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Database: UniProt
Entry: C9WXU2_9BURK
LinkDB: C9WXU2_9BURK
Original site: C9WXU2_9BURK 
ID   C9WXU2_9BURK            Unreviewed;       336 AA.
AC   C9WXU2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
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:CAU94907.1};
OS   Roseateles depolymerans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=76731 {ECO:0000313|EMBL:CAU94907.1};
RN   [1] {ECO:0000313|EMBL:CAU94907.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCUG 52220 {ECO:0000313|EMBL:CAU94908.1}, and Type strain: CCUG
RC   52219 {ECO:0000313|EMBL:CAU94907.1};
RX   PubMed=19661516; DOI=10.1099/ijs.0.011478-0;
RA   Gomila M., Pinhassi J., Falsen E., Moore E.R., Lalucat J.;
RT   "Kinneretia asaccharophila gen. nov., sp. nov., isolated from a freshwater
RT   lake, a member of the Rubrivivax branch of the family Comamonadaceae.";
RL   Int. J. Syst. Evol. Microbiol. 60:809-814(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; FM945420; CAU94907.1; -; Genomic_DNA.
DR   EMBL; FM945421; CAU94908.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9WXU2; -.
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; 3.30.565.10; 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; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
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   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.
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          152..326
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAU94907.1"
FT   NON_TER         336
FT                   /evidence="ECO:0000313|EMBL:CAU94907.1"
SQ   SEQUENCE   336 AA;  37491 MW;  29A5240337D31EE1 CRC64;
     DKHEPKRSAA EIALTELHAG GKFNQNSYKV SGGLHGVGVS CVNALSKWLR LTVRREGKVH
     QLEFRKGVPQ DRVIEVRDGF ETSPMKIVGE TDKRGTEVHF LPDTEIFTQN HEFHYDILAK
     RLRELSFLNN GVKIRLADER NNKEDNFAYS GGVRGFVEFI NKGKTTLHPN IFHAQGDKLS
     DQGTNIGVEV SMQWNDGFNE SVLCFTNNIP QRDGGTHLTG LRAAMTRVIN KYIEDNELAK
     KAKVDVSGDD MREGLACVVS VKVPEPKFSS QTKDKLVSSE VRGPVEEIVA AKLNDWLLEN
     PIDAKIICGK IVDAARAREA ARKAREMTRR KGVLDG
//
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