ID A0A0G0XXA8_9BACT Unreviewed; 640 AA.
AC A0A0G0XXA8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=UU42_C0001G0171 {ECO:0000313|EMBL:KKR92567.1};
OS Candidatus Woesebacteria bacterium GW2011_GWA1_41_13b.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618555 {ECO:0000313|EMBL:KKR92567.1, ECO:0000313|Proteomes:UP000034676};
RN [1] {ECO:0000313|EMBL:KKR92567.1, ECO:0000313|Proteomes:UP000034676}
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:KKR92567.1}.
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DR EMBL; LCAO01000001; KKR92567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0XXA8; -.
DR PATRIC; fig|1618555.3.peg.186; -.
DR Proteomes; UP000034676; 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 426..540
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 640 AA; 70490 MW; 7B1CF84354DBF9A1 CRC64;
MTDDYTAEQI QVLEGLEPVR KRPGMYIGST DTRGLHECLR EIVDNSVDES FAGVANTVWV
SLNKDGSATV RDNGRGIPVE KQKKTGVSAL ELTMTKLHAG GKFGGGAYKV SGGLHGVGAS
VVNALSSYFR VVVLRDSKAY YQEYKRGIAL KPVGEASRKQ LDEWGIKLDG AGTITNFIPD
KEIFGDVVLE NTKVKNLLRD RAYLIAGLTF HFEDLNDGDE ATFYFEGGIK SLVAHTNRGR
DVLNDVIYFS KNDGAMTAEV ALQYSDSFNE NVKGFVNGIY TTDGGTHVTG FRIALTRAIS
DYYKKIQNGG KDEAALTGDD MKEGLTAIVY IKMPSESLQF ESQTKAKLNN PEVQGFVSTA
VKEGLDQYFE EHPAEARKVV EKITLAARAR LAARAAKDAV LRKGALEGAT LPGKLADCQS
SDASVSELYI VEGDSAGGSA KQGRDRRHQA ILPLGGKILN TERAHLDKIV KFEEIKDLII
ALGGGIGETL NYDKMRYHRV IIMTDADVDG AHISTLLLTF FYRHMPEIIT RGYLYMALPP
LFRVQIGKDV NYAYTEEERD MITAKSPGIK AIIQRYKGLG EMNPTQLWET TMNPETRTLK
QVTVESMEAA GNMFEMLMGE EVPPRKKYIQ THAKLATLDV
//
