ID A0A0G0U6Y7_9BACT Unreviewed; 701 AA.
AC A0A0G0U6Y7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=UT81_C0004G0030 {ECO:0000313|EMBL:KKR45932.1};
OS Parcubacteria group bacterium GW2011_GWA2_40_14.
OC Bacteria.
OX NCBI_TaxID=1618814 {ECO:0000313|EMBL:KKR45932.1, ECO:0000313|Proteomes:UP000034892};
RN [1] {ECO:0000313|EMBL:KKR45932.1, ECO:0000313|Proteomes:UP000034892}
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:KKR45932.1}.
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DR EMBL; LBYF01000004; KKR45932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0U6Y7; -.
DR STRING; 1618814.UT81_C0004G0030; -.
DR PATRIC; fig|1618814.3.peg.237; -.
DR Proteomes; UP000034892; 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};
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 450..564
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 701 AA; 77289 MW; 8C287A4359F2F609 CRC64;
MAKVKEDKKA EKTSSYGAEQ ITILEGLAPV RKRPGMYIGT TGLDGLQHLI TEIFDNARDE
AMGGFANDIE VTLLPNNRVR VTDNGRGIPI DIHKQSKVSA LETIMTTLHA GGKFGEDSSG
YKVSGGLHGV GASVVNALSI YCKVTVHKDG GVYMQEYSQG KKKASVKKVG TTKQHGTIVV
FEPDPAIFPE IAFDFQKVVD HLRQQAYLVK GLRITVNDAR ETQEKIKEDE VFKISELGLE
IPSMSFYFEG GLLSLVKFYN STQKPIHKNI FYVEKKTNEY ESVEVALQYV DDISSRVLPF
ANNIYTAEGG THVTGFKTAL TRTLNTYGRK NNLIKESEDN FTGEDVLEGL TAVISVKLRE
IQFEGQTKSK LGSVEAQSSV NTVFSESFSY FLEENPDDAR AIIMKVILAL RARKAAKAAK
DSILRKGALE GMTLPGKLAD CQSGTTPEDA ELFVVEGDSA GGTAKTGRDR RTQAILPLRG
KILNIERARL DRMLESEQIK NLVIALGTAI GDTFDISKLR YHKVIIATDA DVDGAHIRTL
ILTLLYRFFK PLIDGGFIYI AQPPLYKIKK GKEIHYAYSD DEKMAVVGDL PADIADETQN
DAEVEVESEI EKEQAEGKLT LGEATTVKKS KISIQRYKGL GEMNAEELWE TTMDPARRIL
KQVTIADAVL ADKVFDILMG SDVPSRKSFI QSNATKATLD I
//
