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Database: UniProt
Entry: E4NI54_KITSK
LinkDB: E4NI54_KITSK
Original site: E4NI54_KITSK 
ID   E4NI54_KITSK            Unreviewed;       706 AA.
AC   E4NI54;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   OrderedLocusNames=KSE_54090 {ECO:0000313|EMBL:BAJ31184.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS   / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ31184.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ31184.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA   Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA   Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
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}.
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DR   EMBL; AP010968; BAJ31184.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4NI54; -.
DR   STRING; 452652.KSE_54090; -.
DR   KEGG; ksk:KSE_54090; -.
DR   PATRIC; fig|452652.3.peg.5410; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_4_1_11; -.
DR   Proteomes; UP000007076; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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:BAJ31184.1};
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:UP000007076};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          479..593
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   706 AA;  77281 MW;  A7BAD31EB642970C CRC64;
     MQSVSGEKTG PSSLVTGEGG SDYTARHLLV LEGLEAVRKR PGMYIGSTDS RGLMHCLWEI
     IDNSVDEALG GFCDRIDVLL HQDGSVEVRD NGRGIPVDVE PKTGLSGVEV VMTKLHAGGK
     FGGGSYAASG GLHGVGASVV NALSARLDVE VDRSGATHAI SFRRGTPGAY AGEGPDAAFE
     PGSGMTKRGK FAKTRTGTRI RYWADRQIFL KDAKLSLESL HSRARQTAFL VPGLTIVVRD
     ERLTESEQVA EETFRYDGGI SEFCEFLAPD RPISDVLRLR GEGTFKETVP VLDELGHMTP
     TEVTRELGVD IALRWGAGYD TTQRSFVNII STPKGGTHVT GFERQLAKTV NEALRAAKLL
     RVAEDDITKD DAQEGLTAVI TVRLAEPQFE GQTKEVLGTS AANRIVAAVV AKELKAFLTS
     AKKDEKLQAR AVLEKVVAAA RTRVAARQHK EAQRRKTALE TSSLPAKLAD CRSDDVERSE
     LFIVEGDSAL GTAKLARNSE FQALLPIRGK ILNVQKASVS DMLKNAECAS IIQVIGAGSG
     RTFDIDQARY GKVIFMADAD VDGSHIRTLL LTLFHRYMRP MVEQGRVFAA VPPLHRIELT
     NPKRGQEKYH YTYSDAELRR TLLQFQGKGL RWKDPIQRYK GLGEMDADQL AETTMDPRFR
     ILRRINLGDL ESAEKTFDLL MGNDVAPRRE FIVDSAATLD RSRIDA
//
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