ID Q1X6C7_9BURK Unreviewed; 640 AA.
AC Q1X6C7;
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:AAY86011.1};
OS Burkholderia cenocepacia.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=95486 {ECO:0000313|EMBL:AAY86011.1};
RN [1] {ECO:0000313|EMBL:AAY86011.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FCF28 {ECO:0000313|EMBL:AAY86011.1};
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; AY996894; AAY86011.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1X6C7; -.
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 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 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 321..436
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAY86011.1"
FT NON_TER 640
FT /evidence="ECO:0000313|EMBL:AAY86011.1"
SQ SEQUENCE 640 AA; 71003 MW; 745C3442D877BBE0 CRC64;
YKVSGGLHGV GVSCVNALSS WLRLTVRRDG KKRFMEFHRG VAQDRVLEVV DGVEVSPMLV
TGDTENRGTE VHFMADPTIF GTVEYHYDIL AKRMRELSFL NNGVRIRLTD LRSGKEDDFA
FAGGVKGFVE YINKTKTNLH PTVFFANGEK DGVGVEVAMQ WNDSYNENVL CFTNNIPQRD
GGTHLTGLRA AMTRVINKYI TDNEIAKKAK VETTGDDMRE GLSCVLSVKV PEPKFSSQTK
DKLVSSEVRA PVEEVVAKAL EEFLLETPID AKIICGKIVE AARARDAARK AREMTRRKGV
LDGVGLPGKL ADCQEKDPAK CEIYIVEGDS AGGSAKQGRD RKFQAILPLR GKVLNVEKAR
YDKLLSSEQI VTLVTALGCG IGKEDYNLDK LRYHRIIIMT DADVDGAHIR TLLLTFLYRQ
MPDMIERGYV YIAQPPLYKI KAGKDERYLK DDVELNAHML RLALQGSELV PGENAAAISG
DALGELARSY LLSQSVIDRL SRLYDPAALE AVMDGVVIDL SNEESTEASA KALHAALHDE
ALKNEVRVVP SYDAVREQRA LHVERTHHGN VRVSVIDQEF QHTADYQQLV TTANTFKGLI
GEGAVIKRGE RSMAVADFKS AMKWLLADAE RNVSKQRYKG
//
