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Database: UniProt
Entry: D9Z724_9BACI
LinkDB: D9Z724_9BACI
Original site: D9Z724_9BACI 
ID   D9Z724_9BACI            Unreviewed;       393 AA.
AC   D9Z724;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE   Flags: Fragment;
GN   Name=gyrB {ECO:0000313|EMBL:ADK92931.1};
OS   Geobacillus jurassicus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=235932 {ECO:0000313|EMBL:ADK92931.1};
RN   [1] {ECO:0000313|EMBL:ADK92931.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 15726 {ECO:0000313|EMBL:ADK92931.1};
RA   Tourova T.P., Korshunova A.V., Mikhailova E.M., Sokolova D.S.,
RA   Poltaraus A.B., Nazina T.N.;
RT   "Application of gyrB and parE Sequence Similarity Analyses for
RT   Differentiation of Species within the Genus Geobacillus.";
RL   Microbiology (Mosc.) 79:356-369(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   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
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DR   EMBL; GU459228; ADK92931.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9Z724; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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; 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; 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          315..393
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADK92931.1"
FT   NON_TER         393
FT                   /evidence="ECO:0000313|EMBL:ADK92931.1"
SQ   SEQUENCE   393 AA;  44046 MW;  132C7BB4AB5943B0 CRC64;
     GGGGYKVSGG LHGVGASVVN ALSEWLEVYV YRDGKIHYQR YERGEPCTDL QVIGETDRTG
     TTTRFKPDPE IFTETTEFDY ETLATRLREL AFLNRGLKIT LTDERVDNRK NEYVYEGGIR
     SYVRHLNRTR EVLHEEPIYI AGERDGIAVE IALQYNDGYT SNIYSFVNNI HTHEGGTHES
     GFKMALTRII NDYARKQQIF KDNDANLTGE DVREGLTAIV SIKHPSPQFE GQTKTKLGNS
     DARTVTDAVF SEQFETFLLE HPTIARKIVE KGMMAARARL AAKKARELTR RKSALEISNL
     PGKLADCSSR DPSISELYIV EGDSAGGSAK QGRDRHFQAI LPLRGKILNV EKARLDKILS
     NNEVRAIITA LGTGIGEDFD ISKARYHKII IMT
//
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