ID A0A0G0MCP1_9BACT Unreviewed; 651 AA.
AC A0A0G0MCP1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=UT24_C0001G0014 {ECO:0000313|EMBL:KKR01854.1};
OS Candidatus Woesebacteria bacterium GW2011_GWB1_39_12.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1618574 {ECO:0000313|EMBL:KKR01854.1, ECO:0000313|Proteomes:UP000033881};
RN [1] {ECO:0000313|EMBL:KKR01854.1, ECO:0000313|Proteomes:UP000033881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR01854.1}.
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DR EMBL; LBWB01000001; KKR01854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MCP1; -.
DR STRING; 1618574.UT24_C0001G0014; -.
DR PATRIC; fig|1618574.4.peg.14; -.
DR Proteomes; UP000033881; 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; 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; 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 437..551
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 651 AA; 72222 MW; 6B0B6F76B1692EF3 CRC64;
MPKIQEYTAK EIQVLEGLEP VRKRPGMFVG STDSRGLHEC LREIVDNSVD ESFAGIAKNI
WVILGKDGSA VIRDDGRGIP VDKHASGVSA LELTMTKLHA GGKFGGGAYK VSGGLHGVGA
SMVNALSSYF RVIVLRNNKA YFQEYKQGKP LKEVSTATQK ELDGWLPGKW NIKLGEDKTG
TITTFIPDEI IFKTSTVFDA EKVKNILKDR AYLVPGLAFH FYDETTDQET HYYFEGGIKA
LVGHSNRDKE TISDVIYVIK SEGDLSVEVA LQYTDSYSEN VKGFVNGINT VDGGTHLTGF
RMALTRSISD YAKKVGNGKN SVQDNGLTGD DMKEGLTAVV YIKMPSEALQ FESQTKAKLN
NPEIQGFVQS GVKEGLDTYF EEHPNDAKRV VEKIFLAAKA RLAARAAKEA VLRKGALEGS
SLPGTLADCQ SRDPEISELY IVEGESAGGS AKQGRDRHFQ AILPLGGKIL NTERAHLDKI
IEFEELKNLI IALGAGVGDI INYDKIRYQR VIIMTDADVD GEHIKTLLLT FFYRHMPEVI
RRGYLYIALP PLYKIQVGKE AYYAYEEDEK TQIIKDKANG KVTIQRYKGL GEMNPEQLWE
TTMDPKVRIL KQVTVEDAEE GDRIFTILMG EEVAPRKKFI QTHAKLATLD I
//
