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Database: UniProt
Entry: D5EIV8_CORAD
LinkDB: D5EIV8_CORAD
Original site: D5EIV8_CORAD 
ID   D5EIV8_CORAD            Unreviewed;       616 AA.
AC   D5EIV8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   OrderedLocusNames=Caka_1337 {ECO:0000313|EMBL:ADE54357.1};
OS   Coraliomargarita akajimensis (strain DSM 45221 / IAM 15411 / JCM 23193 /
OS   KCTC 12865 / 04OKA010-24).
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC   Coraliomargaritaceae; Coraliomargarita.
OX   NCBI_TaxID=583355 {ECO:0000313|EMBL:ADE54357.1, ECO:0000313|Proteomes:UP000000925};
RN   [1] {ECO:0000313|EMBL:ADE54357.1, ECO:0000313|Proteomes:UP000000925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45221 / IAM 15411 / JCM 23193 / KCTC 12865
RC   {ECO:0000313|Proteomes:UP000000925};
RX   PubMed=21304713; DOI=10.4056/sigs.952166;
RA   Mavromatis K., Abt B., Brambilla E., Lapidus A., Copeland A., Deshpande S.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Han C., Detter J.C., Woyke T.,
RA   Goodwin L., Pitluck S., Held B., Brettin T., Tapia R., Ivanova N.,
RA   Mikhailova N., Pati A., Liolios K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Coraliomargarita akajimensis type strain
RT   (04OKA010-24).";
RL   Stand. Genomic Sci. 2:290-299(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; CP001998; ADE54357.1; -; Genomic_DNA.
DR   RefSeq; WP_013043079.1; NC_014008.1.
DR   AlphaFoldDB; D5EIV8; -.
DR   STRING; 583355.Caka_1337; -.
DR   KEGG; caa:Caka_1337; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_1_1_0; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000000925; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   CDD; cd01030; TOPRIM_TopoIIA_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ADE54357.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000925}.
FT   DOMAIN          404..510
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   COILED          349..376
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   616 AA;  69535 MW;  B94296269280F35A CRC64;
     MSANYTEDSI KSLDWKEHIR LRPGMYIGKL GDGSSQDDGI YILLKEVIDN SIDEFVMGHG
     KIIEVNIDGT HVSVRDYGRG IPLGKLKDCA SKINTGAKYD SEAFKKSVGL NGVGIKAVNA
     LSKEFEIQAY REGKTRCVAF AQGEVTTEDK RDKAADADNG TALRFDPDPD IFGKCRFRED
     YVEDMLWNYA YLNSGLTIVY NGKKFKSDKG LHDLLENKLD GDPLYPIIHL KDKDVEIAFT
     HASGYGEDYY SFVNGQHTTM GGTHLAAFRE ALAKTVKDFY KKDFDAVDIR TSICAAVSVK
     VEEPVFESQT KTKLGSLEMG PKGPTVRTFM NNFIKQALDN YLHRSPETAK ELLSKIQESE
     RNRKELKGIQ KLARERAKKA KIHNKKLRDC RIHLDTKKEG RLDSTLFITE GDSASGSITK
     ARDVNTQAVF SLKGKPLNSF GLTKKVVYEN EEFNLLQDAL NIEDGLDGLR YNNVVIATDA
     DVDGMHIRLL LITFFLQFFP ELIRQGHLHI LQTPLFRVRN KKVTRYCYSD EERLAAIEEC
     KPKPEITRFK GLGEISPDEF SNFIGKNIRL DPVIIPKGMT TKDLLTFYMG KNTPERQEFI
     IENLRIEKDA AEPVSA
//
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