ID E1CHQ9_9BURK Unreviewed; 426 AA.
AC E1CHQ9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-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:BAJ12094.1};
OS Pandoraea oxalativorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=573737 {ECO:0000313|EMBL:BAJ12094.1};
RN [1] {ECO:0000313|EMBL:BAJ12094.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA25 {ECO:0000313|EMBL:BAJ12094.1};
RA Sahin N., Tani A., Kotan R., Sedlacek I., Kimbara K., Tamer A.U.;
RT "Pandoraea oxalativorans sp. nov., Pandoraea faecigallinarum sp. nov. and
RT Pandoraea vervacti sp. nov., isolated from oxalate-enriched culture.";
RL Int. J. Syst. Evol. Microbiol. 61:2247-2253(2011).
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; AB553287; BAJ12094.1; -; Genomic_DNA.
DR AlphaFoldDB; E1CHQ9; -.
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; 3.40.50.670; -; 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 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; 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 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 313..426
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAJ12094.1"
FT NON_TER 426
FT /evidence="ECO:0000313|EMBL:BAJ12094.1"
SQ SEQUENCE 426 AA; 47529 MW; C9D3F5A2165226AB CRC64;
GVGVSCVNAL STYLKLTVRR DGKKHFMEFH QGVPQNRELE MVDGVETSPL KLLGDTDKRG
TEVHFLADET IFGKVEYHYD ILAKRMRELS FLNNGVRIRL TDQRTGKEDD FAFGGGVKGF
VEYINKSKTV LHPTVFHVMG ERDGIGVEVA MQWNDSYNET VLCFTNNIPQ RDGGSHLTGL
RAAMTRVINK YIAESEIAKK AKVETTGDDM REGLTCVLSV KVPEPKFSSQ TKDKLVSSEV
RAPVEEYVAK ALEDFLQETP NDAKIICTKI VEAARARDAA RKAREMTRRK GVLDGVGLPG
KLADCQEKDP ALCEIYVVEG DSAGGSAKQG RDRKFQAILP LRGKVLNVEK ARFDKLISSE
QIVTLITALG CGIGKDDYNI DKLRYHRIII MTDADVDGAH IRTLLLTFLY RQGPELIERG
YVYIAH
//
