ID J0NTQ7_HELPX Unreviewed; 773 AA. AC J0NTQ7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 19-FEB-2014, entry version 13. DE RecName: Full=DNA gyrase subunit B; DE EC=5.99.1.3; GN Name=gyrB; ORFNames=HPHPH19_0829; OS Helicobacter pylori Hp H-19. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=992066; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hp H-19; RX PubMed=23661595; DOI=10.1111/2049-632X.12045; RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M., RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K., RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.; RT "Genome sequences of 65 Helicobacter pylori strains isolated from RT asymptomatic individuals and patients with gastric cancer, peptic RT ulcer disease, or gastritis."; RL Pathogens Dis 68:39-43(2013). CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double- CC stranded DNA in an ATP-dependent manner and also catalyzes the CC interconversion of other topological isomers of double-stranded CC DNA rings, including catenanes and knotted rings (By similarity). CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. CC -!- COFACTOR: Magnesium. Binds two Mg(2+) per subunit. The magnesium CC ions form salt bridges with both the protein and the DNA. Can also CC accept other divalent metal cations, such as Mn(2+) and Ca(2+) (By CC similarity). CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. CC Within the heterotetramer, GyrA contains the active site tyrosine CC that forms a covalent intermediate with the DNA, while GyrB CC contributes the cofactor binding sites and catalyzes ATP CC hydrolysis (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the type II topoisomerase family. CC -!- SIMILARITY: Contains 1 Toprim domain. CC -!- SIMILARITY: Contains Toprim domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; AKPE01000004; EJB89767.1; -; Genomic_DNA. DR EnsemblBacteria; EJB89767; EJB89767; HPHPH19_0829. 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-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006200; P:ATP catabolic process; IEA:GOC. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. 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; IPR003594; HATPase_ATP-bd. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR001241; Topo_IIA. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR013759; Topo_IIA_cen_dom. DR InterPro; IPR013760; Topo_IIA_like_dom. DR InterPro; IPR018522; TopoIIA_CS. DR InterPro; IPR006171; Toprim_domain. 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; PR00418; TPI2FAMILY. 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; 2. DR TIGRFAMs; TIGR01059; gyrB; 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; KW Metal-binding; Nucleotide-binding; Topoisomerase. FT DOMAIN 416 530 Toprim (By similarity). FT METAL 422 422 Magnesium 1; catalytic (By similarity). FT METAL 495 495 Magnesium 1; catalytic (By similarity). FT METAL 495 495 Magnesium 2 (By similarity). FT METAL 497 497 Magnesium 2 (By similarity). FT SITE 447 447 Interaction with DNA (By similarity). FT SITE 450 450 Interaction with DNA (By similarity). SQ SEQUENCE 773 AA; 87503 MW; F25F88C038BE5E1C CRC64; MQNYQSHSIK VLKGLEGVRK RPGMYIGDTN IGGLHHMVYE VVDNAVDESM AGFCDTINIT LTEEGSCIVE DNGRGIPVDI HPTEKIPACT VVLTILHAGG KFDNDTYKVS GGLHGVGVSV VNALSKRLIM TIKKEGQIYR QEFEKGIPIS ELEIIGKTKS AKESGTTIEF FPDESVMEVV EFQAGILQKR FREMAYLNDG LKISFKEEKT QLQETYFYED GLKQFVKDSA KKELLTPIIA FKSMDEEMRT SIEVALAYAD DYNENTLSFV NNIKTSEGGT HEAGFKMGLS KAILQYIDNN IKTKDSRPIS EDIKEGLIAV VSLKMSEPLF EGQTKSKLGS SYARALVSKL VYDKIHQFLE ENPNEAKIIA NKALLAAKAR EASKKARELT RKKDNLSVGT LPGKLADCQS KDPLESEIFL VEGDSAGGSA KQGRDRVFQA ILPLKGKILN VEKSHLSKIL KSEEIKNMIT AFGCGIQESF DIERLRYHKI IIMTDADVDG SHIQTLLMTF FYRYLRPLIE QGHVYIAQAP LYKYKKGKTE IYLKDSVALD HFLIEHGINS VDIEGIGKND LMNLLKVVHH YRYTLLELEK RYNLLEVLRF LIETKDALSL DMKVLEKSIL EKLEGLNYQI LRSFATEESL HLHAQTPKGL VEFNLDDNLF KEVLFEEANY TYQKLMEYNL DFLENKDILA FLEEVENHAK KGANIQRYKG LGEMNPNDLW ETTMHKENRS LIKLKIEDLE KTDAIFSLCM GDEVEPRRAF IQAHAKDVKQ LDV //