TOPS_BPT4
ID TOPS_BPT4 Reviewed; 160 AA.
AC P23992;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=DNA topoisomerase small subunit;
DE EC=5.6.2.2 {ECO:0000269|PubMed:226976};
DE AltName: Full=DNA topoisomerase 18-kDa subunit;
DE AltName: Full=Protein Gp60;
GN Name=60;
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 1-58 AND 82-99.
RX PubMed=2830666; DOI=10.1126/science.2830666;
RA Huang W.M., Ao S.-Z., Casjens S., Orlandi R., Zeikus R., Weiss R.,
RA Winge D., Fang M.;
RT "A persistent untranslated sequence within bacteriophage T4 DNA
RT topoisomerase gene 60.";
RL Science 239:1005-1012(1988).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-160.
RX PubMed=2379817; DOI=10.1093/genetics/125.2.237;
RA Daegelen P., Brody E.;
RT "The rIIA gene of bacteriophage T4. I. Its DNA sequence and discovery of a
RT new open reading frame between genes 60 and rIIA.";
RL Genetics 125:237-248(1990).
RN [4]
RP IDENTIFICATION IN THE DNA TOPOISOMERASE COMPLEX, CATALYTIC ACTIVITY,
RP FUNCTION, AND COFACTOR.
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).
RN [6]
RP TRANSLATIONAL BYPASSING.
RX PubMed=10835364; DOI=10.1093/emboj/19.11.2671;
RA Herr A.J., Gesteland R.F., Atkins J.F.;
RT "One protein from two open reading frames: mechanism of a 50 nt
RT translational bypass.";
RL EMBO J. 19:2671-2680(2000).
RN [7]
RP TRANSLATIONAL BYPASSING.
RX PubMed=23492219; DOI=10.1261/rna.037291.112;
RA Todd G.C., Walter N.G.;
RT "Secondary structure of bacteriophage T4 gene 60 mRNA: implications for
RT translational bypassing.";
RL RNA 19:685-700(2013).
RN [8]
RP TRANSLATIONAL BYPASSING.
RX PubMed=25041899; DOI=10.1038/ncomms5459;
RA Samatova E., Konevega A.L., Wills N.M., Atkins J.F., Rodnina M.V.;
RT "High-efficiency translational bypassing of non-coding nucleotides
RT specified by mRNA structure and nascent peptide.";
RL Nat. Commun. 5:4459-4459(2014).
RN [9] {ECO:0007744|PDB:5NP6}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 1-46, AND
RP TRANSLATIONAL BYPASSING.
RX PubMed=28630923; DOI=10.1126/sciadv.1700147;
RA Agirrezabala X., Samatova E., Klimova M., Zamora M., Gil-Carton D.,
RA Rodnina M.V., Valle M.;
RT "Ribosome rearrangements at the onset of translational bypassing.";
RL Sci. Adv. 3:e1700147-e1700147(2017).
CC -!- FUNCTION: Small 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 -!- MISCELLANEOUS: There is a 50-nucleotide untranslated region in the
CC coding sequence of gene 60. The ribosome apparently skips this region
CC while reading the mRNA. {ECO:0000269|PubMed:23492219,
CC ECO:0000269|PubMed:25041899, ECO:0000269|PubMed:2830666,
CC ECO:0000269|PubMed:28630923}.
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DR EMBL; M19728; AAA32490.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42506.1; -; Genomic_DNA.
DR EMBL; X52686; CAA36909.1; -; Genomic_DNA.
DR PIR; JT0209; ISBP24.
DR RefSeq; NP_049618.1; NC_000866.4.
DR PDB; 5NP6; EM; 3.60 A; C=1-46.
DR PDBsum; 5NP6; -.
DR SMR; P23992; -.
DR GeneID; 1258779; -.
DR KEGG; vg:1258779; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IMP:CACAO.
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; 3.40.50.670; -; 1.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR031660; TOPRIM_C.
DR Pfam; PF16898; TOPRIM_C; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA-binding;
KW Isomerase; Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..160
FT /note="DNA topoisomerase small subunit"
FT /id="PRO_0000145393"
SQ SEQUENCE 160 AA; 18630 MW; D4B8804C6462FF90 CRC64;
MKFVKIDSSS VDMKKYKLQN NVRRSIKSSS MNYANVAIMT DADHDGLGSI YPSLLGFFSN
WPELFEQGRI RFVKTPVIIA QVGKKQEWFY TVAEYESAKD ALPKHSIRYI KGLGSLEKSE
YREMIQNPVY DVVKLPENWK ELFEMLMGDN ADLRKEWMSQ
