ID   A0A1F1DU44_9PORP        Unreviewed;       631 AA.
AC   A0A1F1DU44;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=HMPREF2890_06925 {ECO:0000313|EMBL:OFR33691.1};
OS   Porphyromonas sp. HMSC065F10.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1739394 {ECO:0000313|EMBL:OFR33691.1, ECO:0000313|Proteomes:UP000177035};
RN   [1] {ECO:0000313|EMBL:OFR33691.1, ECO:0000313|Proteomes:UP000177035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC065F10 {ECO:0000313|EMBL:OFR33691.1,
RC   ECO:0000313|Proteomes:UP000177035};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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:OFR33691.1}.
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DR   EMBL; LTXH01000189; OFR33691.1; -; Genomic_DNA.
DR   RefSeq; WP_070466980.1; NZ_KV793802.1.
DR   AlphaFoldDB; A0A1F1DU44; -.
DR   STRING; 1739394.HMPREF2890_06925; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000177035; 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; 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; PS50880; TOPRIM; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OFR33691.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177035}.
FT   DOMAIN          424..530
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  71909 MW;  D936D3F708302B24 CRC64;
     MTDAEEKLTP TPLPSTPDPL YQEDKIVTLD PMEHIRLRPG MYIGKLGDGT APDDGIYVLL
     KEVIDNSIDE YTMGYGKHIY ITIDEEEHRH VTVRDHGRGI PQGSLAKAVG TMNTGAKYDN
     EVFKKSVGLN GVGLKAVNAL STRMAVSSYR DGTVKTVVFE RGKLIEESDI LPAPGEHDGT
     FVDYYADPDI FRNYRYQQEY VHSMIRMYTY LQPGLTIHLN GTRFISRNGL LDLLEDNMTA
     TPLYPIIHLQ GDDIEVAITH STQYGEEYYS FVNGQNTLHG GTHLSAFKEA IGKTVKEFFD
     KSYDYNDIRS GITAAISIRI QEPVFESQTK TKLGSREISE GGISIQKFVI DFVKLQLDNY
     LHKHPDTAEI LQKKVVDNER ERKALQGISK KAKERVKKAS LYNKKLRDCT VHFNDPKAKE
     PERTEIFITE GLSASGSITQ SRDPEYQAVF SLRGKPLNSY GLSKKVVYEN EEFNLLQAAL
     NIEDGLEDLR YNRVIVATDA DVDGMHIRLL IITFFLQFFP ELIRENHVFI LQTPLFRVRD
     RQGKEIIYCY DERERNEAMK KIGKSASVTR FKGLGEIKPE EFGNFIGENM RLDPVVMKKE
     DNVPELLKFY MGTNSRERQD FIVDNLETDD I
//