ID A0A165K1L4_9BURK Unreviewed; 868 AA. AC A0A165K1L4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 27-NOV-2024, entry version 43. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898}; DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01898}; GN Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898, GN ECO:0000313|EMBL:KZT14929.1}; GN ORFNames=A1D30_03695 {ECO:0000313|EMBL:KZT14929.1}; OS Acidovorax sp. GW101-3H11. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Acidovorax. OX NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT14929.1, ECO:0000313|Proteomes:UP000077219}; RN [1] {ECO:0000313|Proteomes:UP000077219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219}; RA Ray J., Price M., Deutschbauer A.; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KZT14929.1, ECO:0000313|Proteomes:UP000077219} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT14929.1, RC ECO:0000313|Proteomes:UP000077219}; RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0; RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H., RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z., RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D., RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.; RT "Mutant phenotypes for thousands of bacterial genes of unknown function."; RL Nature 557:503-509(2018). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed CC circular double-stranded (ds) DNA in an ATP-dependent manner to CC modulate DNA topology and maintain chromosomes in an underwound state. CC Negative supercoiling favors strand separation, and DNA replication, CC transcription, recombination and repair, all of which involve strand CC separation. Also able to catalyze the interconversion of other CC topological isomers of dsDNA rings, including catenanes and knotted CC rings. Type II topoisomerases break and join 2 DNA strands CC simultaneously in an ATP-dependent manner. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185, CC ECO:0000256|HAMAP-Rule:MF_01898}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01898}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges CC with both the protein and the DNA. Can also accept other divalent metal CC cations, such as Mn(2+) or Ca(2+). {ECO:0000256|HAMAP-Rule:MF_01898}; CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In CC the heterotetramer, GyrA contains the active site tyrosine that forms a CC transient covalent intermediate with DNA, while GyrB binds cofactors CC and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming CC negative supercoils. Not all organisms have 2 type II topoisomerases; CC in organisms with a single type II topoisomerase this enzyme also has CC to decatenate newly replicated chromosomes. {ECO:0000256|HAMAP- CC Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family. CC {ECO:0000256|ARBA:ARBA00010708, ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KZT14929.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LUKZ01000013; KZT14929.1; -; Genomic_DNA. DR RefSeq; WP_063461435.1; NZ_LUKZ01000013.1. DR AlphaFoldDB; A0A165K1L4; -. DR STRING; 1813946.A1D30_03695; -. DR OrthoDB; 9802808at2; -. DR Proteomes; UP000077219; Unassembled WGS sequence. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule. DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd16928; HATPase_GyrB-like; 1. DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1. DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1. DR FunFam; 3.30.230.10:FF:000005; DNA gyrase subunit B; 1. DR FunFam; 3.30.565.10:FF:000002; DNA gyrase subunit B; 1. DR FunFam; 3.40.50.670:FF:000004; DNA gyrase subunit B; 1. DR FunFam; 3.40.50.670:FF:000001; DNA topoisomerase 2; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.670; -; 2. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR HAMAP; MF_01898; GyrB; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR011557; GyrB. DR InterPro; IPR049353; GyrB_hook. DR InterPro; IPR041423; GyrB_insert. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR000565; Topo_IIA_B. DR InterPro; IPR013759; Topo_IIA_B_C. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR006171; TOPRIM_dom. DR InterPro; IPR034160; TOPRIM_GyrB. DR NCBIfam; TIGR01059; gyrB; 1. DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1. DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF21249; GyrB_hook; 1. DR Pfam; PF18053; GyrB_insert; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR01159; DNAGYRASEB. DR PRINTS; PR00418; TPI2FAMILY. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01898}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01898}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01898}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01898}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01898}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01898}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP- KW Rule:MF_01898}. FT DOMAIN 473..595 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 479 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 560 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 560 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 562 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT SITE 504 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT SITE 507 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" SQ SEQUENCE 868 AA; 95379 MW; 6F9D70F13174E505 CRC64; MTADNNLPEQ EPTGTGEPVP HKIDTNQAGA SESYGEGSIT ILEGLEAVRK RPGMYIGDTS DGTGLHHLVF EVVDNSIDEA LAGHCDDIVV TIHTDNSISV TDNGRGIPTG VKMDDKHEPK RSAAEIALTE LHAGGKFNQN SYKVSGGLHG VGVSCVNALS KWLRLTVRRE GKVHQIEFAR GFVQDRLLDK VDGFEVSPMK VTGETEKRGT EVHFLPDTEI FKENYDFHYE ILAKRLRELS FLNNGVRIRL KDERSGKEDD FSGAGGVRGF VEFINKGKTV LHPTSFYAAG ERPAETYGGI PGTHIGVEVS MQWNSAYTEQ VLCFTNNIPQ RDGGTHLTGL RAAMTRVINK YIEENELAKK AKVEVTGDDM REGLCCVLSV KVPEPKFSSQ TKDKLVSSEV RAPVEDIVGK LLTDYLQERP ADAKIICGKI VEAARAREAA RKAREMTRRK GVLDGMGLPG KLADCQEKDP AMCEIYIVEG DSAGGSAKQG RDRKFQAILP LRGKILNVEK ARYEKLLTSN EILTLITALG TGIGKAGGTT GGDDFDVAKL RYHRIIIMTD ADVDGAHIRT LLLTFFYRQM PELVERGHIY IAQPPLYKVK AGKEELYLKD GPALDGFLLR IALNHASVST GGANPQVLAG DTLAELARKH QVAESVIHRL SNFMDQEALR AVADGVSLKL DTVAEAEASA VALQIKLREL NTTGTPAEVA GEFDARTDKP ILRISRRHHG NVKSSVITQD FVHGADYAAL AEAADTFRGL LGEGAKALRG EGDKQKEEKV GDFRQAMKWL ISEAERTTSR QRYKGLGEMN PEQLWETTMD PNVRRLLRVQ IDDAIEADRV FTMLMGDEVE PRRDFIETNA LRAGNIDV //