ID A0A117R9R6_9ACTN Unreviewed; 707 AA.
AC A0A117R9R6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=AQJ66_30090 {ECO:0000313|EMBL:KUN78900.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN78900.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN78900.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN78900.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-2015) 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:KUN78900.1}.
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DR EMBL; LMWX01000056; KUN78900.1; -; Genomic_DNA.
DR RefSeq; WP_061928251.1; NZ_KQ948870.1.
DR AlphaFoldDB; A0A117R9R6; -.
DR STRING; 285568.AQJ66_30090; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000053024; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
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, ECO:0000313|EMBL:KUN78900.1};
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:UP000053024};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 480..594
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 707 AA; 77261 MW; 22A2E660581D5C5A CRC64;
MTADTSVPST ALLAGADRDG SNYTARHLLV LEGLEAVRKR PGMYIGSTDS RGLMHCLWEI
IDNSVDEALG GYCDHIEVIL HDDGSVEVRD NGRGIPVDVE PKTGLSGVEV VMTKLHAGGK
FGGGSYAASG GLHGVGASVV NALSARLDVE VDRSGHTHAI SFRRGVPGAF RGYGPDAKFE
AASGLAKAKK IPKSRTGTRV RYWADRQIFL KDAKLSLETL HQRARQTAFL VPGLTIVVRD
EVGLGEGGSK GEESFRFDGG ISEFCEYLAK DRAVCDVLRF SGQGTFKETV PVLDEHGQMT
PTEVTRELGV DVAMRWGTGY DTTLRSFVNI IATPKGGTHV AGFEQAVTKT LLEAVRAKKL
LRVAEDDIVK DDALEGLTAV VTVRLAEPQF EGQTKEVLGT SAARRIVFNV ISKELKAFLT
STKRDAAAQA RVVMEKVVAA ARTRVAARQH KDAQRRKTAL ESSSLPAKLA DCRSDDVDRS
ELFIVEGDSA LGTAKLARNS EFQALLPIRG KILNVQRSSV TDMLKNAECG AIIQVIGAGS
GRTFDIDQAR YGKIIMMTDA DVDGSHIRCL LLTLFQRYMR PMVEAGRVFA AVPPLHRIEL
VQPRKGQDKY VYTYSDRELR DKLMEFESKG VRYKDSIQRY KGLGEMDADQ LAETTMDPRH
RTLRRINLSD LEAAEQVFDL LMGNDVAPRK EFISSSAATL DRSRIDA
//