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Database: UniProt
Entry: F2XFJ6_RHIRD
LinkDB: F2XFJ6_RHIRD
Original site: F2XFJ6_RHIRD 
ID   F2XFJ6_RHIRD            Unreviewed;       358 AA.
AC   F2XFJ6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
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:AEA36055.1};
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358 {ECO:0000313|EMBL:AEA36055.1};
RN   [1] {ECO:0000313|EMBL:AEA36055.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=131ab {ECO:0000313|EMBL:AEA36055.1};
RA   Pulawska J., Kaluzna M.;
RT   "Phylogenetic relationship and genetic diversity of Agrobacterium spp.
RT   isolated in Poland based on gyrB gene sequence analysis and RAPD.";
RL   Eur. J. Plant Pathol. 133:379-390(2012).
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; HQ438210; AEA36055.1; -; Genomic_DNA.
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          310..358
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEA36055.1"
FT   NON_TER         358
FT                   /evidence="ECO:0000313|EMBL:AEA36055.1"
SQ   SEQUENCE   358 AA;  39405 MW;  139A1159CEA5404C CRC64;
     VSGGLHGVGV SVVNALSVWL KLRIRRNGKL HEIGFTHGVA DAPLSVIGEY EGRSGTEVTF
     LASPDTFTMT DYDFGTLEHR LRELAFLNSG VRIVLTDKRH SDIKQEELLY DGGLEAFVRY
     LDRAKKPLVD KPVAIHGEKD GITVEVALWW NDSYHENVLC FTNNIPQRDG GTHMAGFRAA
     LTRQMTSYAE TSGIMKREKV SLQGEDCREG LTAILSVKVP DPKFSSQTKD KLVSSEVRPV
     VESLVNEALS TWLEEHPSDA KILVGKVVEA AIAREAARKA RELTRRXGAL DIASLPGKLA
     DCSERDPAKS ELFLVEGDSA GGSAKQGRSR ETQAILPLRG KILNVERARF DKMLSTQE
//
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