ID   A0A133QHI8_9BACT        Unreviewed;       649 AA.
AC   A0A133QHI8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-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=HMPREF3226_00708 {ECO:0000313|EMBL:KXA42351.1};
OS   Prevotella corporis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA42351.1, ECO:0000313|Proteomes:UP000070533};
RN   [1] {ECO:0000313|Proteomes:UP000070533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-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:KXA42351.1}.
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DR   EMBL; LRQG01000037; KXA42351.1; -; Genomic_DNA.
DR   RefSeq; WP_060940298.1; NZ_KQ957205.1.
DR   AlphaFoldDB; A0A133QHI8; -.
DR   STRING; 28128.HMPREF3226_00708; -.
DR   PATRIC; fig|28128.5.peg.715; -.
DR   eggNOG; COG0187; Bacteria.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000070533; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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; PF00986; DNA_gyraseB_C; 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};
KW   Kinase {ECO:0000313|EMBL:KXA42351.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070533};
KW   Transferase {ECO:0000313|EMBL:KXA42351.1}.
FT   DOMAIN          407..517
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   649 AA;  74286 MW;  FF13E1D53D90CC1F CRC64;
     MDNNPVSYTD ENIRHLSDME HVRTRPGMYI GRLGDGNLPE DGIYVLLKEV LDNSIDEFKM
     NAGTRIEIDV EDNLRVSVRD YGRGIPQGKL VEAVSVLNTG GKYDSKAFKK SVGLNGVGVK
     AVNALSANFE VKSFRDGKVR ELTFEKGELK SDNTQKSKDE NGTYIFFEPD ATLFKNYSFH
     DDIVETMLRN YTYLNTGLTI MYNGRRIVSR HGLKDLLTDN MTVDPLYPIV HMKGDDIEIA
     FTHTNQYGEE YYSFVNGQHT TQGGTHQSAF KEHIARTIKD YFGKYEYGDI RNGMVAAIAV
     NVEEPVFESQ TKIKLGSTQM SPDGETINKF VGDFIKTNVD NFLHIHKEDF TDILENKIKE
     TERERKAMAG VTKLARERAK KANLHNRKLR DCRVHFSDTK SDRKEESCIF ITEGDSASGS
     ITKSRDVNTQ AVFSLRGKPL NCFGLTKKVV YENEEFNLLQ AALDIEDGLD TLRYNKVIVA
     TDADVDGMHI RLLIITFFLQ FFPELIKKGH VYVLQTPLFR VRNRRTKIKN KQTIEEIDAR
     RAKGEKKSDF VTMYCYNEEE RQNAIRDLGP DPEITRFKGL GEISPDEFAH FIGPDMRLEQ
     VTLHKNDQVQ KLLEYYMGKN SMERQNFIID NLVIEEDLAE EEEAEAQEN
//