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
//