ID A0A1F6WC24_9BACT Unreviewed; 691 AA.
AC A0A1F6WC24;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=A3F19_01295 {ECO:0000313|EMBL:OGI79439.1};
OS Candidatus Nomurabacteria bacterium RIFCSPHIGHO2_12_FULL_37_29.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801759 {ECO:0000313|EMBL:OGI79439.1, ECO:0000313|Proteomes:UP000177052};
RN [1] {ECO:0000313|EMBL:OGI79439.1, ECO:0000313|Proteomes:UP000177052}
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:OGI79439.1}.
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DR EMBL; MFUJ01000010; OGI79439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6WC24; -.
DR Proteomes; UP000177052; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
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; IPR011557; GyrB.
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 NCBIfam; TIGR01059; gyrB; 1.
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 447..561
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 691 AA; 76772 MW; F57D767AF971804E CRC64;
MAKEKEEKKG NGHHYDASDI SVLEGLEPVR RRPGMYIGTT GPEGLHHLVW EIFDNSRDEA
MGDFCDDIEV VLLPNNRIRI ADNGRGIPID IHKKTKVSAL ETVMTTLHAG GKFGGEGYKV
SGGLHGVGAS VVNALSIYCK AEIHRDGGKY VQEYSRGKKK SVVKKVGTSK LHGTIVTFEP
DVEIFKDIKF DWHTIVNHIR QQAYLVKGLK ILIIDARGWD DKKGMDDSDV FYFRDLGLEL
SSTSFYFEGG LISLIKYYNK FQKSIQDNIF YVEKESDGVG VEIALQYVDD IVDRIIPFAN
NIHTPEGGTH VTGFKTALTR TLNTYCKKNE MMKESEGGFT GEDVLEGLTC AISVKLREIQ
FEGQTKAKLG SQEAQGAVAT VFGEAFNNFL EENPNEAKSI INKSILALKA RKAAKAAKDS
ILRKGALEGM TLPGKLADCQ SKDASESELF LVEGDSAGGS AKQGRDRRTQ AILPLRGKIL
NVERARIDKM LASKEVKSLV IAMGTSIGDT FDLSKMRYHK IIIATDADVD GSHIRTLLLT
LFYRYFRAVI DAGYIYIAQP PLYKIKKGKE ISYAYTDDEK LKIVGKGADV SEIQEVEASE
EAEIPSEGEG KEEEITKKSN KIHIQRFKGL GEMNPEELWE TTMDPMNRVL KKVNIDDAEE
ANKIFDILMG SEVPPRKSFI QSNAKLAEID I
//
