ID J0NTQ7_HELPX Unreviewed; 773 AA. AC J0NTQ7; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 28-JUN-2023, entry version 63. 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:EJB89767.1}; GN ORFNames=HPHPH19_0829 {ECO:0000313|EMBL:EJB89767.1}; OS Helicobacter pylori Hp H-19. OC Bacteria; Campylobacterota; 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 ulcer RT disease, or gastritis."; RL Pathog. Dis. 68:39-43(2013). 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: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 AlphaFoldDB; J0NTQ7; -. DR EnsemblBacteria; EJB89767; EJB89767; HPHPH19_0829. DR PATRIC; fig|992066.3.peg.801; -. 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-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; -; 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; 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; 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 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 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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01898}; Cytoplasm {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 416..530 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT BINDING 422 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 495 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT BINDING 495 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 497 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT SITE 447 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01898" FT SITE 450 FT /note="Interaction with DNA" FT /evidence="ECO:0000256|HAMAP-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 //