ID A0A1F6XMJ7_9BACT Unreviewed; 693 AA.
AC A0A1F6XMJ7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=A2917_02100 {ECO:0000313|EMBL:OGI95336.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_42_17.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801780 {ECO:0000313|EMBL:OGI95336.1, ECO:0000313|Proteomes:UP000178104};
RN [1] {ECO:0000313|EMBL:OGI95336.1, ECO:0000313|Proteomes:UP000178104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGI95336.1}.
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DR EMBL; MFVE01000005; OGI95336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6XMJ7; -.
DR STRING; 1801780.A2917_02100; -.
DR Proteomes; UP000178104; 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 CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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 InterPro; IPR034160; TOPRIM_GyrB.
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:OGI95336.1};
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 450..564
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 596..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 76562 MW; DAAA3AF25479D85D CRC64;
MAKEDVTKKG NGHHYDASDI SVLEGLEPVR RRPGMYIGTT GPEGLHHLVW EIFDNSRDEA
MGGFCNDIEV VLLPGNRVRV ADNGRGIPVD THKKTKVSAL ETVMTTLHAG GKFGGEGYKV
SGGLHGVGAS VVNALSIFCK AEVHRDGGKY VQEYSQGKKK SAVKKVGSSK LHGTIVTFEP
DVEIFKDIKF DWNTVVNHIR QQAYLVKGLK ILIIDARDAK ELHDKKGMDD SDVFYFRDLG
LELPSISFYF EGGLISLIKY YNKFQKPIQS NIFYVEKELD GVGVEIALQY VDDIVDRIVP
FANNINTPEG GTHVTGFKTA LTRTLNTYCK KNEMMKESEG GFTGEDVLEG LTVAISVKLR
EIQFEGQTKA KLGSMEAQGA VATVFGEAFN NFLEENPDEA KVIINKSILA LKARKAAKAA
KDSILRKGAL EGMTLPGKLA DCQSKNAEES ELFLVEGDSA GGSAKQGRDR RTQAILPLKG
KILNVERARI DKMLASKEIK SLVIALGTSI GDTFDLAKMR YHKIIIATDA DVDGSHIRTL
LLTLFYRYFR QIIDAGYIYI AQPPLYKIKK GKEISYAYTD EERIKIVGKG ADISDIQPAD
VEDDSGEAKE GEEESVGKEK SAKIHIQRYK GLGEMNPEEL WETTMDPAHR VLKKVNIDDA
EEANKIFDIL MGSEVPPRKS FIQSNAKLAE IDI
//
