ID A0A1C9ZWI2_9ESCH Unreviewed; 274 AA. AC A0A1C9ZWI2; DT 30-NOV-2016, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 1. DT 22-FEB-2023, entry version 15. 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:BAV58437.1}; OS Escherichia albertii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=208962 {ECO:0000313|EMBL:BAV58437.1}; RN [1] {ECO:0000313|EMBL:BAV58437.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P2660 {ECO:0000313|EMBL:BAV58437.1}; RX PubMed=27580579; RA Hinenoya A., Yasuda N., Hibino T., Shima A., Nagita A., Tsukamoto T., RA Yamasaki S.; RT "Isolation and Characterization of an Escherichia albertii Strain Producing RT Three Different Toxins from a Child with Diarrhea."; RL Jpn. J. Infect. Dis. 70:252-257(2017). 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; LC159067; BAV58437.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1C9ZWI2; -. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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; cd16928; HATPase_GyrB-like; 1. DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. 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; IPR013506; Topo_IIA_bsu_dom2. 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; PF02518; HATPase_c; 1. 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. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235}. FT DOMAIN 1..139 FT /note="Histidine kinase/HSP90-like ATPase" FT /evidence="ECO:0000259|SMART:SM00387" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAV58437.1" FT NON_TER 274 FT /evidence="ECO:0000313|EMBL:BAV58437.1" SQ SEQUENCE 274 AA; 30391 MW; B93333D0B500294B CRC64; HHMVFEVVDN AIDEALAGHC KEIIVTIHAD NSVSVQDDGR GIPTGIHPEE GVSAAEVIMT VLHAGGKFDD NSYKVSGGLH GVGVSVVNAL SQKLELVIQR EGKIHRQIYE HGVPQAPLAV TGDTDKTGTM VRFWPSLETF TNVTEFEYDI LAKRLRELSF LNSGVSIRLK DKRDGKEDHF HYEGGIKAFV EYLNKNKTPI HPNIFYFSTE KDGIGVEVAL QWNDGFQENI YCFTNNIPQR DGGTHLAGFR AAMTRTLNAY MDKEGYSKKA KVSA //