ID A0A0G0BZP5_9BACT Unreviewed; 641 AA.
AC A0A0G0BZP5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=UR34_C0003G0011 {ECO:0000313|EMBL:KKP44385.1};
OS candidate division WS6 bacterium GW2011_GWC1_33_20.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1619089 {ECO:0000313|EMBL:KKP44385.1, ECO:0000313|Proteomes:UP000034302};
RN [1] {ECO:0000313|EMBL:KKP44385.1, ECO:0000313|Proteomes:UP000034302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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:KKP44385.1}.
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DR EMBL; LBOV01000003; KKP44385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0BZP5; -.
DR PATRIC; fig|1619089.3.peg.199; -.
DR Proteomes; UP000034302; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
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_domain.
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 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, ECO:0000313|EMBL:KKP44385.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 425..539
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 641 AA; 71313 MW; 92CFB30B7BD172E7 CRC64;
MPKKSDYQAS NIQVLEGLEA VRKRPAMYIG STDRNGLHHI FTEILDNSVD EAIAGYCSRI
WVTLELDGSI SVKDNGRGIP VEIHPQTKVS TLETVMTNLH AGGKFDDGAY KVSGGLHGVG
MKCTNALSEW MITTVTRDGG IYRQEYKRGI PQAPVKKVGS IDDSITGTEH RFLPDDEIFS
ETTFDFKEII KKCRQHAYLT AGLRITVKDL RVEQGHAPKI FDLYFEDGIK SYVLFMNIDE
KFVNEQPFYV NKENEGVLVE AAIQYTNSMD ENVKCYTNNI INPEGGTHLA GFRTALTSAI
NTYAQKSELL KGLTSTLNGD DVREGLTAVI SVKVANPQFE GQTKIKLNNP EVKNAVAKVI
RDELLIYFDE HPKEAKAIID KAILSYKAKA AAKAARDAVI RKSALESTAL PGKLADCISS
NPADSELYIV EGDSAGGSAK QGRDRHTQAV LPLRGKIINT HKYRVDRVLG NNEFKDITTA
LGVGIGTTLD IAKLRYHKIV IMSDADVDGL HITTLVLTLL YRFFKPLIDG GYVYVAQPPL
HKVEIGKKKY YFLNDNEKDE FVRKAKAAGK VPVSNRFKGL GEMNPGQLWE TTMSPETRVL
KQVKIDDAEE AEKVFEMLMG TEVPPRRRFI QKYAKRANLD V
//
