ID GYRB_STRP8 Reviewed; 650 AA. AC Q8P1M4; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=DNA gyrase subunit B {ECO:0000255|HAMAP-Rule:MF_01898}; DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01898}; GN Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; GN OrderedLocusNames=spyM18_0795; OS Streptococcus pyogenes serotype M18 (strain MGAS8232). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=186103; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGAS8232; RX PubMed=11917108; DOI=10.1073/pnas.062526099; RA Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., RA Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., RA Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., RA Veasy L.G., Musser J.M.; RT "Genome sequence and comparative microarray analysis of serotype M18 group RT A Streptococcus strains associated with acute rheumatic fever outbreaks."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002). 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:0000255|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:0000255|HAMAP- CC Rule:MF_01898}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP- CC 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:0000255|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:0000255|HAMAP-Rule:MF_01898}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_01898}. CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family. CC {ECO:0000255|HAMAP-Rule:MF_01898}. 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; AE009949; AAL97459.1; -; Genomic_DNA. DR RefSeq; WP_011017600.1; NC_003485.1. DR AlphaFoldDB; Q8P1M4; -. DR SMR; Q8P1M4; -. DR KEGG; spm:spyM18_0795; -. DR HOGENOM; CLU_006146_4_1_9; -. 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 Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.670; -; 1. 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; IPR003594; HATPase_C. DR InterPro; IPR036890; HATPase_C_sf. 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_domain. 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; 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; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Nucleotide-binding; Topoisomerase. FT CHAIN 1..650 FT /note="DNA gyrase subunit B" FT /id="PRO_0000145352" FT DOMAIN 429..543 FT /note="Toprim" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" FT BINDING 435 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" FT BINDING 508 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" FT BINDING 508 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" FT BINDING 510 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" FT SITE 460 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" FT SITE 463 FT /note="Interaction with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898" SQ SEQUENCE 650 AA; 72309 MW; 2CF598897B872ACB CRC64; MIEENKHFEK KMQEYDASQI QVLEGLEAVR MRPGMYIGST AKEGLHHLVW EIVDNSIDEA LAGFASHIKV FIEADNSITV VDDGRGIPVD IQAKTGRPAV ETVFTVLHAG GKFGGGGYKV SGGLHGVGSS VVNALSTQLD VRVYKNGQIH YQEFKRGAVV ADLEIIGTTD VTGTTVHFTP DPEIFTETTQ FDYSVLAKRI QELAFLNRGL KISITDKRSG MEQEEHFHYE GGIGSYVEFL NDKKDVIFET PIYTDGELEG IAVEVAMQYT TSYQETVMSF ANNIHTHEGG THEQGFRAAL TRVINDYAKK NKILKENEDN LTGEDVREGL TAVISVKHPN PQFEGQTKTK LGNSEVVKIT NRLFSEAFQR FLLENPQVAR KIVEKGILAS KARIAAKRAR EVTRKKSGLE ISNLPGKLAD CSSNDANQNE LFIVEGDSAG GSAKSGRNRE FQAILPIRGK ILNVEKATMD KILANEEIRS LFTAMGTGFG ADFDVSKARY QKLVIMTDAD VDGAHIRTLL LTLIYRFMRP VLEAGYVYIA QPPIYGVKVG SEIKEYIQPG IDQEDQLKTA LEKYSIGRSK PTVQRYKGLG EMDDHQLWET TMDPENRLMA RVTVDDAAEA DKVFDMLMGD RVEPRRDFIE ENAVYSTLDI //