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Reverse gyrase [Includes: Helicase (EC 3.6.4.12); Topoisomerase (EC 5.99.1.3)]

 F0S2F6_DESTD            Unreviewed;      1182 AA.
F0S2F6;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
27-SEP-2017, entry version 51.
RecName: Full=Reverse gyrase {ECO:0000256|HAMAP-Rule:MF_01125};
Includes:
RecName: Full=Helicase {ECO:0000256|HAMAP-Rule:MF_01125};
EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01125};
Includes:
RecName: Full=Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01125};
EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01125};
Name=rgy {ECO:0000256|HAMAP-Rule:MF_01125};
OrderedLocusNames=Dester_0373 {ECO:0000313|EMBL:ADY73028.1};
Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
Desulfurobacterium.
NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73028.1, ECO:0000313|Proteomes:UP000007102};
[1] {ECO:0000313|Proteomes:UP000007102}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
Brambilla E., Klenk H.-P., Eisen J.A.;
"The complete genome of Desulfurobacterium thermolithotrophum DSM
11699.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Modifies the topological state of DNA by introducing
positive supercoils in an ATP-dependent process. It cleaves
transiently a single DNA strand and remains covalently bound to
the 5' DNA end through a tyrosine residue. May be involved in
rewinding the DNA strands in the regions of the chromosome that
have opened up to allow transcription or replication.
{ECO:0000256|HAMAP-Rule:MF_01125, ECO:0000256|RuleBase:RU004026}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|HAMAP-Rule:MF_01125}.
-!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01125}.
-!- DOMAIN: Both the DNA unwinding and positive supercoiling
activities require the cooperation of both domains. The
cooperative action between the helicase-like and the topoisomerase
domains is specific. The helicase-like domain probably does not
directly unwind DNA but acts more likely by driving ATP-dependent
conformational changes within the whole enzyme, functioning more
like a protein motor. The "latch" region of the N-terminal domain
plays a regulatory role in the enzyme, repressing topoisomerase
activity in the absence of ATP and therefore preventing the enzyme
from acting as an ATP-independent relaxing enzyme; it also helps
to coordinate nucleotide hydrolysis by the ATPase domain with the
supercoiling activity of the topoisomerase domain.
{ECO:0000256|HAMAP-Rule:MF_01125}.
-!- MISCELLANEOUS: This enzyme is the only unique feature of
hyperthermophilic bacteria/archaea discovered so far. It appears
to be essential for adaptation to life at high temperatures.
{ECO:0000256|HAMAP-Rule:MF_01125}.
-!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
type I/III topoisomerase family. {ECO:0000256|HAMAP-
Rule:MF_01125}.
-!- SIMILARITY: In the N-terminal section; belongs to the DEAD box
helicase family. DDVD subfamily. {ECO:0000256|HAMAP-
Rule:MF_01125}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01125}.
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EMBL; CP002543; ADY73028.1; -; Genomic_DNA.
RefSeq; WP_013637986.1; NC_015185.1.
STRING; 868864.Dester_0373; -.
EnsemblBacteria; ADY73028; ADY73028; Dester_0373.
KEGG; dte:Dester_0373; -.
eggNOG; ENOG4106K5Q; Bacteria.
eggNOG; COG1110; LUCA.
KO; K03170; -.
OMA; GVATYYG; -.
OrthoDB; POG091H02BN; -.
Proteomes; UP000007102; Chromosome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
CDD; cd00186; TOP1Ac; 1.
Gene3D; 2.70.20.10; -; 1.
HAMAP; MF_01125; Reverse_gyrase; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005736; Reverse_gyrase.
InterPro; IPR003601; Topo_IA_2.
InterPro; IPR013497; Topo_IA_cen.
InterPro; IPR013825; Topo_IA_cen_sub2.
InterPro; IPR023405; Topo_IA_core_domain.
InterPro; IPR003602; Topo_IA_DNA-bd_dom.
InterPro; IPR006171; TOPRIM_domain.
Pfam; PF00270; DEAD; 1.
Pfam; PF01131; Topoisom_bac; 1.
Pfam; PF01751; Toprim; 1.
PRINTS; PR00417; PRTPISMRASEI.
SMART; SM00487; DEXDc; 1.
SMART; SM00437; TOP1Ac; 1.
