ID   TOP5_BPT4               Reviewed;         442 AA.
AC   P07065;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=DNA topoisomerase medium subunit;
DE            EC=5.6.2.2 {ECO:0000269|PubMed:226976};
DE   AltName: Full=DNA topoisomerase 51-kDa subunit;
DE   AltName: Full=Protein Gp52;
GN   Name=52;
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].
RX   PubMed=3020513;
RA   Huang W.M.;
RT   "The 52-protein subunit of T4 DNA topoisomerase is homologous to the gyrA-
RT   protein of gyrase.";
RL   Nucleic Acids Res. 14:7379-7390(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RX   PubMed=3280805; DOI=10.1016/0022-2836(88)90320-8;
RA   Chapman D., Morad I., Kaufmann G., Gait M.J., Jorissen L., Snyder L.;
RT   "Nucleotide and deduced amino acid sequence of stp: the bacteriophage T4
RT   anticodon nuclease gene.";
RL   J. Mol. Biol. 199:373-377(1988).
RN   [5]
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   [6]
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: Medium subunit of the DNA topoisomerase that untwists
CC       superhelical DNA. Controls topological states of double-stranded DNA by
CC       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, ECO:0000269|PubMed:6296073}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. {ECO:0000305}.
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DR   EMBL; X04376; CAA27959.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42487.1; -; Genomic_DNA.
DR   PIR; B24705; ITBPT4.
DR   RefSeq; NP_049875.1; NC_000866.4.
DR   SMR; P07065; -.
DR   GeneID; 1258768; -.
DR   KEGG; vg:1258768; -.
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; 1.10.268.10; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW   Reference proteome; Topoisomerase.
FT   CHAIN           1..442
FT                   /note="DNA topoisomerase medium subunit"
FT                   /id="PRO_0000145391"
FT   ACT_SITE        117
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   442 AA;  50494 MW;  519E60AEE6F75AF7 CRC64;
     MQLNNRDLKS IIDNEALAYA MYTVENRAIP NMIDGFKPVQ RFVIARALDL ARGNKDKFHK
     LASIAGGVAD LGYHHGENSA QDAGALMANT WNNNFPLLDG QGNFGSRTVQ KAAASRYIFA
     RVSKNFYNVY KDTEYAPVHQ DKEHIPPAFY LPIIPTVLLN GVSGIATGYA TYILPHSVSS
     VKKAVLQALQ GKKVTKPKVE FPEFRGEVVE IDGQYEIRGT YKFTSRTQMH ITEIPYKYDR
     ETYVSKILDP LENKGFITWD DACGEHGFGF KVKFRKEYSL SDNEEERHAK IMKDFGLIER
     RSQNITVINE KGKLQVYDNV VDLIKDFVEV RKTYVQKRID NKIKETESAF RLAFAKAHFI
     KKVISGEIVV QGKTRKELTE ELSKIDMYSS YVDKLVGMNI FHMTSDEAKK LAEEAKAKKE
     ENEYWKTTDV VTEYTKDLEE IK