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Database: UniProt
Entry: E5WWG3_9BACE
LinkDB: E5WWG3_9BACE
Original site: E5WWG3_9BACE 
ID   E5WWG3_9BACE            Unreviewed;       640 AA.
AC   E5WWG3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=HMPREF1016_01011 {ECO:0000313|EMBL:EFV31119.1};
OS   Bacteroides eggerthii 1_2_48FAA.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV31119.1, ECO:0000313|Proteomes:UP000003246};
RN   [1] {ECO:0000313|EMBL:EFV31119.1, ECO:0000313|Proteomes:UP000003246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV31119.1,
RC   ECO:0000313|Proteomes:UP000003246};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA   Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL   Submitted (OCT-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   -!- 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:EFV31119.1}.
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DR   EMBL; ACWG01000008; EFV31119.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5WWG3; -.
DR   HOGENOM; CLU_006146_1_1_10; -.
DR   Proteomes; UP000003246; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd01030; TOPRIM_TopoIIA_like; 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; 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; 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:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
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}.
FT   DOMAIN          432..542
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   640 AA;  72928 MW;  1ACA7558C6F453A8 CRC64;
     MEDNNMTLPL EASADYEEKA TSANIGSNEV EYNEDNIRHL DDMEHIRVRS GMYIGRLGDG
     SQNDDGIYVL LKEVMDNSID EFKMGAGKRI EVNIEDNLRV SVRDYGRGIP QGKLVEAVSK
     LNTGGKYDSK AFKKSVGLNG VGIKAVNALS SRFEVRSYRD GKVRTVIFEK GVLQSDVTED
     STEENGTYIF FEPDNTLFLN YSFQNQFVET LLRNYTYLNT GLTFIYNGQR IISRHGLEDL
     LKDNMTSEGL YDIVHLKGED IEIAFTHTNQ YGEEYYSFVN GQHTTQGGTH QTALKEHIAR
     TIKEFYNKNQ DYADIRNGLV AAIAIDVEEP MFESQTKTKL GSNNMWPDGP TVNKYVGDFI
     KTEVDNFLHK NPLVTEVMLQ KIQDSEKERK AIAGVTKLAR ERAKKANLHN RKLRDCRFHL
     SDGKGKEQET DSCIFITEGD SASGSITKSR DVNTQAVFSL RGKPLNSYGL TKKVVYENEE
     FNLLQAALNI EDGIEGLRYN KVIVATDADV DGMHIRLLII TFFLQFFPDL IKKGHVYILQ
     TPLFRVRNKK KTNYCYTEDE RIKAIEELGP NPEITRFKGL GEISPDEFKH FIGKDMRLEQ
     VSLRKTDLVK ELLEFYMGKN TMERQNFIID NLVIEEDLAS
//
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