GenomeNet

Database: UniProt
Entry: A0A087CDS3_9BIFI
LinkDB: A0A087CDS3_9BIFI
Original site: A0A087CDS3_9BIFI 
ID   A0A087CDS3_9BIFI        Unreviewed;       801 AA.
AC   A0A087CDS3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=BPSY_1831 {ECO:0000313|EMBL:KFI81423.1};
OS   Bifidobacterium psychraerophilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=218140 {ECO:0000313|EMBL:KFI81423.1, ECO:0000313|Proteomes:UP000029050};
RN   [1] {ECO:0000313|EMBL:KFI81423.1, ECO:0000313|Proteomes:UP000029050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21775 {ECO:0000313|EMBL:KFI81423.1,
RC   ECO:0000313|Proteomes:UP000029050};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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}.
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:KFI81423.1}.
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; JGZI01000010; KFI81423.1; -; Genomic_DNA.
DR   RefSeq; WP_033495251.1; NZ_JGZI01000010.1.
DR   AlphaFoldDB; A0A087CDS3; -.
DR   STRING; 218140.BPSY_1831; -.
DR   eggNOG; COG0187; Bacteria.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000029050; 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: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:KFI81423.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029050};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          576..690
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          147..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  87545 MW;  D2C4D3BA481A9DA2 CRC64;
     MAKSYGAESL TILEGLDAVR KRPGMYIGTT DSQGLMHCLW EIIDNSVDEA LAGACTNIEV
     TLHQDASITV ADNGRGIPVD VEPKTGLTGV EVVLTKLHAG AKFGNSSYNA VGGLHGVGSS
     VVNALSARFD VEVDRDGKTY RMEFKQGHPG VYEDTADGNP SPDAPFKRTR RNKPTELRVV
     AKVPAKRTGT RIRYWADPEI FNSTATFSYE QLIERVRQTS FLVPGLKITV IDENIAENTG
     ENTAENLNEN IAAQDVIDAD AMSDVAVREA GPSDGPESGT SVAESADQAA PDEMDGDLSG
     DAESDAMASD EARSDDDAED DAAESDAVST GLHRESGLHH PRVQEFLHSG GVVDFVDFLS
     KGEAINDIWH ISGEAEYEEE TQKVVEGGQL HAEKVRRTCG VDIALRWVNG YDTTLLSFVN
     VVETPGGGMH VDGFLNALTR QVRKTVESNA RKLKVNLRDS HSKIERDDVL AGLVAVVTAR
     IAEPQFQGQT KDVLGTAQVK PIVTRMTDKQ FSEMISGSKR GFKEQSSRVL EKIVGEMHAR
     VQARKTKEVT RRKNALESAS MPAKLSDSQP GNDDIAELFI VEGDSALGTA KAARNSMFQA
     LLPIRGKILN VQKASVSQML SNKECAAIIQ VIGAGSGASF DITQSRYNKV IMMTDADVDG
     AHIRILLLTL FYRYMRPLVE AGHVYAAVPP LHRIALAGKR KGEYIYTYSD DELAGKLAEL
     KKQRIDFHED IQRYKGLGEM DADQLADTTM DPRSRMLRRI RMEDAEHASD VFSLLMGDDV
     PPRKQFIVEN ADDFDRSKID T
//
DBGET integrated database retrieval system