ID A0A165K1L4_9BURK Unreviewed; 868 AA. AC A0A165K1L4; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 31-JUL-2019, entry version 25. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898}; DE EC=5.6.2.3 {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; Proteobacteria; 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., RA Esquivel Z., Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., RA Wall J.D., Visel A., Bristow J., Blow M.J., Arkin A.P., RA Deutschbauer A.M.; RT "Mutant phenotypes for thousands of bacterial genes of unknown RT function."; RL Nature 557:503-509(2018). CC -!- FUNCTION: A type II topoisomerase that negatively supercoils CC closed circular double-stranded (ds) DNA in an ATP-dependent CC manner to modulate DNA topology and maintain chromosomes in an CC underwound state. Negative supercoiling favors strand separation, CC and DNA replication, transcription, recombination and repair, all CC of which involve strand separation. Also able to catalyze the CC interconversion of other topological isomers of dsDNA rings, CC including catenanes and knotted rings. Type II topoisomerases CC break and join 2 DNA strands simultaneously in an ATP-dependent CC manner. {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00612567}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00709652}; CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC In the heterotetramer, GyrA contains the active site tyrosine that CC forms a transient covalent intermediate with DNA, while GyrB binds CC cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP- CC 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 CC topoisomerases; in organisms with a single type II topoisomerase CC this enzyme also has to decatenate newly replicated chromosomes. CC {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase family. CC {ECO:0000256|HAMAP-Rule:MF_01898}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KZT14929; KZT14929; A1D30_03695. 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 (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-dependent DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR Gene3D; 3.40.50.670; -; 2. DR HAMAP; MF_01898; GyrB; 1. DR InterPro; IPR002288; DNA_gyrase_B_C. DR InterPro; IPR011557; GyrB. DR InterPro; IPR041423; GyrB_insert. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013760; Topo_IIA-like_dom_sf. DR InterPro; IPR013759; Topo_IIA_B_C. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR006171; TOPRIM_domain. DR InterPro; IPR034160; TOPRIM_GyrB. DR Pfam; PF00204; DNA_gyraseB; 1. DR Pfam; PF00986; DNA_gyraseB_C; 1. DR Pfam; PF18053; GyrB_insert; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF01751; Toprim; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00433; TOP2c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR SUPFAM; SSF56719; SSF56719; 1. DR TIGRFAMs; TIGR01059; gyrB; 1. DR PROSITE; PS00177; TOPOISOMERASE_II; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528655}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000077219}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}; KW DNA-binding {ECO:0000256|SAAS:SAAS00709661}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00470744}; KW Magnesium {ECO:0000256|SAAS:SAAS00445358}; KW Metal-binding {ECO:0000256|SAAS:SAAS00445373}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528653}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00528650}. FT DOMAIN 473 595 Toprim. {ECO:0000259|PROSITE:PS50880}. FT REGION 1 33 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 683 703 {ECO:0000256|SAM:Coils}. 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 //