ID A0A395YK27_9CLOT Unreviewed; 639 AA.
AC A0A395YK27;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=DXA13_14290 {ECO:0000313|EMBL:RGY97475.1};
OS Clostridium sp. AM58-1XD.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2292307 {ECO:0000313|EMBL:RGY97475.1, ECO:0000313|Proteomes:UP000266320};
RN [1] {ECO:0000313|EMBL:RGY97475.1, ECO:0000313|Proteomes:UP000266320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM58-1XD {ECO:0000313|EMBL:RGY97475.1,
RC ECO:0000313|Proteomes:UP000266320};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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:RGY97475.1}.
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DR EMBL; QSDR01000023; RGY97475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395YK27; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000266320; 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:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000266320};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 421..539
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 639 AA; 71206 MW; CB4EA69016F22527 CRC64;
MAKTQYNADS ITVLEGLEAV RKRPGMYIGG VGSKGLNHLI YEIVDNAVDE HLAGFCDEIW
VTLESDGSCT VKDSGRGIPV EMHKKGVSAE RVVLATLHAG GKFDNTAYKT SGGLHGVGSS
VVNALSAHMD VKVYKGGFIH HDVYEKGVPV IELENGLLPV IGKTRQTGTE INFLPDEEIF
ERIRFKADWL KSRLHETAYL NPKLTIHYQN KRPGEAEKID YAEPEGLIAY VKELNTGKDA
VHDPIYYKGS VDGIEVEAAV QFVDTFEENI LGFCNNIFTQ EGGTHLAGFK TRFTQMINSY
ARELGILKDK DTNFTGADTR NGMTAVVAVK HPDPIFEGQT KTKLASADAT KAVFTVTGDE
LSLYFDRNLE VLKGIIGCAE KSAKIRKAEE KAKTNMLSKS KFSFDSNGKL ANCESRDASK
CEIFIVEGDS AGGSAKTARN RQYQAILPIR GKILNVEKAS MDKVLANAEI KTMINTFGCG
FSEGYGNDFD ITKLRYDKII LMTDADVDGS HIDTLLLTFL YRFMPELIYN GHVYIAMPPL
FKVIPKKGEE QYLYDEKELE KYRKTHTGDF TLQRYKGLGE MDAEQLWETT LDPERRVLKQ
VEIEDARLAS EITELLMGSD VPPRRRFIYE HADEAEIDA
//
