ID A0A1G2SDA4_9BACT Unreviewed; 687 AA.
AC A0A1G2SDA4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=A2937_02330 {ECO:0000313|EMBL:OHA83033.1};
OS Candidatus Yonathbacteria bacterium RIFCSPLOWO2_01_FULL_47_33b.
OC Bacteria; Candidatus Yonathbacteria.
OX NCBI_TaxID=1802727 {ECO:0000313|EMBL:OHA83033.1, ECO:0000313|Proteomes:UP000177987};
RN [1] {ECO:0000313|EMBL:OHA83033.1, ECO:0000313|Proteomes:UP000177987}
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:OHA83033.1}.
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; MHUW01000021; OHA83033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2SDA4; -.
DR STRING; 1802727.A2937_02330; -.
DR Proteomes; UP000177987; 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:OHA83033.1};
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 441..555
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 687 AA; 76656 MW; 08E95E62D2E47C1E CRC64;
MAKKDEKTVG YGAEDIVVLE GLEPVRKRPG MYIGSTGPEG LHHLIWEIFD NSRDEAMGGF
ADRIEVVLLP GNRVRVVDNG RGIPVDIHSK TKVSALETIM TTLHAGGKFE GESYKVSGGL
HGVGASVVNA LSVYTEVRVH RDGGIHMQEY ERGKRKAAVK KIGTTKFRGT IVTFEPDELI
FKEMGWNWNQ IVNHLRQQAY LVKGLHIAIL DAREYAGKLK LDNVVYFEDL SLEVPSMSFY
FDGGLVSLVR FYNQHQKPIH KNICYVDKEV DGVQVEVAIQ YIDDISSREL AFANNIYNME
GGTHVTGFRT ALTRKINEYG RKNNFIKENE ENFTADDVRE GLTSAISVKM REIQFEGQTK
GKLGSVEARS AVEKVFGEAL GMFLEENPED ARAIVNKVII ALRARKAAKA AKDSVMRKGA
LEGLTLPGKL ADCQTSKAED SEVFIVEGDS AGGSSKQGRD RRTQAILPLK GKILNVERAR
LDRMLASVEI RSLVVAMGTG IGDIFDISKL RYHKIIIATD ADVDGAHIRT LLLTLFYRYF
KPVIEGGFIY IAQPPLYKIK KGKEITYVYS EAEKIAYLGK DVSLLEVVEE GEEEEFEGTE
EEVAAEAEEK GKKREPKVSL QRYKGLGEMN PEELWETTMD PKRRILKQVR IEDAVDADKA
FDVLMGEDVA SRKSFIQSNA KMANIDA
//
