RGYR2_AQUAE
ID RGYR2_AQUAE Reviewed; 1159 AA.
AC O67226;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=topG2;
GN OrderedLocusNames=aq_1159;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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: Ile-198 is present instead of the conserved Val which is part
CC of the DDVD box. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC07187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000657; AAC07187.1; ALT_INIT; Genomic_DNA.
DR PIR; G70399; G70399.
DR RefSeq; NP_213790.1; NC_000918.1.
DR AlphaFoldDB; O67226; -.
DR SMR; O67226; -.
DR STRING; 224324.aq_1159; -.
DR PRIDE; O67226; -.
DR EnsemblBacteria; AAC07187; AAC07187; aq_1159.
DR KEGG; aae:aq_1159; -.
DR PATRIC; fig|224324.8.peg.903; -.
DR eggNOG; COG1110; Bacteria.
DR HOGENOM; CLU_002886_0_0_0; -.
DR InParanoid; O67226; -.
DR OMA; MASQMRP; -.
DR OrthoDB; 223233at2; -.
DR Proteomes; UP000000798; 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 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..1159
FT /note="Reverse gyrase 2"
FT /id="PRO_0000158081"
FT DOMAIN 86..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT DOMAIN 587..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 REGION 593..1159
FT /note="Topoisomerase I"
FT MOTIF 196..199
FT /note="DEAD box"
FT ACT_SITE 902
FT /note="For DNA cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01125"
FT BINDING 593
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 1159 AA; 134557 MW; 20FB48491E3244B9 CRC64;
MALELIERGC PNCGGVISSD RLEKGLPCSK CLPKPTEEKV CDALEELKTL KYLKPFCDTD
KSLERFINFF EKAVGAKPWS LQRVWAKRVF MNQSFAIVAP TGVGKTTFGL VMSLFLKGRV
LAIFPTRLLA QQAGDRLSEL AQKVGVNKKI LIYQSKKNIR EQFLNGDWDI LLGTNMFLHK
NFENLINFKF KLIFIDDIDS FLKRGKNVDY LFKLLGFSGE EIKLALKENK TQRDYDRLAR
IRKRKRDTVL IVSSATLKPR GKRAYLFRNL LGFDVQKAIT TLRNIVDVAE PVKDLEEALE
KSVELIKKLG KGGLVYLSVF YGKDKVQEVK EFYRKHGINA VSYLDYKPEE LYQILEKGEF
DVAVGISHIT NPLVRGIDLP HIIRYAVFLD PPKHVFPTEL TLSPPLLHGL LLTLLNLFEG
DDRLKAIQYV MYLKRYLTLR EEQLDNYPRI KERVEEIKNF LENYLKDENF LKKIKESEDI
SLVPKEGKLY IVVGDANSYI QASGRTSRFI AGGMTKGLSV VYYSDPKAFY SLKKRLALYY
MTQEIEFKRL SEVDLNKLIK EIDEDRKRAR EILQGKGVAQ IKDLFKTTLV IVESPNKART
IAGFFGKPQM RLVEDSVAYE VPLGDRLLVI TASLGHVLDL VTDKGFFGVL DDTYPYLPVY
DTIKICRETH EQHTEYEYLK KRCKGKIEDK LEIIKGVREV SYEVDEVFIA TDPDAEGEKI
GYDLYLLSKP FNFNIKRAEF HEVTPKAFRE AIQNPREVDL NLVKAQLVRR ILDRWVGFTL
SHILWDAFGK KWLSAGRVQT PVLGWVIKRY EESKEKKGEI LLHVNDFPLK IEIEDLMFAK
EIFKDLELAD ISLSNPQEEE KRPLPPYTTD TVLEDANEKL HLSAHKTMKI LQELFEAGYI
TYHRTDSTRV SDAGKYLVAK PYITKMFGEE YFYPRSWGEG GAHECIRPTR PLEPKDLEFM
ITAGIAEFED PENALKVYEL IFKRFMASQM RPAKVITEEI ILKLPYFEWK ERVVTEVKEH
GFDLMYPTFK VFPKKEKLEI THKEFREVPK VYPYTQGTLI QEMKRRGLGR PSTYAQIVQT
LLERHYVVEE KGFLIPTDLG REVYEYLTKH FPEWTSEELT RKLEEAMDKI ERGELDYMEV
LKEVHRIKVL LKEEKAFKK
