RGYR_SACSH
ID RGYR_SACSH Reviewed; 1166 AA.
AC P74759;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=topR;
OS Saccharolobus shibatae (Sulfolobus shibatae).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=2286;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX PubMed=8972852; DOI=10.1093/nar/24.23.4668;
RA Jaxel C., Bouthier de la Tour C., Duguet M., Nadal M.;
RT "Reverse gyrase gene from Sulfolobus shibatae B12: gene structure,
RT transcription unit and comparative sequence analysis of the two domains.";
RL Nucleic Acids Res. 24:4668-4675(1996).
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}.
CC -!- CAUTION: Ala-192 is present instead of the conserved Val which is part
CC of the DDVD box. {ECO:0000305}.
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DR EMBL; X98420; CAA67064.1; -; Genomic_DNA.
DR PIR; T29099; T29099.
DR AlphaFoldDB; P74759; -.
DR SMR; P74759; -.
DR BRENDA; 5.6.2.2; 6162.
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 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Repeat; Topoisomerase; Zinc;
KW Zinc-finger.
FT CHAIN 1..1166
FT /note="Reverse gyrase"
FT /id="PRO_0000158091"
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; 132080 MW; 88699E51300E2770 CRC64;
MINVMYKNSC PNCGGDISAD RLLNGLPCET CLPYINGIDG IDHISKVKAL YNILLDNDKI
KNYWNLYYNI TTFETVFKYF KDKTGYEPWS LQKLWLRRLV SNQSFTMSAP TGLGKTTTLM
TYSVFIGQDV VYIVPTKSLM EQVCKRLEKL GAQVSCGKVD QRKVSVITIS YLNKNADSIT
SYKPNFVAID DADAVIKSGK TTDRLVSLLG IPNDVYESAI QLIRLRNKYY FSNEFTEEIK
EKIRELELKI AEFKDKISQL VIASATIRPK GIKQKALRLL TGFEPSSIQL YARNIIDTYT
DNLDLSIIKE LGSGGLILVS KEYGRSRLNE IKKYVEDLGF NAKLAISGRK FLDDFSQGKV
DILVGSASYY GVAVRGIDEP KRLKYVIYYG VPKIKAKLFD ALSNPFTLLR VGKMIGVNFS
ELQNKILVLS PSEAQLLKFS IIKGETINYQ KLEQLRQELL YYISLVKDKL KEIGEETLIS
DNFVIAKQNT NYYIIYPDMI TYLQGSGRAS RLYNGGLTLG FSIILVDDKH IFEILKKKMQ
KLFPNTNFTS LSNINLSEIK TKLEESRKEE GNRVHFNIST GLLIVESPTK AKTIAKMFSR
PSVRVINKVP VYETIIVDGN QIYVLDVVAS KGHIVDLTLE DIGYYGIKIE YSGIIKPYYD
LIKKCLDCNK TFSIASDKCP YCGSTNVQTA QTTINLLREL ALSVDKVFIA SDPDTEGEKI
AYDLASFLSP YNSNIYRITY HEITKKAILE ALRNPMKINT NLVMSQIVRR IEDRWIGFTL
SNLLKTKFNG HNHGAGRVQT PVLGWIVDKT IKYKSAMGYV VYIDIAGYPI KMHFSERKKM
EEYINNLQVV KIEKIFEEKI LLSPLPPFTT DTLLIEANMK YKLPANLVMK IAQDLFEAGL
ITYHRTDSTH ISSVGIEIAK EYLQKQGLIK DFVPRSWESS EEGAHEAIRP TRAIDVNELI
QEIEENPYKY SIRFSKLHFL IYDLIFRRFM ASQMSHAVGT KSRYLIKLNK NDNINAELLS
NAEGGFIKVY PVKVYNLPLG EVKPKVNTGK GSSEQLLSYS DVISLMKSKG IGRPSTYAKT
IENLVRHGYI VSSKRKSYLI ATNRGISAYQ FLSSKFYDLV SEGTTAKLMS KLDDIALSKL
SASTVLLEIF SEISTLVNPL KSEQNV