SMART; SM00436; TOP1Bc; 1.
SMART; SM00493; TOPRIM; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF56712; SSF56712; 1.
TIGRFAMs; TIGR01054; rgy; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS50880; TOPRIM; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000007102};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Helicase {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Isomerase {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Reference proteome {ECO:0000313|Proteomes:UP000007102};
Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026};
Zinc {ECO:0000256|HAMAP-Rule:MF_01125, ECO:0000256|RuleBase:RU004026};
Zinc-finger {ECO:0000256|HAMAP-Rule:MF_01125,
ECO:0000256|RuleBase:RU004026}.
DOMAIN 88 289 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 611 766 Toprim. {ECO:0000259|PROSITE:PS50880}.
ZN_FING 10 31 C4-type 1. {ECO:0000256|HAMAP-
Rule:MF_01125}.
NP_BIND 101 108 ATP. {ECO:0000256|HAMAP-Rule:MF_01125}.
REGION 617 1182 Topoisomerase I. {ECO:0000256|HAMAP-
Rule:MF_01125}.
COILED 1145 1172 {ECO:0000256|SAM:Coils}.
ACT_SITE 923 923 For DNA cleavage activity.
{ECO:0000256|HAMAP-Rule:MF_01125}.
BINDING 84 84 ATP. {ECO:0000256|HAMAP-Rule:MF_01125}.
SEQUENCE 1182 AA; 135432 MW; CCDC4798222C6739 CRC64;
MKLAEFHRMC PNCGGIISDE RLKAGLPCEK CLPKELFYTN RKEICNALGN KLQDFKKICL
LDEFTENYVK FFKEKTGFTP WTLQVMWARR VALSKSFTMI APTGVGKTTW GLVTSAYLSG
KVYILVPTKL LVLQTVEKLS KLTNKKIVAY TGKKSEKGTI QSGNFEILVT TTNFLYRNFE
IIPKPFDFVF VDDVDSLLKS AKNVDKVIRL LGFTEEDISI AEKVLELKSL VAKFGEKVDR
KLIEKLKKLE NFLEKRKSEI KNVLVVSSAT SQPKSKRVKL FRELLGFEVG KSATALRNVE
DVLIYTDKDY LEETVKIIKK YGKGVFVFIS EDLGKDYVEE VVNFLNKKGI STVSYENFSS
ENQGNFIDGK IQAVVGIASY RNPLARGIDL PQAVRYAVFL GVPKLEFNLK LSLAPVKLFG
ILLVLRELIE DKTKVMSYLS YLKKYLSLKK ELLDKYPKVK EKLEEIKGFL ESYLSNKEFL
EKVRASEDIS LKEKNGELFV VVGDATGYVQ ASGRTSRMFA GGLTKGVSLM LVDDLKALNS
LKKRLSIFLE DLNFKVLDYD KGKELAEKFG FELIDEEKLN KIFKTVDEDR KRVKEILEGK
IKAETKNLVN TALIVVESPN KARTIANFFG KPVRRKVLDI DVYEINIGDR LLLLTASKGH
VFDLTVRDGL WGVKEEESSY IPVYDTIKYC TKCFEQTTEP FCSKCSGKPD VDKITVVRAL
REVGLEIDEV YIASDPDTEG EKIGWDIGTV IKPFQKKVRR MEFHEVTKWA FMEALKTPKE
IDENLVKAQI VRRIADRWVG FALSQHLWKV FKKHWLSAGR VQTPVLGWVI KRYEESKEKK
GIIVVETKAG SFRFEFDNLE EFQKIAIDKV EIKVKEKSIF EKNSLPPFNT GELLKEASNN
LGISAEETMN IAQALFESGF ITYHRTDSTR VSTAGMGVAK EYISQKFGAE FIKLRSWGDG
GAHECIRPTR PLDAESLKAL VLVSGSSSKM TKNHFRIYDL IFKRFMASQM IPTKVEKCKL
LVKLLPVEKE EEEERIAKIV KNGWNLIQPL NLEPLSVELK KEKTYYFEII SYVKKKVPKV
FPYTQGELIE EMRKKEIGRP STYAKIVQTL LDRKYIIEKG KFLYPTKLGI EVYNYLSEKF
PDYTSEEFTR ELENIMDKVE RGEEDYQKVI ENLKPILEIR YS


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