ID A0A1B9XXD0_9FLAO Unreviewed; 618 AA.
AC A0A1B9XXD0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=BA195_11330 {ECO:0000313|EMBL:OCK42210.1};
OS Tenacibaculum soleae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK42210.1, ECO:0000313|Proteomes:UP000093186};
RN [1] {ECO:0000313|EMBL:OCK42210.1, ECO:0000313|Proteomes:UP000093186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK42210.1,
RC ECO:0000313|Proteomes:UP000093186};
RA Eisen J.A., Coil D.A., Lujan K.M.;
RT "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OCK42210.1}.
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DR EMBL; MAKX01000024; OCK42210.1; -; Genomic_DNA.
DR RefSeq; WP_068705635.1; NZ_MAKX01000024.1.
DR AlphaFoldDB; A0A1B9XXD0; -.
DR STRING; 447689.BA195_11330; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000093186; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR CDD; cd01030; TOPRIM_TopoIIA_like; 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; 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; 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; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
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 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OCK42210.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093186}.
FT DOMAIN 408..514
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 618 AA; 70508 MW; 0A625A459C1D3F9C CRC64;
MAQETKYTED NIRSLDWKEH IRMRPGMYIG KLGDGTSPDD GIYILVKEVL DNSIDEFVMG
TGKTIEVSVQ GEKVIVRDYG RGIPLGKVVD VVSKMNTGGK YDSRAFKKSV GLNGVGTKAV
NALSTFFRVE STRDGKSASA EFEKGELVNQ DLLEETSRRR GTKVTFIADN SIFKNYKYRP
EYIIRLLKNY VYLNPGLTIV FNGEKFHSKN GLKDLLEDNN NQDDMLYPII HLRGDDIEVA
ITHSKTQYSE EYHSFVNGQH TTQGGTHQAA FREAIVKTIR EFYGKNFDAS DVRKSIISAI
AIKVMEPVFE SQTKTKLGST EMGGDLPTVR TYINDFIKTK LDNFLHKNVE IADKLQKKII
QAEKERKELS GIRKLAKDRA KKASLHNKKL RDCRIHLGDI KKENHLDTTL FITEGDSASG
SITKSRNVNT QAVFSLKGKP LNSYGLSKKI VYENEEFNLL QAALNIEDGL EDLRYNNIVI
ATDADVDGMH IRLLLITFFL QFFPEVIKER HLYILETPLF RVRNKKETIY CYSEDEKRAA
IDKLRGKPEI TRFKGLGEIS PNEFVHFIGD DIRLDPVMLD KEMSIEQMLE FYMGKNTPDR
QKFIIENLKV ELDAIEEV
//