ID Q8RQY3_9BACT Unreviewed; 391 AA.
AC Q8RQY3;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 84.
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:BAB88361.1};
OS CFB-group bacterium QA93A.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=173727 {ECO:0000313|EMBL:BAB88361.1};
RN [1] {ECO:0000313|EMBL:BAB88361.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12542710; DOI=10.1046/j.1462-2920.2003.00382.x;
RA Matsuo Y., Suzuki M., Kasai H., Shizuri Y., Harayama S.;
RT "Isolation and phylogenetic characterization of bacteria capable of
RT inducing differentiation in the green alga Monostroma oxyspermum.";
RL Environ. Microbiol. 5:25-35(2003).
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; AB073059; BAB88361.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RQY3; -.
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, ECO:0000313|EMBL:BAB88361.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 314..391
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAB88361.1"
FT NON_TER 391
FT /evidence="ECO:0000313|EMBL:BAB88361.1"
SQ SEQUENCE 391 AA; 43337 MW; C0D5DC45153B3C4E CRC64;
VSGGLHGVGV SCVNALSDHL TATVHKEGKI WQQEYERGKT LYPVKTIGDT DFTGTIVTFL
PDKSIFQQTT EYNYDTLATR MRELAYLNKG ITITLTDKRN QDDEGNDISE VFHSEEGLSE
FVKFLDGTRT QIIQDVISME GEKNGIPVEV AMVYNDSYAE NLHSYVNNIN THEGGTHLSG
FRRGLTHTLK KYADESGLLK NVKFEIAGDD FREGLTAIVS VKVAEPQFEG QTKTKLGNRE
VSAAVSQAVS EMLTDYLEEN PNDAKTIVQK VILAAQARHA ARKAREMVQR KTVMSIGGLP
GKLSDCSETD PAQCEIFLVE GDSAGGTAKQ GRDRNFQAIL PLRGKILNVE KAMQHKVFEN
EEIKNMFTAL GVSIGTEDDP RELNLSKLRY H
//
