GenomeNet

Database: UniProt
Entry: V6KTN7_STRRC
LinkDB: V6KTN7_STRRC
Original site: V6KTN7_STRRC 
ID   V6KTN7_STRRC            Unreviewed;       703 AA.
AC   V6KTN7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=M878_05430 {ECO:0000313|EMBL:EST35502.1};
OS   Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST35502.1, ECO:0000313|Proteomes:UP000017984};
RN   [1] {ECO:0000313|EMBL:EST35502.1, ECO:0000313|Proteomes:UP000017984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS 12.976 {ECO:0000313|EMBL:EST35502.1,
RC   ECO:0000313|Proteomes:UP000017984};
RX   PubMed=24407645;
RA   Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT   12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL   Genome Announc. 2:e01147-e01113(2014).
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:EST35502.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWQX01000050; EST35502.1; -; Genomic_DNA.
DR   RefSeq; WP_023545088.1; NZ_CM002285.1.
DR   AlphaFoldDB; V6KTN7; -.
DR   STRING; 1352936.M878_05430; -.
DR   PATRIC; fig|1352936.5.peg.1165; -.
DR   HOGENOM; CLU_006146_4_1_11; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000017984; 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   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:EST35502.1};
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:UP000017984};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          476..590
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   703 AA;  76779 MW;  ABC4BDA337FC2EB6 CRC64;
     MSTLPAPAAG SRPQDGSDYT ARHLMVLEGL EAVRKRPGMY IGSSDSRGLM HCLWEIIDNA
     VDEALAGACD YIEVILHDDG SVEVTDNGRG IPVDTEPRTG LSGVEIAYTK LHAGGKFGGG
     SYAASGGLHG VGASVVNALS ARLDVEVDRH GRTHAISFRR GTPGTYTGPG PDAPFTPAQG
     LRQTTKIPKS RTGTRVRYWA DRQSFLKDAK LSLENLHQRA RQTAFLVPGL TIVVRDEFGL
     GEGGSKGEES FRFDGGISEF CEFLASDTPV CDILRFSGQG TFKETVPVLD EHGQMTPTEV
     TRELGVDVAL RWGTGYDTTV RSFVNIIATP KGGTHVAGFE QAVGKTLNEV LRAKKLLRVA
     EDDIAKDDAL EGLTAVVTVR LAEPQFEGQT KEVLGTSAAR RIVNNVISKE LKAFLTSTKR
     DAAQQARVVM EKAVAAARTR IAARQHKDAQ RRKSALESSS LPAKLADCRS DDVDRSELFI
     VEGDSALGTA KLARNSEFQA LLPIRGKILN VQRSSVSDML KNAECGAIIQ VIGAGSGRTF
     DIDTARYGKI IMMTDADVDG SHIRTLLLTL FHRYMRPMVE AGRVFAAVPP LHRIELVQPR
     KGQERYVYTY SDRELRDKLM EFQSKGIRYK DSVQRYKGLG EMDADQLAET TMDPRHRTLR
     RINLTDLEAA EGVFDLLMGN DVAPRKEFIT SSAATLDRSR IDV
//
DBGET integrated database retrieval system