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Database: UniProt
Entry: D5KJX0_BACPU
LinkDB: D5KJX0_BACPU
Original site: D5KJX0_BACPU 
ID   D5KJX0_BACPU            Unreviewed;       354 AA.
AC   D5KJX0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
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:ADF50153.1};
OS   Bacillus pumilus (Bacillus mesentericus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1408 {ECO:0000313|EMBL:ADF50153.1};
RN   [1] {ECO:0000313|EMBL:ADF50153.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GBSW2 {ECO:0000313|EMBL:ADF50153.1};
RA   Xue P.Q., Gao X.W.;
RT   "Genotypic and phenotypic analysis of antagonistic Bacillus spp. isolated
RT   from rhizosphere soil of plants in Tibet.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; GU568234; ADF50153.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5KJX0; -.
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; 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          296..354
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADF50153.1"
FT   NON_TER         354
FT                   /evidence="ECO:0000313|EMBL:ADF50153.1"
SQ   SEQUENCE   354 AA;  39276 MW;  4EF4BFD59FE65361 CRC64;
     ALSTTLDVTV YRDGKIHYQQ FKRGVPAGDL EIIGETDVTG TTTHFVPDPE IFTETIEFDY
     DTLANRVREL AFLTKGVNII IEDLREGKER RNEYCYEGGI KSYVEHLNRS KEVVHEEPVY
     IEGEKDGITI EVALQYNDSY SSNIYSFANN INTYEGGTHE AGFKTGLTRV INDYARKNGV
     FKDGDSNLSG EDVREGLTAI ISIKHPDPQF EGQTKTKLGN SEARTITDSL FSEALEKFLL
     ENPDAAKKIV EKGVMAARAR MAAKKARELT RRKSALEVSS LPGKLADCSS KDPSISELYI
     VEGDSAGGSA KQGRDRHFQA ILPLRGKILN VEKARLDKIL SNNEVRSMIT ALGT
//
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