ID F2QKG4_9FLAO Unreviewed; 427 AA.
AC F2QKG4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:CBY89181.1};
OS Flavobacterium sp. R-40835.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=944693 {ECO:0000313|EMBL:CBY89181.1};
RN [1] {ECO:0000313|EMBL:CBY89181.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R-40835 {ECO:0000313|EMBL:CBY89181.1};
RA Peeters K., Willems A.;
RT "The gyrB gene is a useful phylogenetic marker for exploring the diversity
RT of Flavobacterium strains isolated from terrestrial and aquatic habitats in
RT Antarctica.";
RL FEMS Microbiol. Lett. 321:130-140(2011).
RN [2] {ECO:0000313|EMBL:CBY89181.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R-40835 {ECO:0000313|EMBL:CBY89181.1};
RA Peeters K.H.A.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; FR772312; CBY89181.1; -; Genomic_DNA.
DR AlphaFoldDB; F2QKG4; -.
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 346..427
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBY89181.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:CBY89181.1"
SQ SEQUENCE 427 AA; 47293 MW; 9E160FAEB0C68939 CRC64;
VGIHKKEGVS ALEVVMTKIG AGGKFDKDSY KVSGGLHGVG VSVVNALSNH LRATVHSSDG
KVYEQEYEKG KALYPVKQIG ETTKRGTIVT FYPDPSIFTQ TIEYSYDTLS ARMRELSFLN
KGITITFTDK REVDKEGNFV SEIFHSDEGL KEYIRYLDGN REPIIAHVIS MDHEKGEIPV
EVALIYNTSY TENIFSYVNN INTHEGGTHL QGFRTGLTRS LKKYADASGM LDKLKFDISG
DDFREGLTAI ISVKVQEPQF EGQTKTKLGN REVVSPVSQA VSEMIENYLE ENPNDARIIV
QKVILAAQAR HAAKKAREMV QRKTVMGGGG LPGKLSDCSE QDPAKCEVYL VEGDSAGGTA
KQGRDRAFQA ILPLRGKILN VEKAMHHKVF ENEEIRNIFT ALGVTVGTEE DSKALNISKL
RYHKVII
//
