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
//