RGYR2_SULTO
ID RGYR2_SULTO Reviewed; 1233 AA.
AC Q975P6; F9VMV8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=STK_03740;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(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. {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; BA000023; BAK54255.1; -; Genomic_DNA.
DR RefSeq; WP_052846290.1; NC_003106.2.
DR AlphaFoldDB; Q975P6; -.
DR SMR; Q975P6; -.
DR STRING; 273063.STK_03740; -.
DR EnsemblBacteria; BAK54255; BAK54255; STK_03740.
DR GeneID; 1458298; -.
DR KEGG; sto:STK_03740; -.
DR PATRIC; fig|273063.9.peg.435; -.
DR eggNOG; arCOG01526; Archaea.
DR OMA; GVATYYG; -.
DR OrthoDB; 1837at2157; -.
DR Proteomes; UP000001015; 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..1233
FT /note="Reverse gyrase 2"
FT /id="PRO_0000158095"
FT DOMAIN 93..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 610..774
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT ZN_FING 13..34
FT /note="C4-type"
FT /evidence="ECO:0000250"
FT REGION 616..1233
FT /note="Topoisomerase I"
FT MOTIF 212..215
FT /note="DEAD box"
FT ACT_SITE 947
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 616
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 743
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 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 745
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
SQ SEQUENCE 1233 AA; 141175 MW; 7D48695C3DF700D2 CRC64;
MNTIPSSNYL SSCPNCGRVI SAERLYKGSV CSECLEEDRE FNSIRELVNE LSRLNKLNRL
NYIKEVLREY DIFVELFKRI IGFPPFGPQK SWIIRVLRKE SFAIIAPPGL GKTTFGIITS
LYFSSKNFRS ILIFPTRSLV KQAVDRISMY SNKTNIETKL LYYHSGINES QKQELYKALN
AGDFNIFIAT NRFFIDKINE LKNIKYDFMF VDDVDTALKS SKSAETILNL AGFSKDDILS
VKELLRKSRE DESVYTKIQE IRGNKLKGKT IVFSSATLTR GNPVLSALMG FRPGSSVIYL
RKIIDTYAYL PNNDDDVVNL LKELLNKLGE GGLIFVPVDK GQEYAKFLEA KLSDSFNVVT
ITSSNTNKIE DFANGNIYAL IGSATHYGIL VRGIDIPWRV KYAIFVGIPK FKFKIGEVMN
LVALSRILSM IGLITKDQDI VRLAGRVRGK LRKLSPAAIS MLTNQAREGK LEDETLLRAY
EVVNKYLEDK DILKKIAELG DLVISNGYIL MPDYLTYIQA SGRTSRIYGG ELTTGLSVLL
IDDINLFNIL NRKLSLILDE IIWQELQIKK NKIGSSDLTE IINKINEERE RILKVKKEGE
IEPSLQKVKT VLFIVESPNK AKTISNFFAK PSIRQLENIR AFETVLEDKI LIVAATGGHV
YDLTTQNIGI YGVEVQQQNS HFNFIPYYNT IKKCINGHQF TDFEQGNQCP KCHTTQIILD
KTATIDALRK LALEADEILI GTDPDTEGEK IAWDIYLALK PFNSNIKRAE FHEVTRKAIL
QAINNPRPFN VNLVKSQIVR RIEDRWIGFK LSTKLQEDFW KEYCKNYNCK SEENKNLSAG
RVQSPVLNWI VNRYDEYNAN KTKIYYGSIK GIDELKFYVF KQNEKIRKNA NIYVKIINTK
VLEEEINPLP PYTTDTLLYD ANQFYGISAS ETMKIAQDLF ELGLITYHRT DSTRISNTGI
SIAEGYLKQI AGENYTKIFK PRSWGEGGAH EAIRPTRPLD VDQLRLLVDE GEIELAKKIT
RAHFLIYDLI FRRFITSQLV PLKVIKERIE YKICEDSNCN SELKTLQNYS EFITDIKLPI
QLDYSKFLYL PTTRIIKNSI IKKLQETTGS TNAELVSKIQ LTGSFVKSTV NLYTQAELVA
EMKRKEIGRP STYATIISTI LKRGYVIESK KTKKLIPTQL GKEVNKYLNQ KFSSFVSEER
TRNLLQLMDM VEQGKQDYIQ ILKDIYYEIK SIR
