ID   RGYR2_SACS2             Reviewed;        1166 AA.
AC   Q97ZF5;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Reverse gyrase 2 {ECO:0000255|HAMAP-Rule:MF_01125};
DE   Includes:
DE     RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_01125};
DE              EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01125};
DE   Includes:
DE     RecName: Full=Topoisomerase {ECO:0000255|HAMAP-Rule:MF_01125};
DE              EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01125};
GN   Name=rgy2 {ECO:0000255|HAMAP-Rule:MF_01125}; OrderedLocusNames=SSO0963;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   INDUCTION BY VIRUS (MICROBIAL INFECTION).
RC   STRAIN=2-2-12;
RX   PubMed=18337566; DOI=10.1128/jvi.02583-07;
RA   Ortmann A.C., Brumfield S.K., Walther J., McInnerney K., Brouns S.J.,
RA   van de Werken H.J., Bothner B., Douglas T., van de Oost J., Young M.J.;
RT   "Transcriptome analysis of infection of the archaeon Sulfolobus
RT   solfataricus with Sulfolobus turreted icosahedral virus.";
RL   J. Virol. 82:4874-4883(2008).
CC   -!- FUNCTION: Modifies the topological state of DNA by introducing positive
CC       supercoils in an ATP-dependent process. It cleaves transiently a single
CC       DNA strand and remains covalently bound to the 5' DNA end through a
CC       tyrosine residue. May be involved in rewinding the DNA strands in the
CC       regions of the chromosome that have opened up to allow transcription or
CC       replication. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
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-
CC         Rule:MF_01125};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01125};
CC       Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01125};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC   -!- INDUCTION: (Microbial infection) At least 4-fold induced following
CC       infection by Sulfolobus turreted icosahedral virus 1 (STIV-1) in strain
CC       2-2-12. {ECO:0000269|PubMed:18337566}.
CC   -!- DOMAIN: Both the DNA unwinding and positive supercoiling activities
CC       require the cooperation of both domains. The cooperative action between
CC       the helicase-like and the topoisomerase domains is specific. The
CC       helicase-like domain probably does not directly unwind DNA but acts
CC       more likely by driving ATP-dependent conformational changes within the
CC       whole enzyme, functioning more like a protein motor. The 'latch' region
CC       of the N-terminal domain plays a regulatory role in the enzyme,
CC       repressing topoisomerase activity in the absence of ATP and therefore
CC       preventing the enzyme from acting as an ATP-independent relaxing
CC       enzyme; it also helps to coordinate nucleotide hydrolysis by the ATPase
CC       domain with the supercoiling activity of the topoisomerase domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01125}.
CC   -!- MISCELLANEOUS: This enzyme is the only unique feature of
CC       hyperthermophilic bacteria/archaea discovered so far. It appears to be
CC       essential for adaptation to life at high temperatures.
CC   -!- MISCELLANEOUS: Strain 2-2-12 is a substrain of P2 that is highly
CC       susceptible to infection by Sulfolobus turreted icosahedral virus 1
CC       (STIV-1). {ECO:0000269|PubMed:18337566}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase
CC       family. DDVD subfamily. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic type
CC       I/III topoisomerase family. {ECO:0000255|HAMAP-Rule:MF_01125}.
CC   -!- CAUTION: Ala-192 is present instead of the conserved Val which is part
CC       of the DDVD box. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006641; AAK41237.1; -; Genomic_DNA.
DR   PIR; F90247; F90247.
DR   RefSeq; WP_009992408.1; NC_002754.1.
DR   AlphaFoldDB; Q97ZF5; -.
DR   SMR; Q97ZF5; -.
DR   STRING; 273057.SSO0963; -.
DR   EnsemblBacteria; AAK41237; AAK41237; SSO0963.
DR   GeneID; 44129894; -.
DR   KEGG; sso:SSO0963; -.
DR   PATRIC; fig|273057.12.peg.961; -.
DR   eggNOG; arCOG01526; Archaea.
DR   HOGENOM; CLU_002886_0_0_2; -.
DR   InParanoid; Q97ZF5; -.
DR   OMA; VMTYIQA; -.
DR   PhylomeDB; Q97ZF5; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc 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; cd00186; TOP1Ac; 1.
