ID A0A374VER6_9BACE Unreviewed; 624 AA.
AC A0A374VER6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=DXC10_01300 {ECO:0000313|EMBL:RGM49954.1};
OS Bacteroides sp. OM08-11.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=2292284 {ECO:0000313|EMBL:RGM49954.1, ECO:0000313|Proteomes:UP000262405};
RN [1] {ECO:0000313|EMBL:RGM49954.1, ECO:0000313|Proteomes:UP000262405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM08-11 {ECO:0000313|EMBL:RGM49954.1,
RC ECO:0000313|Proteomes:UP000262405};
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 -!- 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:RGM49954.1}.
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DR EMBL; QSTJ01000001; RGM49954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374VER6; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000262405; 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; 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; 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; 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, ECO:0000313|EMBL:RGM49954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000262405}.
FT DOMAIN 416..526
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 624 AA; 70901 MW; 9A0D80E435675AB2 CRC64;
MEEEINGLIP GNNVEYTEDN IRHLDDMEHI RVRSGMYIGR LGDGSQNDDG IYVLLKEVMD
NSIDEFKMGA GKRIEVNIED NLRVSVRDYG RGIPQGKLVE AVSKLNTGGK YDSKAFKKSV
GLNGVGIKAV NALSSRFEVR SYRDGKVRTA IFEKGVLIND VTENTLEENG TYIFFEADNT
LFLNYSYQNT FVETLLRNYT YLNTGLAIIY NGQRILSRHG LEDLLKDNMT AEGLYDIIHL
KGEDIEIAFT HTNQYGEEYY SFVNGQHTTQ GGTHQSALKE HIARTIKEFY NKNQDYADIR
NGIVAAIAIN VEEPQFEGQT KTKLGSPSME PGGVSINKYV GDFIKTEVDN YLHKNPLVAE
VMLQKIQDSE KERKAIAGVT KLARERAKKA NLHNRKLRDC RFHLSDGKGK DQETESCIFI
TEGDSASGSI TKSRDVNTQA VFSLRGKPLN SYGLTKKVVY ENEEFNLLQA ALNIEDGIEG
LRYNKVIVAT DADVDGMHIR LLIITFFLQF FPDLIKKGHV YILQTPLFRV RNKKKTNYCY
TEDERLKSIE ELGPNPEITR FKGLGEISPD EFKHFIGKDM RLEQVSLRKT DLVKELLEFY
MGKNTMERQN FIINNLVIEE DLAS
//