ID   C3GSX9_BACTU            Unreviewed;       723 AA.
AC   C3GSX9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=bthur0010_53930 {ECO:0000313|EMBL:EEM74634.1};
OS   Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM74634.1};
RN   [1] {ECO:0000313|EMBL:EEM74634.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM74634.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
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   -!- 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:EEM74634.1}.
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DR   EMBL; ACNH01000122; EEM74634.1; -; Genomic_DNA.
DR   AlphaFoldDB; C3GSX9; -.
DR   HOGENOM; CLU_006146_1_2_9; -.
DR   Proteomes; UP000006660; Chromosome.
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:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd01030; TOPRIM_TopoIIA_like; 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; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
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; 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; PF00986; DNA_gyraseB_C; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          470..589
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   723 AA;  81680 MW;  C1B57F7F972E3873 CRC64;
     MSQNYGNNSI DSLEGAERVR RRPAAVLGSS GIEGARHGVT EIVGNSVDEG TAGFGSKLDI
     NYFKDGSISI RDYGRGVPMG YNENKGISNW FLVFNEMYAG GKYKDYQEEL RAIKDWSTFN
     PTDYNYLFSI GLNGLGAAST QYTSEFFEAI SITDGIATKM EFRGGYPILK DANGNEVHAI
     IGEERLLEEH GIVLKEYVAE TYETEEENGT YIHWKPDIRV FSDVDITLGW IKDVCESVAY
     ISGLDVNLYD EATDTMHEYQ SGTISDLNLI LNEKNLVNED SPSVYEDNDI THGNVKQNNE
     NFIYVFKADV SVVRTREKGK TVCFHNAIKM KGGAQYRAVD SAVADFVIGL GNTKGVKVVE
     RDFEGKLGVV VKSYSNVASY KGQTKDEVDD NFIYRDLKTI IYRLINTEYH KGNKDIIEFV
     DKVLEEAELR ITLQEQAKML REVKKTSRTR KLPEKFLPSK LFKEKIVKKS ELWIVEGDSA
     KTSVKNARDP LFQAIYAVRG KVTNALKASF KKLMESEEIR DIFSLLGTGM DVELLDDNEF
     DIDACRFEKI IIGTDADEDG YQIRVLLFVV FWVLAPEIIK RGMLYIGETP KFGIKLSNGE
     MVYAINEVDK AEREKEYAGQ IVKVERYKGL GEVNADVLGF TTLAPETRNL IQIKLDPADH
     ILSEFVETLF GKDPYKKRKE TMLRVLGSDA MDMFNDTDEK EEFSIVDVLD ADDVEEENEL
     EVI
//