ID D5U2V5_THEAM Unreviewed; 1295 AA.
AC D5U2V5;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Reverse gyrase {ECO:0000256|HAMAP-Rule:MF_01125, ECO:0000256|RuleBase:RU004026};
DE EC=5.6.2.- {ECO:0000256|HAMAP-Rule:MF_01125};
GN Name=rgy {ECO:0000256|HAMAP-Rule:MF_01125};
GN OrderedLocusNames=Tagg_1187 {ECO:0000313|EMBL:ADG91455.1};
OS Thermosphaera aggregans (strain DSM 11486 / M11TL).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermosphaera.
OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG91455.1, ECO:0000313|Proteomes:UP000002376};
RN [1] {ECO:0000313|EMBL:ADG91455.1, ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX PubMed=21304709;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [2] {ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX DOI=10.4056/sigs.821804;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain
RT (M11TLT).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11486;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P.,
RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive
CC supercoils in an ATP-dependent process, increasing the linking number
CC in steps of +1. Binds to single-stranded DNA, transiently cleaves and
CC then rejoins the ends, introducing a positive supercoil in the process.
CC The scissile phosphodiester is attacked by the catalytic tyrosine of
CC the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-
CC enzyme intermediate. Involved in rewinding DNA strands in regions of
CC the chromosome that have opened up to allow replication, transcription,
CC DNA repair and/or for DNA protection. {ECO:0000256|RuleBase:RU004026}.
CC -!- FUNCTION: Modifies the topological state of DNA by introducing positive
CC supercoils in an ATP-dependent process, increasing the linking number
CC in steps of +1. Binds to single-stranded DNA, transiently cleaves and
CC then rejoins the ends, introducing a positive supercoil in the process.
CC The scissile phosphodiester is attacked by the catalytic tyrosine of
CC the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-
CC enzyme intermediate. Probably involved in rewinding DNA strands in
CC regions of the chromosome that have opened up to allow replication,
CC transcription, DNA repair and/or for DNA protection.
CC {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001836, ECO:0000256|HAMAP-
CC Rule:MF_01125, ECO:0000256|RuleBase:RU004026};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01125};
CC Note=Binds 1 or 2 zinc ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01125};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01125}.
CC -!- DOMAIN: Introduction of positive supercoils requires the cooperation of
CC both domains. The helicase-like domain probably does not directly
CC unwind DNA, but more likely acts by driving ATP-dependent
CC conformational changes within the whole enzyme. A beta hairpin in the
CC 'latch' region of the N-terminal domain plays a regulatory role in the
CC enzyme, repressing topoisomerase activity in the absence of ATP and
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:0000256|HAMAP-Rule:MF_01125}.
CC -!- MISCELLANEOUS: This enzyme is the only unique feature of
CC hyperthermophilic bacteria/archaea known and seems to be essential for
CC adaptation to life at high temperatures. It may play a role in
CC stabilization of DNA at high temperatures. {ECO:0000256|HAMAP-
CC Rule:MF_01125}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the type IA
CC topoisomerase family. {ECO:0000256|HAMAP-Rule:MF_01125}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box helicase
CC family. DDVD subfamily. {ECO:0000256|ARBA:ARBA00043976,
CC ECO:0000256|HAMAP-Rule:MF_01125}.
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DR EMBL; CP001939; ADG91455.1; -; Genomic_DNA.
DR RefSeq; WP_013130048.1; NC_014160.1.
DR STRING; 633148.Tagg_1187; -.
DR GeneID; 9166226; -.
DR KEGG; tag:Tagg_1187; -.
DR eggNOG; arCOG01526; Archaea.
DR HOGENOM; CLU_002886_0_0_2; -.
DR OrthoDB; 30963at2157; -.
DR Proteomes; UP000002376; 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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase 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; cd17924; DDXDc_reverse_gyrase; 1.
DR CDD; cd18798; SF2_C_reverse_gyrase; 1.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03361; TOPRIM_TopoIA_RevGyr; 1.
