ID J0NTQ7_HELPX Unreviewed; 773 AA. AC J0NTQ7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 17-FEB-2016, entry version 29. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00504111}; DE EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470646}; GN Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898, GN ECO:0000313|EMBL:EJB89767.1}; GN ORFNames=HPHPH19_0829 {ECO:0000313|EMBL:EJB89767.1}; OS Helicobacter pylori Hp H-19. OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=992066 {ECO:0000313|EMBL:EJB89767.1, ECO:0000313|Proteomes:UP000005191}; RN [1] {ECO:0000313|EMBL:EJB89767.1, ECO:0000313|Proteomes:UP000005191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hp H-19 {ECO:0000313|EMBL:EJB89767.1, RC ECO:0000313|Proteomes:UP000005191}; 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: 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 -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898, CC ECO:0000256|SAAS:SAAS00470725}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01898}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01898}; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01898}; CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt CC bridges with both the protein and the DNA. Can also accept other CC divalent metal cations, such as Mn(2+) or Ca(2+). CC {ECO:0000256|HAMAP-Rule:MF_01898}; 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 -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP- CC 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:EJB89767.1}. 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; AKPE01000004; EJB89767.1; -; Genomic_DNA. DR RefSeq; WP_001181970.1; NZ_AKPE01000004.1. DR EnsemblBacteria; EJB89767; EJB89767; HPHPH19_0829. DR Proteomes; UP000005191; 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-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: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_C. 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. DR InterPro; IPR013506; Topo_IIA_bsu_dom2. DR InterPro; IPR013759; Topo_IIA_cen_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 {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00470817}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000005191}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01898}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00470744, ECO:0000313|EMBL:EJB89767.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01898}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00470788}; KW Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898, KW ECO:0000256|SAAS:SAAS00470796}. FT DOMAIN 416 530 Toprim. {ECO:0000259|PROSITE:PS50880}. FT COILED 372 392 {ECO:0000256|SAM:Coils}. FT METAL 422 422 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01898}. FT METAL 495 495 Magnesium 1; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01898}. FT METAL 495 495 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_01898}. FT METAL 497 497 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_01898}. FT SITE 447 447 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_01898}. FT SITE 450 450 Interaction with DNA. {ECO:0000256|HAMAP- FT Rule:MF_01898}. 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 //