ID A0A1F6DAG4_9BACT Unreviewed; 680 AA.
AC A0A1F6DAG4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=A2765_05655 {ECO:0000313|EMBL:OGG58404.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_01_FULL_56_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798487 {ECO:0000313|EMBL:OGG58404.1, ECO:0000313|Proteomes:UP000176377};
RN [1] {ECO:0000313|EMBL:OGG58404.1, ECO:0000313|Proteomes:UP000176377}
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:OGG58404.1}.
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DR EMBL; MFLA01000033; OGG58404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6DAG4; -.
DR Proteomes; UP000176377; 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:OGG58404.1};
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 443..557
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 580..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 74488 MW; 552A4FFE82960BA8 CRC64;
MAETKVKKSS YGAADITVLE GLEAVRRRPG MYIGTTGPTG LHHLIWEIFD NSRDEAMGGF
ADDIEVALLP GNRIRVADNG RGIPVEIHPK TKVSTLETVL TVLHAGGKFG GEGYKVSGGL
HGVGAAVVNA LSVHMRAEVH RDGGKFVQEY KNGGKPVGKT KREGASKFNG TIITFEPDKS
IFPEVKFEYD TIVAHLRQQA YLVKGMRIAI IDMRDVESAG RRIDDESVIY LRDLGIDAPS
TTFYFEGGLK SLVTFQNRHQ TAVHKNVFYV EKEQDNVMVE IALQYVDDFT TRLSAFANNI
HTAEGGMHVT GFKTALTRTL NNASKGGNGK EGDSYTGDDV LEGLTAVISV KLREIQFEGQ
TKSKLGSVEA RGATETVFSE AFTAFLEEHP DDCRAILGKA TLAMKARKAA KAAKDSVLRK
GALEGLSLPG KLADCQVRDP AEAEIFIVEG DSAGGTAKAG RDRRTQAVLP LRGKILNIER
ARLDKMLASE QITNLVVAMG TAIGDVFDIT KLRYHKIIIA TDADVDGAHI RTLLLTLFYR
HFRPIIDGGF LYIAQPPLYK IKKGKEVFYA YSEEEKTKIA GNDMPIESEE SQSGEDEEEE
VAGKAKRAPK LSVQRYKGLG EMNAEELKET TMDVNNRILQ IVTVEDASEA DRTFDILMGT
DVPSRKTFIQ SHAKEANLDI
//