DR Gene3D; 2.60.510.20; -; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR HAMAP; MF_01125; Reverse_gyrase; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 NCBIfam; TIGR01054; rgy; 1.
DR PANTHER; PTHR43505; REVERSE GYRASE; 1.
DR PANTHER; PTHR43505:SF1; REVERSE GYRASE; 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; SM00490; HELICc; 1.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01125}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01125};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01125}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01125};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01125,
KW ECO:0000256|RuleBase:RU004026};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01125}; Reference proteome {ECO:0000313|Proteomes:UP000002376};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01125};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01125};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_01125}.
FT DOMAIN 108..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 664..822
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 660..1295
FT /note="Topoisomerase I"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125"
FT COILED 282..316
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 1016
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01125"
SQ SEQUENCE 1295 AA; 148285 MW; F6467F4158167A41 CRC64;
MSNLLNPYGF YRHACPNCGG EISDHRLFYK APCEKCLSEG DFKKTLKRIR SEGLRDYKSI
IEAYYKDLKN PEGLRQLLDE EVALEDFEEF FERATRGNKL WSAQRTWARR VLKKKSFSII
APTGTGKTVF SLVISLYTVA KSQRGDRRRV YLVFPTLPLL LQAESKVKHF ATNAGLKICE
DRAEESCIRI LVAHGRSDKK SKEELMEQVR NGDFDILLST SAFFHRNFEL LKNKDFALIV
MDDVDAVLKS GKAIRKLLNL VNVTDDAIND GLNLIKLRQR IVFSSGEEKE KLSAEIEELE
KKIARVKSEI KTTLVVNSAT GRPRGIYPKL FKVFLDFEAG SKPEAIRNIV DAYIEADDPE
NALLEIASKL KDGFLVFVPV DRGVEYADKI AELLKAHGLK SESFHAKKKI DVLNDFARGE
LNCLVGVATY YGVMVRGIDL PERVKYVIFL GVPRHKFSTA LEEISPTDLL RIISVLRDIA
PEESKRELES LVGRLSNRLK RISQGALFKL REDFAKRLKG EHVEETVLIK ELLRAYELAR
ELLRDEEIWR KLSNLGDVGL LWENGRQYLL IPDVATYIQA SGRCSRLYPG GITKGLSVII
VDDKRLLNGL NKRLRWIFEG VSIANLRELE LEKLITEIEQ ERVIVGKILR NEYRPEGQVD
LIKSALLIVE SPNKAKTIAN FFGKPSVRVL GKSLQAYEVT IGDYVLSIVA SAGHVYDLVV
DLQENYGVRR VGSRFIPVYT DIKKCVNGHQ FVDETDKCPR CGTSRVVRKA DIVSALKELA
REVDLVLIGT DPDSEGEKIG WDLKVLLEPY AREVRRVEFH EVTRRAILEA IRNPRSFDTR
LVGAQIVRRV EDRWIGFSLS EIVQKYAWTS YCFENLKDKG HDCCRENRNL SAGRVQTPVL
GYIIKRYRDK EDKSLYKYRL LAEKDGEKIS FTIDRAQAVN AGLVSILEKN NKRRKKDKNY
PPLVIKEREL IVEAKNPPPP FSTDALLEEA SKSLGLATTR TMEIAQDLFE MGLITYHRTD
STRISEAGLT VARQYLEERY GDKYRDVFQP RTWGEGGAHE AIRPTRPIDA DRLAELVREG
VIVLTGRLTR QHILVYDLIF RRFIASQMKP AKIGKQVLTV SINGVEAVVE RVVEVVEKGY
LEVYQDVKLE TRITEGEGRI TEVVEVKPPM ARYHDVIRWM KENGIGRPST YAKIIQTLLD
RRYVDVTKKH KALRPTERGI FIYRFLDEKF KEVVSVETTR RLEKDMSDIE EGRVEHMKIL
EKLYNELREK ILDNPIIKEL EDEYSERCGR KSDAA
//
