ID A0A1F6G5H6_9BACT Unreviewed; 693 AA.
AC A0A1F6G5H6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=A2609_01545 {ECO:0000313|EMBL:OGG93356.1};
OS Candidatus Kaiserbacteria bacterium RIFOXYD1_FULL_47_14.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798533 {ECO:0000313|EMBL:OGG93356.1, ECO:0000313|Proteomes:UP000176867};
RN [1] {ECO:0000313|EMBL:OGG93356.1, ECO:0000313|Proteomes:UP000176867}
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:OGG93356.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFMU01000009; OGG93356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6G5H6; -.
DR STRING; 1798533.A2609_01545; -.
DR Proteomes; UP000176867; 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:OGG93356.1};
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 446..560
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 693 AA; 75717 MW; 04CA7F8622E31A80 CRC64;
MAKTTEKEPK KKAYDASSIT VLEGLEPVRK RPGMYIGTTG PDGLHHLVWE IFDNARDEAM
AGRCDDIEVA LLPDNYVRVA DNGNGIPVGI HPKTKVSALE TIMTTLHAGG KFDNEAYKVS
GGLHGVGASV VNALSEHTKV VVHQDGGMHV QEYKIGKPVA KVKKIGTSKE HGTIVIFKPD
AVIFKEGIEL DLEKIITHVR QQAYLIKGVR VSVVDARQSE AKILSGVEGL FMRDQALGVP
SMTFYFEGGL KSLVAFYNKH QTPVHKNIFY VDHEQDNVGV EVALQYVDDI TPRITAFANN
TYNSEGGTHI TGFKTALTRS LNTYGRNANI LKEKDENFTG DDVLEGITAV VSVKLPEIQF
EGQTKSKLGS VEAQGAVATV FGEALAAFLE ENPDDARAII NKVLLALKAR KAAKAAKDSV
LRKGALEGMT LPGKLADCQT KSAEEGELFI VEGDSAGGSS KQGRDRRTQA ILPLRGKILN
VERARIDRML ASVEIRALIV AMGTAIGDIF DISKLRYHKI IIATDADVDG AHIRTLLLTL
LYRHFKPIIE GGFVYIAQPP LYKITKGKSM AYAYSDKEKE EVLKELGVAA SEVQEVNPDD
ESAELAEEIE AEEEKVATKK STKVNIQRYK GLGEMNPSEL WETTMNPARR VLKRVTTDDA
AAADRIFDIL MGTDVASRKS FIQSNAKMAT VDL
//
