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Database: UniProt
Entry: Q68YT8_9FUSO
LinkDB: Q68YT8_9FUSO
Original site: Q68YT8_9FUSO 
ID   Q68YT8_9FUSO            Unreviewed;       522 AA.
AC   Q68YT8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 87.
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:AAT76295.1};
OS   Fusobacterium canifelinum.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=285729 {ECO:0000313|EMBL:AAT76295.1};
RN   [1] {ECO:0000313|EMBL:AAT76295.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-690 {ECO:0000313|EMBL:AAT76295.1};
RX   PubMed=15616329; DOI=10.1128/AAC.49.1.434-437.2005;
RA   Conrads G., Citron D.M., Goldstein E.J.;
RT   "Genetic determinant of intrinsic quinolone resistance in Fusobacterium
RT   canifelinum.";
RL   Antimicrob. Agents Chemother. 49:434-437(2005).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
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DR   EMBL; AY660895; AAT76295.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q68YT8; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd16928; HATPase_GyrB-like; 1.
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; IPR003594; HATPase_C.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          422..522
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         522
FT                   /evidence="ECO:0000313|EMBL:AAT76295.1"
SQ   SEQUENCE   522 AA;  57897 MW;  D04BA9DD43F68FCE CRC64;
     MEEIMSYEAQ NITVLEGLEA VRKRPGMYIG TTSERGLHHL VWEIVDNSVD EALAGYCNKI
     EVKILPENII EVVDNGRGIP TDIHPKYGKS ALEIVLTVLH AGGKFENDNY KVSGGLHGVG
     VSVVNALSEW LEVEVRKNGV VYYQKYHRGK PEEDVKIIGS CDEGEHGTIV RFKADGDIFE
     TLIYNYFTLS NRLKELAYLN KGLTIVLSDL RKEEKKEEIY KFDGGILDFL NEIVKEEATI
     IEKPFYVSSE QDNVGVDVTF TYTTSQNEVI YSFVNNINTH EGGTHVQGFR TALTKVINDV
     GKAQGLLKDK DGKLMGNDIR EGVVGIVSTK IPQPQFEGQT KGKLGNSEVS GIVNTIVSNS
     LKIFLEDNPN ITKIIIEKIL NSKKAREAAQ KARELVLRKS VLEVGSLPGK LADCTSKKAE
     ECEIFIVEGD SAGGSAKQGR DRYNQAILPL RGKIINVEKA GLHKSLESSE IRAMVTAFGT
     SIGETFDISK LRYGKIILMT DADVDGAHIR TLILTFLYRY MI
//
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