ID   RGYR_SULAC              Reviewed;        1248 AA.
AC   Q08582; Q4JAH3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Reverse gyrase {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=rgy {ECO:0000255|HAMAP-Rule:MF_01125}; Synonyms=top-rg;
GN   OrderedLocusNames=Saci_0839;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=8389456; DOI=10.1073/pnas.90.10.4753;
RA   Confalonieri F., Elie C., Nadal M., de la Tour C.B., Forterre P.,
RA   Duguet M.;
RT   "Reverse gyrase: a helicase-like domain and a type I topoisomerase in the
RT   same polypeptide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:4753-4757(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8389456.
RA   Confalonieri F., Elie C., Nadal M., de la Tour C.B., Forterre P.,
RA   Duguet M.;
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3478-3478(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
RN   [4]
RP   MUTAGENESIS OF TYR-965.
RX   PubMed=10748189; DOI=10.1074/jbc.m910091199;
RA   Declais A.C., Marsault J., Confalonieri F., de La Tour C.B., Duguet M.;
RT   "Reverse gyrase, the two domains intimately cooperate to promote positive
RT   supercoiling.";
RL   J. Biol. Chem. 275:19498-19504(2000).
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.
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.
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   -!- PTM: The N-terminus is blocked.
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   -!- 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   -!- SEQUENCE CAUTION:
CC       Sequence=AAY80206.1; Type=Frameshift; Evidence={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; L10651; AAA72346.1; -; Genomic_DNA.
DR   EMBL; CP000077; AAY80206.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A47445; A47445.
DR   AlphaFoldDB; Q08582; -.
DR   SMR; Q08582; -.
DR   STRING; 330779.Saci_0839; -.
DR   EnsemblBacteria; AAY80206; AAY80206; Saci_0839.
DR   KEGG; sai:Saci_0839; -.
DR   PATRIC; fig|330779.12.peg.804; -.
DR   eggNOG; arCOG01526; Archaea.
DR   HOGENOM; CLU_002886_0_0_2; -.
DR   BRENDA; 5.6.2.2; 6160.
DR   Proteomes; UP000001018; 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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 1.
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   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
KW   Isomerase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Topoisomerase; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..1248
FT                   /note="Reverse gyrase"
FT                   /id="PRO_0000158090"
FT   DOMAIN          96..262
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   DOMAIN          625..789
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   ZN_FING         16..37
FT                   /note="C4-type"
FT                   /evidence="ECO:0000250"
FT   REGION          631..1248
FT                   /note="Topoisomerase I"
FT   MOTIF           219..222
FT                   /note="DEAD box"
FT   ACT_SITE        965
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         631
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         758
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         758
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   BINDING         760
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT   MUTAGEN         965
FT                   /note="Y->F: Loss of topoisomerase activity."
FT                   /evidence="ECO:0000269|PubMed:10748189"
SQ   SEQUENCE   1248 AA;  142746 MW;  16FA5EB2F032E49A CRC64;
     MQSLSDIPPS IYLFSCPNCG RSISTYRLLL GSVCNICLEE DKEYKNIGDL IKDIEKQGNL
     IKLKDIQRVL DDYESFVSVF RRLLGFPPFG PQKSWIYRLL SGESFAIIAP PGLGKTTFGL
     ISSIYLYLRG KKSILVFPTK SLVRQAIDKL SSYIQNLAEI KENPPKVIYY YSGMSASERK
     EADEGLQSKT FDIFISTNRF LIDNIDQISS TSYQFLFVDD VDTALKSSKS AQAILKLLGF
     TPSDQDKIKE SLKKYRENTQ KNEQNEYIFE EIDKIRKDRL ASKTVIFSSA TLNRSNPILT
     SLVGFKPGSS VIYIRKVYDM YVKQPDKEQE TFNLIKSLLH RLGDGGLIFV PVDKKQEYIK
     RLQSELSNEF NVAAITSTSA TKIDDFANGE IDVLIGSATH YGILVRGLDL PWRVKYSIFV
     GIPKFKFRLG EKVNLLTLSR LLSLIALITK DQEVIYISRR VKDKIRRLSP AALTMLSVQA
     KEGKLEDSIL LKAYDLLNKY LSNQNVLKRI SEIGDFVLSP DNDILIPDYL TYVQASGRTS
     RIYAGDVTTG LSILLVDDFN LFRLLNKKLQ YILDDIQWRE LDVEKWTAGD VEIKNLISKI
     NEERNEISKL KNEGNVAPAL QKVKTVLLVV ESPNKAKTIS SFFSRPSIRQ IGNMRVYETV
     LGDKVLMVTA SGGHVYDLTT QDMGIYGVDI MKQNSSLVFI PIYNSIKKCE NNHQFTDFFE
     SNKCPRCMTT KVRYDSLKSI NVLRNLAVEA DEVLIGTDPD TEGEKIAWDL YLALRPYNSN
     IRRAEFHEVT RKAILQAINQ PREFNVNLVK SQLVRRIEDR WIGFKLSSIL QTRFWPEYCK
     SLSSNKQLNC NENKNLSAGR VQTPVLSWIV DRYTEYQRNK SRVYYGKIDQ LQDIVIYVPK
     QDGVRKNSKI VVVFNEINQL EEEFGPLPPY TTDTLLSDSN NFFGLSAPET MRIAQDLFEL
     GLITYHRTDS NRISNTGISV AENYLKDVLG DKYTNIFKPR SWGDGGAHEG IRPTKPIDVE
     QLRLLIEEGE LELAKRLTNN HFKVYDIIFR RFISSQIIPL KVRKEIVKIE LYGENKKEKI
     NSNQNIIEVI TGITLPGIDT EISKFAYVPV RNVSRSVAER LKELGRSIPT DFSIEISNSF
     IKSTVNLYTQ ADLVMEMKNK KIGRPSTYAT IIGTILRRGY VLESLKTKKL IPTRLGVEVN
     KYLNENYGRF VSEDRTRKLL QLMDMVEAGQ EKYEEVLKQV YEEINEIR