ID A0A4R0W5K2_BIFLN Unreviewed; 771 AA. AC A0A4R0W5K2; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 03-MAY-2023, entry version 11. DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895}; DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895}; GN ORFNames=MCC10128_1303 {ECO:0000313|EMBL:TCF82553.1}; OS Bifidobacterium longum subsp. longum. OC Bacteria; Actinomycetota; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1679 {ECO:0000313|EMBL:TCF82553.1, ECO:0000313|Proteomes:UP000293683}; RN [1] {ECO:0000313|EMBL:TCF82553.1, ECO:0000313|Proteomes:UP000293683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCC10128 {ECO:0000313|EMBL:TCF82553.1, RC ECO:0000313|Proteomes:UP000293683}; RX PubMed=29311585; DOI=.1038/s41598-017-18391-x; RA Odamaki T., Bottacini F., Kato K., Mitsuyama E., Yoshida K., Horigome A., RA Xiao J.Z., van Sinderen D.; RT "Genomic diversity and distribution of Bifidobacterium longum subsp. longum RT across the human lifespan."; RL Sci. Rep. 8:85-85(2018). 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:TCF82553.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; SHTO01000022; TCF82553.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4R0W5K2; -. DR Proteomes; UP000293683; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt. 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; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_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; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. FT DOMAIN 546..660 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT REGION 145..170 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 771 AA; 84558 MW; 6B798E4D96B17B58 CRC64; MPKEEYGAKD LAVLEGLDAV RKRPGMYIGT TDSQGLMHCL WEIIDNSVDE ALAGFCNDIV VTLHTDGSVE VADNGRGIPV DKEPKTGLSG VEVVLTKLHA GAKFGNSSYN AVGGLHGVGS SVVNALSSRL DVEVDRDGKT HHMTFHQGHP GVYTDADPAN PSPDSPFKRT RKNRPTELEI IGKVSPKTTG TRIRYWYDPE IFNKTAEFSY EQLIDRVRQT SFLVPGLKIT IVDENVPETA TDTAEAIDAD AVEPAQDQAP ALDVSSNDAE LFDDSTEAQA DSTESLSEED FSLTAGDQVV DGAFGEQPAH PRVVEFLHTG GVKDFVDFLS KGEPISDIWR IQGEGTYKEE TQAVGKGGEL HAQEIERTCG VDIALRWVNG YDTTIMSFVN IVETPGGGTH VDGFMNAITK QIRKAVEDNA RKLKVNMKDS AMKVERDDIQ AGLVAVVTAR VAEPQFQGQT KDVLGTAQVK PIVTRLTDKQ FGEMITGSKR GYKEQSGRVL EKIVGEMHAR IQSRKAKEVT RRKNALESAS MPAKLSDCQP GNDDVAELFI VEGDSALGTA KAARNAGFQA LLPIRGKILN VQKASITQML SNKECAAIIQ VVGAGSGQSF DIEQSRYHKI IMMTDADVDG AHIRILLLTL FYRYMRPLIE HGYVYAAVPP LHRIALTGSH KGEYIYTYSD DELAGKLADL DKKRIGYNDD IQRYKGLGEM DADQLADTTM DPRTRMLRRI RMEDAAQASE IFSLLMGDDV PPRKQFIVDN ADDFDRSKID T //