ID   TOPL_BPT4               Reviewed;         516 AA.
AC   P09176;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=DNA topoisomerase large subunit;
DE            EC=5.6.2.2 {ECO:0000269|PubMed:226976};
DE   AltName: Full=DNA topoisomerase 64-kDa subunit;
DE   AltName: Full=Protein Gp39;
GN   Name=39;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RX   PubMed=3022233; DOI=10.1093/nar/14.19.7751;
RA   Huang W.M.;
RT   "Nucleotide sequence of a type II DNA topoisomerase gene. Bacteriophage T4
RT   gene 39.";
RL   Nucleic Acids Res. 14:7751-7765(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Huang W.M.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [4]
RP   IDENTIFICATION IN THE DNA TOPOISOMERASE COMPLEX, CATALYTIC ACTIVITY, AND
RP   FUNCTION.
RX   PubMed=226976; DOI=10.1073/pnas.76.8.3737;
RA   Stetler G.L., King G.J., Huang W.M.;
RT   "T4 DNA-delay proteins, required for specific DNA replication, form a
RT   complex that has ATP-dependent DNA topoisomerase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 76:3737-3741(1979).
RN   [5]
RP   IDENTIFICATION IN THE DNA TOPOISOMERASE COMPLEX.
RX   PubMed=6296073; DOI=10.1016/s0021-9258(18)33182-x;
RA   Seasholtz A.F., Greenberg G.R.;
RT   "Identification of bacteriophage T4 gene 60 product and a role for this
RT   protein in DNA topoisomerase.";
RL   J. Biol. Chem. 258:1221-1226(1983).
CC   -!- FUNCTION: Large subunit of the DNA topoisomerase that untwists
CC       superhelical DNA. Controls of topological states of double-stranded DNA
CC       by transient breakage and subsequent rejoining of DNA strands.
CC       {ECO:0000269|PubMed:226976}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000269|PubMed:226976};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:226976};
CC   -!- SUBUNIT: Part of the DNA topoisomerase complex made of gp39, gp52 and
CC       gp60. {ECO:0000269|PubMed:226976}.
CC   -!- MISCELLANEOUS: Binds both single and double-stranded DNA.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR   EMBL; X06220; CAA29569.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42462.1; -; Genomic_DNA.
DR   PIR; A25763; ISBPT4.
DR   RefSeq; NP_049621.1; NC_000866.4.
DR   SMR; P09176; -.
DR   GeneID; 1258807; -.
DR   KEGG; vg:1258807; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
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; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; DNA-binding; Isomerase;
KW   Nucleotide-binding; Reference proteome; Topoisomerase.
FT   CHAIN           1..516
FT                   /note="DNA topoisomerase large subunit"
FT                   /id="PRO_0000145392"
FT   DNA_BIND        369..400
FT                   /evidence="ECO:0000255"
FT   BINDING         128..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   516 AA;  57977 MW;  A9F7B81659E61768 CRC64;
     MIKNEIKILS DIEHIKKRSG MYIGSSANET HERFMFGKWE SVQYVPGLVK LIDEIIDNSV
     DEGIRTKFKF ANKINVTIKN NQVTVEDNGR GIPQAMVKTP TGEEIPGPVA AWTIPKAGGN
     FGDDKERVTG GMNGVGSSLT NIFSVMFVGE TGDGQNNIVV RCSNGMENKS WEDIPGKWKG
     TRVTFIPDFM SFETNELSQV YLDITLDRLQ TLAVVYPDIQ FTFNGKKVQG NFKKYARQYD
     EHAIVQEQEN CSIAVGRSPD GFRQLTYVNN IHTKNGGHHI DCAMDDICED LIPQIKRKFK
     IDVTKARVKE CLTIVMFVRD MKNMRLIRQT KERLTSPFGE IRSHIQLDAK KISRDILNNE
     AILMPIIEAA LARKLAAEKA AETKAAKKAS KAKVHKHIKA NLCGKDADTT LFLTEGDSAI
     GYLIDVRDKE LHGGYPLRGK VLNSWGMSYA DMLKNKELFD ICAITGLVLG EKAFEEKEDG
     EWFTFELNGD TIIVNENDEV QINGKWITVG ELRKNL