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Database: UniProt
Entry: Q1X6A7_BURVI
LinkDB: Q1X6A7_BURVI
Original site: Q1X6A7_BURVI 
ID   Q1X6A7_BURVI            Unreviewed;       603 AA.
AC   Q1X6A7;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 86.
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:AAY86031.1};
OS   Burkholderia vietnamiensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=60552 {ECO:0000313|EMBL:AAY86031.1};
RN   [1] {ECO:0000313|EMBL:AAY86031.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FCF42 {ECO:0000313|EMBL:AAY86031.1};
RX   PubMed=18312571; DOI=10.1111/j.1574-6968.2008.01105.x;
RA   Tabacchioni S., Ferri L., Manno G., Mentasti M., Cocchi P., Campana S.,
RA   Ravenni N., Taccetti G., Dalmastri C., Chiarini L., Bevivino A., Fani R.;
RT   "Use of the gyrB gene to discriminate among species of the Burkholderia
RT   cepacia complex.";
RL   FEMS Microbiol. Lett. 281:175-182(2008).
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; AY996914; AAY86031.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1X6A7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.300.370; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR049353; GyrB_hook.
DR   InterPro; IPR041423; GyrB_insert.
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   InterPro; IPR034160; TOPRIM_GyrB.
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; PF21249; GyrB_hook; 1.
DR   Pfam; PF18053; GyrB_insert; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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          284..399
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY86031.1"
FT   NON_TER         603
FT                   /evidence="ECO:0000313|EMBL:AAY86031.1"
SQ   SEQUENCE   603 AA;  66955 MW;  22768E1BBFD4A36B CRC64;
     HRGIAQDRVL EQVDGVEVSP MLVTGDTENR GTEVHFMADP TIFGTVEYHY DILAKRMREL
     SFLNNGVRIR LTDLRSGKED DFAFAGGVKG FVEYINKTKT NLHPTVFFAN GEKDGVGVEV
     AMQWNDSYNE NVLCFTNNIP QRDGGTHLTG LRAAMTRVIN KYITDNEIAK KAKVETTGDD
     MREGLSCVLS VKVPEPKFSS QTKDKLVSSE VRAPVEEVVA KALEEFLLET PTDAKIICGK
     IVEAARARDA ARKAREMTRR KGVLDGVGLP GKLADCQEKD PAKCEIYIVE GDSAGGSAKQ
     GRDRKFQAIL PLRGKVLNVE KARYDKLLSS EQIVTLVTAL GCGIGKDDYN LDKLRYHRII
     IMTDADVDGA HIRTLLLTFF YRQMPEMVER GYVYIAQPPL YKIKAGKDER YLKDDAELNA
     HMLRLALQGS ELVPSENGAA ISGDALGELA RSYLLSQSVI GRLSRLYDPA ALEAIMDGVS
     IDLSSEESTE ASARALHAAL HDETLKNEVR VVPSYDPVRE LRSLRVERAH HGNVRVSVID
     EEFQHTADYQ QLVTTAKTFE GLIQAGAVIK RGERSMAVTD FKSAMKWLLA DAERNVSKQR
     YKG
//
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