [Escherichia coli] |
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No pathways have been reviewed or authored by UniProt:P0AES6 gyrB (9761014)
