ID X4ZN18_9BACL Unreviewed; 660 AA.
AC X4ZN18;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=PSAB_15465 {ECO:0000313|EMBL:AHV98000.1};
OS Paenibacillus sabinae T27.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1268072 {ECO:0000313|EMBL:AHV98000.1, ECO:0000313|Proteomes:UP000019772};
RN [1] {ECO:0000313|EMBL:AHV98000.1, ECO:0000313|Proteomes:UP000019772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T27 {ECO:0000313|EMBL:AHV98000.1,
RC ECO:0000313|Proteomes:UP000019772};
RX PubMed=24651173;
RA Xie J.B., Du Z., Bai L., Tian C., Zhang Y., Xie J.Y., Wang T., Liu X.,
RA Chen X., Cheng Q., Chen S., Li J.;
RT "Comparative Genomic Analysis of N2-Fixing and Non-N2-Fixing Paenibacillus
RT spp.: Organization, Evolution and Expression of the Nitrogen Fixation
RT Genes.";
RL PLoS Genet. 10:E1004231-E1004231(2014).
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};
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DR EMBL; CP004078; AHV98000.1; -; Genomic_DNA.
DR RefSeq; WP_025335498.1; NZ_CP004078.1.
DR AlphaFoldDB; X4ZN18; -.
DR STRING; 1268072.PSAB_15465; -.
DR KEGG; psab:PSAB_15465; -.
DR PATRIC; fig|1268072.3.peg.3197; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_1_2_9; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000019772; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005740; ParE_type2.
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 NCBIfam; TIGR01058; parE_Gpos; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF12; 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, ECO:0000313|EMBL:AHV98000.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 443..557
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 407..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 73509 MW; 99F05A878C4B183C CRC64;
MFEQVDMFAE VTKNGAADRT GYDADDIQVL EGLVAVRKRP GMYIGSTSSS GLHHLVWEIV
DNAVDEHLAK FCSKIDITLR KDGSVTVTDN GRGIPTGMHK TGIPTPQVVF TMLHAGGKFG
GSGYKKSGGL HGVGASVTNA LSEWLEVEIY REGKIHRQRF EYWVDNNGKE HVGEPVTGLE
VLGNTNKTGS KIMFKPDIRV FQGGISLNYD TLSERLQEIA FLNSGLRITL TDERSGRQDE
YYYEGGASEF VRYLNEGKDV LHDVIHFSAE KDEIEVEVAI QYNGGYTETI ASFVNSIPTR
SGGTHETGFK TAYTRVMNDY ARRTGLLKEK DKNLDGGDLR EGMMAVISIK MSEVEFVGQT
KDQLGSASAR SAVDFIVSEN MQRFLEENPQ VAQSLLKKSI QAARAREAAR KARDEIRSGK
KRSEGTNLGG KLTPAQSKDF SRTELFIVEG DSAGGSAKQG RDSKIQAILP LKGKPMNPEK
AKLAEILKND EYRAIISAIG AGIGSDFAVE DSNYSKIIIM TDADTDGAHI QVLLLTFFYR
YMKPLIDAGK VYIAQPPLYK LTRKSGKLET VRYAWTDEQL QNYLKEFGKN FELQRYKGLG
EMNPDQLWET TMNPETRTML QVQIEDAAKA ERRVSTLMGD KVDPRKRWIV ENVDFTEIVE
//