DR   CDD; cd03361; TOPRIM_TopoIA_RevGyr; 1.
DR   Gene3D; 1.10.290.10; -; 1.
DR   Gene3D; 1.10.460.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   HAMAP; MF_01125; Reverse_gyrase; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005736; Reverse_gyrase.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034142; TOPRIM_RevGyr.
DR   InterPro; IPR040569; Znf_Rg.
DR   PANTHER; PTHR43505; PTHR43505; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF17915; zf_Rg; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF56712; SSF56712; 1.
DR   TIGRFAMs; TIGR01054; rgy; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA-binding; Helicase; Hydrolase; Isomerase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW   Topoisomerase; Zinc; Zinc-finger.
FT   CHAIN           1..1166
FT                   /note="Reverse gyrase 2"
FT                   /id="PRO_0000158093"
FT   DOMAIN          96..285
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   DOMAIN          580..743
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   ZN_FING         10..31
FT                   /note="C4-type 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   ZN_FING         665..682
FT                   /note="C4-type 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   REGION          586..1166
FT                   /note="Topoisomerase I"
FT   MOTIF           190..193
FT                   /note="DEAD box"
FT   ACT_SITE        903
FT                   /note="For DNA cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         109..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         586
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         712
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         712
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         714
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
SQ   SEQUENCE   1166 AA;  132077 MW;  F3929256A59F791D CRC64;
     MINVMYKNSC PNCGGDISGD RLLNGLPCEA CLPYINGIDD VDHISKVKTL YNILLNNDKI
     KNYWNLYYNI TTFETVFKYF RDKTGYEPWS LQKLWLRRLA SNQSFTMSAP TGLGKTTTLM
     TYSVFIGQDV VYIVPTKSLM EQVCKRLEKL GAQVSCGKID QKKVSVITIS YLNKNADSIV
     SLKPNFVVID DADAVIKSGK TTDRLVSLLG IPKDVYESAI QLIRLRNKYY FSNEYTEEVK
     EKIRELELKI AEFKDKISQL VIASATIRPK GIKQKALRLL TGFEPSSIQL YARNIIDAYT
     ENLDLSIVKE LGSGGLILVS KEYGRSKLNE IKKYVEDLGF NAKLAISGRK FLDDFSQGKV
     DILVGSASYY GVAVRGIDEP KRLKYVIYYG VPKIRAKLFD ALSNPFTLLR VGKLIGIDFS
     KLQNKILILN PSEVQLLKFS IIKGESINYH KLEQLRQELL YYMSLVKDKL KEKVEDTLIS
     DSFVITKQNG NYYIVYPDMI TYLQGSGRAS RLYNGGLTLG FSIILVDDRH IFEILEKKMQ
     KLFPNTTFTS LSNTNLSEIK IKLEDSRKEE GNRVHFNIST GLLIVESPTK AKTIAKMFSR
     PSVRIRNKVP VYETIIVDGN QIYVLDIVAS KGHIVDLTLE DIGYYGIKVE DDGTIKPYYD
     LIKKCLDCNK IFSSASDKCP YCGSANLQSA QTTINLLREL ALSVDKVFIA SDPDTEGEKI
     AYDLASFLSP YNSNVYRVVY HEITKKAILE ALRNPKKINT NLVMSQIVRR IEDRWIGFTL
     SNLLKTKFNG HNHGAGRVQT PVLGWIVNKT IKYKSAMGHV VYIDIAGYSI KKYFSEKRKV
     EEYINNLQVA RIEKISEEKI LLSPLPPFTT DTLLIEANMK YKLPANLVMK IAQDLFEAGL
     ITYHRTDSTH ISSVGIEIAK EYLQKQALIK EFVPRSWESS EEGAHEAIRP TRAIDVNELI
     QEIEENPYKY SIRFSKLHLL IYDLIFKRFI ASQMSHAVGT KSRYLIKLGK DDNVDVELLS
     NAEGGFIKVY PVKVYNLPVG EIQPKVNITK GSSEQLLSYS DVISLMKSKG IGRPSTYAKT
     IENLMKHGYI VSSKRKSYLI ATNRGISVYQ FLSSKFYDLV SESTTSRLMT KLDDIALSKL
     NASTVLLEIF SEISTLVNPL KSEQNV