TOP6A_SACSH
ID TOP6A_SACSH Reviewed; 389 AA.
AC O05208;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00132, ECO:0000305|PubMed:7961685};
DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
GN Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132};
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 212-221 AND
RP 344-352.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=9121560; DOI=10.1038/386414a0;
RA Bergerat A., de Massy B., Gadelle D., Varoutas P.-C., Nicolas A.,
RA Forterre P.;
RT "An atypical topoisomerase II from Archaea with implications for meiotic
RT recombination.";
RL Nature 386:414-417(1997).
RN [2]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBUNIT.
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=7961685; DOI=10.1016/s0021-9258(18)47037-8;
RA Bergerat A., Gadelle D., Forterre P.;
RT "Purification of a DNA topoisomerase II from the hyperthermophilic archaeon
RT Sulfolobus shibatae. A thermostable enzyme with both bacterial and eucaryal
RT features.";
RL J. Biol. Chem. 269:27663-27669(1994).
RN [3]
RP FUNCTION, COFACTOR, SUBUNIT, AND PROBABLE ACTIVE SITE.
RX PubMed=11485995; DOI=10.1074/jbc.m101823200;
RA Buhler C., Lebbink J.H., Bocs C., Ladenstein R., Forterre P.;
RT "DNA topoisomerase VI generates ATP-dependent double-strand breaks with
RT two-nucleotide overhangs.";
RL J. Biol. Chem. 276:37215-37222(2001).
RN [4] {ECO:0007744|PDB:2ZBK}
RP X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) IN COMPLEX WITH TOP6B AND RADICICOL,
RP AND SUBUNIT.
RX PubMed=18334211; DOI=10.1016/j.str.2007.12.020;
RA Graille M., Cladiere L., Durand D., Lecointe F., Gadelle D.,
RA Quevillon-Cheruel S., Vachette P., Forterre P., van Tilbeurgh H.;
RT "Crystal structure of an intact type II DNA topoisomerase: insights into
RT DNA transfer mechanisms.";
RL Structure 16:360-370(2008).
CC -!- FUNCTION: Relaxes both positive and negative supercoils and exhibits a
CC strong decatenase and unknotting activity; it cannot introduce DNA
CC supercoils (PubMed:7961685). ATP is absolutely required for DNA
CC cleavage; the nonhydrolyzable analog AMP-PNP generates nicked or linear
CC products from a supercoiled dsDNA substrate. Generates staggered two-
CC nucleotide long 5' overhangs. The enzyme is covalently attached
CC transiently to the 5'-ends of the cleaved strands (PubMed:11485995).
CC {ECO:0000269|PubMed:11485995, ECO:0000269|PubMed:7961685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00132,
CC ECO:0000305|PubMed:7961685};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132,
CC ECO:0000269|PubMed:11485995, ECO:0000269|PubMed:7961685};
CC -!- ACTIVITY REGULATION: Not inhibited by the DNA gyrase inhibitor
CC novobiocin, instead inhibited by eukaryotic topoisomerase inhibitors
CC such as m- and o-amsacrine, ellipticine, and the quinolone CP-115,953
CC (PubMed:7961685). {ECO:0000269|PubMed:7961685}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70-80 degrees Celsius.
CC {ECO:0000269|PubMed:7961685};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000255|HAMAP-Rule:MF_00132, ECO:0000269|PubMed:11485995,
CC ECO:0000269|PubMed:18334211, ECO:0000269|PubMed:7961685}.
CC -!- INTERACTION:
CC O05208; O05207: top6B; NbExp=5; IntAct=EBI-6430603, EBI-9026762;
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC Rule:MF_00132}.
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DR EMBL; Y10582; CAA71605.1; -; Genomic_DNA.
DR PDB; 2ZBK; X-ray; 3.56 A; A/C/E/G=1-389.
DR PDBsum; 2ZBK; -.
DR AlphaFoldDB; O05208; -.
DR SMR; O05208; -.
DR DIP; DIP-29417N; -.
DR IntAct; O05208; 1.
DR BRENDA; 5.6.2.2; 6162.
DR EvolutionaryTrace; O05208; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00132; Top6A; 1.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR004085; TopoVI_A.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA-binding;
KW Isomerase; Magnesium; Metal-binding; Nucleotide-binding; Topoisomerase.
FT CHAIN 1..389
FT /note="Type 2 DNA topoisomerase 6 subunit A"
FT /id="PRO_0000145456"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132,
FT ECO:0000305|PubMed:11485995"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ SEQUENCE 389 AA; 45055 MW; 6F617CB8231431B7 CRC64;
MSSEFISKVD KEARRKAANI LRDKFLNLVE QLKKGEPLVM EIPMRTLSNA IYDEKRKLLL
LGEKKLRRNF LDLNEAKRFM QTVLMASIIY DALVSDEYPT IRDLYYRGKH SLLLKSIEGN
KIVSEENTWD EQKESDSVIV DIEVFTSLLR EEMLILSKEK GKVVGNLRIR SGNDVIDLSK
TGHGAYAIEP TPDLIDFIDV DAEFVLVVEK DAVFQQLHRA GFWKQYKSIL ITSAGQPDRA
TRRFVRRLNE ELKLPVYILT DADPYGWYIF SVFRIGSISL SYESERLATP DAKFLGVSMG
DIFGNSRKKP YLSEAERKNY IIKAKDADIK RAEEIKNYEW FKTKAWQEEI NTFLQRKAKL
EIEAMASKGL KFLAFQYIPE KITNKDYIA
