ID T2D1K8_9GAMM Unreviewed; 372 AA. AC T2D1K8; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 27-NOV-2024, entry version 32. DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166}; DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895}; DE Flags: Fragment; GN Name=gyrB {ECO:0000313|EMBL:AGV40784.1}; OS Arsukibacterium tuosuense. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Arsukibacterium. OX NCBI_TaxID=1323745 {ECO:0000313|EMBL:AGV40784.1}; RN [1] {ECO:0000313|EMBL:AGV40784.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TS-T4 {ECO:0000313|EMBL:AGV40784.1}; RX PubMed=24408524; DOI=10.1099/ijs.0.056473-0; RA Zhong Z.P., Liu Y., Liu L.Z., Wang F., Zhou Y.G., Liu Z.P.; RT "Rheinheimera tuosuensis sp. nov., isolated from a saline lake."; RL Int. J. Syst. Evol. Microbiol. 64:1142-1148(2014). 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family. CC {ECO:0000256|ARBA:ARBA00010708}. 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; KF156795; AGV40784.1; -; Genomic_DNA. DR AlphaFoldDB; T2D1K8; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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-EC. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1. DR FunFam; 3.30.230.10:FF:000005; DNA gyrase subunit B; 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 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_dom. 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; PF01751; Toprim; 1. DR PRINTS; PR01159; DNAGYRASEB. DR PRINTS; PR00418; TPI2FAMILY. 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 {ECO:0000256|ARBA:ARBA00022840}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}. FT DOMAIN 301..372 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGV40784.1" FT NON_TER 372 FT /evidence="ECO:0000313|EMBL:AGV40784.1" SQ SEQUENCE 372 AA; 41151 MW; B20E90A69492492B CRC64; VGISVVNALS DKLELTIRRK GQVHNQIYHL GVPQAPLAVI GETEDTGTAI RFWPSPTVFS DIDYHYDILA KRLRELSFLN SGVSIILSDE RNDKKDHFKY EGGIEAFVQY LNRSKTSVHP KAFYFTDQRE DGISVEVAMQ WNDSYQENVF CFTNNIPQRD GGAHLAGFRG ALTRVLNNYI EHEGYAKKMK VQASGDDARE GLTAVVSVKV PDPKFSSQTK DKLVSSEVRS AVEGIMGEKL NEYLLENPGD AKIIVGKIVD AARARDAARK AREMTRRKGA LDIAGLPGKL ADCQEKDPAF SELYIVEGDS AGGSAKQGRN RKNQAILPLK GKILNVEKAR FDKMLSSQEV GTLITALGCG IGREEYNPDK TR //