ID A0A1F5Z2L5_9BACT Unreviewed; 640 AA.
AC A0A1F5Z2L5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=A2872_01335 {ECO:0000313|EMBL:OGG06352.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_01_FULL_42_12.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798377 {ECO:0000313|EMBL:OGG06352.1, ECO:0000313|Proteomes:UP000178681};
RN [1] {ECO:0000313|EMBL:OGG06352.1, ECO:0000313|Proteomes:UP000178681}
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:OGG06352.1}.
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DR EMBL; MFJG01000023; OGG06352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5Z2L5; -.
DR STRING; 1798377.A2872_01335; -.
DR Proteomes; UP000178681; 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:OGG06352.1};
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 425..539
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 640 AA; 71016 MW; F556D45002E6B74B CRC64;
MAIKSDYSAA NITVLEGLEP VRKRPGMYIG STDEKGLHHL VTEIVDNSVD EALGGFANKI
FVTINKDSSL TIEDNGRGIP VGINEKYKVS GVELALTKLH AGGKFDDKSY KASSGLHGVG
ASAVNALSEW MQVEVYQNGK VHGISFRIGK ADGPLKVTGK TEATGTKVTF LPDNTIFSTT
EWKYDTLRNM LRNYAYLVPK LMFKLKDERE NQNREDTFYF EGGIKSLVGY LSGSKDNVSE
IFYVQKDVET NVANVSVEVA LQYNDDFGEN LESFVNAVNT PDGGTHVSGF RMALTRAIND
YGKKIGAIKD GQESFIGEDL REGLTAVVYI KMSSDKLQFE SQTKTRLNNP EIQPAVSAVV
KEGLDAFFEE NPRDGRAILE KVFLAAKARL AARAAKESII RKGALEGSTL PGKLADCQLR
DPSQTELFIV EGDSAGGSAK QGRDRKFQAI LPLFGKPLNT ERARIDQIID SEKFKPLIIA
IGAGIADQFN IEKLRYHRII IMADADVDGS HIKCLYLTFL YRHLKEIIDR GHVYVALPPL
YKLEWGKGNK KYVYTEAEKE NFIKTLGESK VNVQRYKGLG EMNATELWDT TLNPQNRMLK
QVTVLDAARA DQVFTMLMSD DVGPRKKFIQ TRAKNATLDI
//
