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Database: UniProt
Entry: A0A1I5UT80_9FIRM
LinkDB: A0A1I5UT80_9FIRM
Original site: A0A1I5UT80_9FIRM 
ID   A0A1I5UT80_9FIRM        Unreviewed;       640 AA.
AC   A0A1I5UT80;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=SAMN02910358_00393 {ECO:0000313|EMBL:SFP98388.1};
OS   Lachnospiraceae bacterium XBB1006.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520827 {ECO:0000313|EMBL:SFP98388.1, ECO:0000313|Proteomes:UP000199554};
RN   [1] {ECO:0000313|EMBL:SFP98388.1, ECO:0000313|Proteomes:UP000199554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XBB1006 {ECO:0000313|EMBL:SFP98388.1,
RC   ECO:0000313|Proteomes:UP000199554};
RA   de Groot N.N.;
RL   Submitted (OCT-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};
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DR   EMBL; FOXT01000004; SFP98388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5UT80; -.
DR   STRING; 1520827.SAMN02910358_00393; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000199554; 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; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF12; DNA TOPOISOMERASE 4 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   4: Predicted;
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   Reference proteome {ECO:0000313|Proteomes:UP000199554}.
FT   DOMAIN          422..540
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   640 AA;  71142 MW;  4BB5850989DC939A CRC64;
     MAGKATYDAS SIKVLEGLEA VRKRPGMYIG SVSRKGLHHL IYEIVDNAVD EHLGGYCNHI
     TVTLEADGSC TVSDDGRGIP VGMHKQGISA ERVVFTTLHA GGKFDNNAYK TSGGLHGVGS
     SVVNALSSFL DVQVKLGGKI HHDRYEKGNP VIALEDGLLP VIGKTKETGT TINFLPDEEI
     FEKIRFVAED VKSRLHETAY LNPKLTITFR DLRGEEPEEV VYHEPKGIVG FVEALNKNAE
     KVHDVIYFEG NADGIEVEVA FQFTTEFREN VLGFCNNIYN AEGGAHITGF KTMFTTVINS
     YARQLGILKE KDANFTGADV RNGMTAVISV KHPDPRFEGQ TKTKLDNQDA ARVTSKVTGD
     EIVLYFDRNL EVLKNVIGCA EKAAKIRKSE EKAKTNLLTK QKFSFDSNGK LANCESRDAK
     KCEIFIVEGD SAGGSAKMAR NRMYQAIMPI RGKILNVEKA TIDKVLANAE IKTMINAFGC
     GFSEGYGNDF DITKLRYDKI VIMADADVDG AHISTLLLTL FYRFMPELIS EGHVYIAMPP
     LYKTIPSKGK GEYLYDDAAL ERYRKTHKEK FTLQRYKGLG EMDAEQLWET TLNPETRMLK
     LVEIEDARMA SDITQMLMGT EVAPRRQFIY ENAKDAQLDI
//
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