RGYR1_SACS2
ID RGYR1_SACS2 Reviewed; 1242 AA.
AC Q97ZZ8;
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 1 {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=rgy1 {ECO:0000255|HAMAP-Rule:MF_01125}; OrderedLocusNames=SSO0420;
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).
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 (By similarity). Its activity is inhibited by the DNA-
CC binding protein 7d (Sso7d), suggesting that the Sso7d activity might
CC counteract the overwinding effect of reverse gyrase.
CC {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 -!- 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 -!- 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}.
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DR EMBL; AE006641; AAK40747.1; -; Genomic_DNA.
DR PIR; D90186; D90186.
DR RefSeq; WP_009988760.1; NC_002754.1.
DR AlphaFoldDB; Q97ZZ8; -.
DR SMR; Q97ZZ8; -.
DR STRING; 273057.SSO0420; -.
DR PRIDE; Q97ZZ8; -.
DR EnsemblBacteria; AAK40747; AAK40747; SSO0420.
DR GeneID; 44129399; -.
DR KEGG; sso:SSO0420; -.
DR PATRIC; fig|273057.12.peg.414; -.
DR eggNOG; arCOG01526; Archaea.
DR HOGENOM; CLU_002886_0_0_2; -.
DR InParanoid; Q97ZZ8; -.
DR OMA; GVATYYG; -.
DR PhylomeDB; Q97ZZ8; -.
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; 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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1242
FT /note="Reverse gyrase 1"
FT /id="PRO_0000158092"
FT DOMAIN 97..298
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 619..785
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 625..1242
FT /note="Topoisomerase I"
FT MOTIF 214..217
FT /note="DEAD box"
FT ACT_SITE 965
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 625
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 754
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 754
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 756
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
SQ SEQUENCE 1242 AA; 141668 MW; EE4C1990F01F26FB CRC64;
MTSINKVPPS IYTRSCPNCG GNISSQRLFN GSVCESCLKD DREFSNLSDL INILSENSNL
KNLTQIRDVL EEYKKVEEIF GKLLNNSKPI GPQRSWTIRF LRGESFAIIA PPGLGKTTFG
LIMSLYNATR NRKSIIIFPT RTLISQTVDK LAKFSELYSY SPRILYNKQS PTQTENILDQ
LKSGNFDIFI STNRFVIQNL SELSNIKFDF IFVDDVDAAL KSGKSAKAIL RLVGFTDEDI
QTTMKLLREN IGEEEKFGKI QEIRESRLKD KIVIFSSATI SRGNPILSSL MGFRPGSSVI
YLRNIYDSYI DLTQTCKGQD FEECTLGTVI KLLKRLNDGT LIFVPIDKGA QYADYLASNL
RDHGINVESV ASSSISKLEK FERGEVSSLV GVATHYGVLV RGIDLPWRVK YSIFVGIPKF
KFKIGEYMHP LALTRLLSLV YLVKNDDKVR GLLSYIRKRL RKISPAALAM LAKDIREGKI
DDERLKEAYN LVNEYLKDNE FLKKVSDVGD LVIEGDYILM PDYLTYIQAS GRTSRLYGAN
LTTGLSVLLI DNSRLFELLN KKLNLILDEV KWYSLDIDAD KLGQVSLSDI SAKITEERES
LSKIKKEGNV ESSSLSVKTT LFIVESPNKA KTISNFFSRP STRSYGKLRV YETVLGDRVL
IVAASGGHIY DLITEDESEK QDDNYVYGVL VKDSKFIPIY STIKKCEKGH QIVKDLSQNK
CPICGSRIVT DKTEVVDILR KLALEVDEVL IGTDPDTEGE KIAWDIYLAI RPFNGNIKRA
EFHEVTRRAI LNAIKNPREF NDNLVKSQIV RRIEDRWIGF KLSRKLQTEF WEQHCTSISK
KNSKDEECKE NRNLSAGRVQ TPVLDWVVNR YQKYNENKKK YLIIESQDKS IFPFSVLALK
KNGLSKNTQI IIHLEDINIK EEEFGPLPPY TTDTLLSDAA NLLRIPASDT MRVAQDLFEL
GLITYHRTDS TRVSNVGISV AETYLKSKQV DISKIFRPRS WGEGGAHEAI RPTKPLDETM
LKASIEQGDL ELSKQLTFNH FRVYNLIFRR FITSQLPPLV VTKQIVRIRA YTKDNIELEL
DENKKEFVIG YKLKEGDEFR QTLQDAIYTL FRLYQPLDEK MKGKELSATI TGTLNKSDVQ
LYTEGELISE MKSKQIGRPS TYAVIISTLK KRRYIIESKN LKKIIPTKLG MAVKEYLMEN
YKQIVSEKRT VKLLEKMNEV EEGKVDYLVL LKELYNEIQT IS
