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Database: UniProt
Entry: D6DD00_BIFLN
LinkDB: D6DD00_BIFLN
Original site: D6DD00_BIFLN 
ID   D6DD00_BIFLN            Unreviewed;       772 AA.
AC   D6DD00;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=BIL_07970 {ECO:0000313|EMBL:CBK70371.1};
OS   Bifidobacterium longum subsp. longum F8.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=722911 {ECO:0000313|EMBL:CBK70371.1, ECO:0000313|Proteomes:UP000007063};
RN   [1] {ECO:0000313|EMBL:CBK70371.1, ECO:0000313|Proteomes:UP000007063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|EMBL:CBK70371.1,
RC   ECO:0000313|Proteomes:UP000007063};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Bifidobacterium longum longum F8.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK70371.1, ECO:0000313|Proteomes:UP000007063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|EMBL:CBK70371.1,
RC   ECO:0000313|Proteomes:UP000007063};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
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DR   EMBL; FP929034; CBK70371.1; -; Genomic_DNA.
DR   RefSeq; WP_008783099.1; NC_021008.1.
DR   AlphaFoldDB; D6DD00; -.
DR   KEGG; blg:BIL_07970; -.
DR   PATRIC; fig|722911.3.peg.149; -.
DR   HOGENOM; CLU_006146_4_1_11; -.
DR   Proteomes; UP000007063; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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_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; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CBK70371.1};
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          547..661
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          145..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   772 AA;  84669 MW;  1ECEA84B3F3F0169 CRC64;
     MPKEEYGAKD LAVLEGLDAV RKRPGMYIGT TDSQGLMHCL WEIIDNSVDE ALAGFCNDIV
     VTLHTDGSVE VADNGRGIPV DKEPKTGLSG VEVVLTKLHA GAKFGNSSYN AVGGLHGVGS
     SVVNALSSRL DVEVDRDGKT HHMTFHQGHP GVYTDADPAN PSPDSPFKRT RKNRPTELEI
     IGKVSPKTTG TRIRYWYDPE IFNKTAEFSY EQLIDRVRQT SFLVPGLKIT IIDENVPETA
     ATDTVEATDD TTVEPAQDQA PALDVSSNDA ELFDDSAESQ SDDAESPAEE DFSLTAGDQV
     VDGAFGEQPA HPRVVEFLHT GGVKDFVDFL SKGEPISDIW RIQGEGTYKE ETQAVGEGGE
     LHAQEIERTC GVDIALRWVN GYDTTIMSFV NIVETPGGGT HVDGFMNAIT KQIRKAVEDN
     ARKLKVNMKD SAMKVERDDI QAGLVAVVTA RVAEPQFQGQ TKDVLGTAQV KPIVTRLTDK
     QFGEMITGSK RGYKEQSGRV LEKIVGEMHA RIQSRKAKEV TRRKNALESA SMPAKLSDCQ
     PGNDDVAELF IVEGDSALGT AKAARNAGFQ ALLPIRGKIL NVQKASITQM LSNKECAAII
     QVVGAGSGQS FDIEQSRYHK IIMMTDADVD GAHIRILLLT LFYRYMRPLI EHGYVYAAVP
     PLHRIALTGS HKGEYIYTYS DDELAGKLAD LDKKHIGYND DIQRYKGLGE MDADQLADTT
     MDPRTRMLRR IRMEDAAQAS EIFSLLMGDD VPPRKQFIVD NADDFDRSKI DT
//
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