ID A0A402BAF6_9CHLR Unreviewed; 698 AA.
AC A0A402BAF6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=gyrB_2 {ECO:0000313|EMBL:GCE28378.1};
GN ORFNames=KDA_38620 {ECO:0000313|EMBL:GCE28378.1};
OS Dictyobacter alpinus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=2014873 {ECO:0000313|EMBL:GCE28378.1, ECO:0000313|Proteomes:UP000287171};
RN [1] {ECO:0000313|Proteomes:UP000287171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno16 {ECO:0000313|Proteomes:UP000287171};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCE28378.1}.
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DR EMBL; BIFT01000001; GCE28378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402BAF6; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000287171; Unassembled WGS sequence.
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; 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; IPR002288; DNA_gyrase_B_C.
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; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF4; DNA TOPOISOMERASE 4 SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000287171}.
FT DOMAIN 481..595
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 698 AA; 78436 MW; 2334E33FC22A934B CRC64;
MFRSPNALPP VQDESDATHE QLSLFATRGT SEHSEDMISN KVEVKQATRT KKSASTYSSA
DIQVLEGIAA IRHRPGMYIG STSTSGLIHL IWEALDNAVD EAVAGYGKNI WVHIDQEGWV
TVRDEGRGMP FDPMRYQGEY LPAATVILTV PHSGGKFAEG AYKTAGGLHG VGSTVINALS
EKLELTIWKD GQQFFQTFSR GVAEPHEITA CDPKLHGTQL RWLYDRTIFD PDAYYSLESL
ESRLKAATYL NRGVTFHLNA WDDATSEQVE HVFYSRDGLP DYVRDLATTT STPLFKNVLN
IVKERDEVRV EVALQPTTGY KISMYSYANA VRTRDGGVHE TGFKAALTKV INDYALKWNI
IRNRERDGFR PEVIQQGLNV VISVKLTNPQ FQGQTKDRLN NAPVEGMVRS VVDEGLKDWF
ESNVGIGKEW LKRIQQMQKA RNEAQLVEEL ARAGTKKSGE LIDTTLSKKF LRCNTNDPSR
AELFIVEGDS AGGSAGQGRF SEFQAVLKLK GKPLNVAKAD LKSIVENEEI RTIINVLGTG
TRDFFDISGL KFNRVIIATD ADVDGLHIQC LLLTLFHQEF SDLIDLGHVY IACPPLYSVK
YKNKVHWLLD DDARIQFVRI HPDAQNLEFK RFKGLGEMNP KELRDTTLDP ARRMLKRVTM
EDGILAAKLV AELMEDKNAE RRRTFLAEHS RKIKELDV
//
